Visual phototransduction (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Visual phototransduction" Data-Source="Reactome - http://www.reactome.org" Version="release 46" Author="Jassal, B" Maintainer="Jassal, B" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">Visual phototransduction is the process by which photon absorption by visual pigment molecules in photoreceptor cells is converted to an electrical cellular response. The events in this process are photochemical, biochemical and electrophysiological and are highly conserved across many species. This process occurs in two types of photoreceptors in the retina, rods and cones. Each type consists of two parts, the outer segment which detects a photon signal and the inner segment which contains the necessary machinery for cell metabolism. Each type of cell functions differently. Rods are very light sensitive but their flash response is slow so they work best in twilight conditions but are not good at detecting objects moving quickly. Cones are less light-sensitive and have a fast flash response so they work best in daylight conditions and are better at detecting fast moving objects than rods.&lt;br&gt;&lt;br&gt;The visual pigment consists of a chromophore (11-cis-retinal, 11cRAL, A1) covalently attached to a GPCR opsin family member. The linkage is via a Schiff base forming retinylidene protein. Upon photon absorption, 11cRAL isomerises to all-trans retinal (atRAL), changing the conformation of opsin to an activated form which can activate the regulatory G protein transducin (Gt). The alpha subunit of Gt activates phosphodiesterase which hydrolyses cGMP to 5'-GMP. As high level of cGMP keep cGMP-gated sodium channels open, the lowering of cGMP levels closes these channels which causes hyperpolarization of the cell and subsequently, closure of voltage-gated calcium channels. As calcium levels drop, the level of the neurotransmitter glutamate also drops causing depolarization of the cell. This effectively relays the light signal to postsynaptic neurons as electrical signal (Burns &amp; Pugh 2010, Korenbrot 2012, Pugh &amp; Lamb 1993).&lt;br&gt;&lt;br&gt;11cRAL cannot be synthesised in vertebrates. Vitamin A from many dietary sources is the precursor for 11cRAL. It is taken from food in the form of esters such as retinyl acetate or palmitate or one of four caretenoids (alpha-carotene, beta-carotene, gamma-carotene and beta-cryptoxanthin). Retinoids are transported from the gut to be stored in liver, until required by target organs such as the eye (Harrison &amp; Hussain 2001, Harrison 2005). In the eye, in the form 11cRAL, it is used in the retinoid (visual) cycle to initiate phototransduction and for visual pigment regeneration to ready the photoreceptor for the next phototransduction event (von Lintig 2012, Blomhoff &amp; Blomhoff 2006, von Lintig et al. 2010, D'Ambrosio et al. 2011, Wang &amp; Kefalov 2011, Kefalov 2012, Wolf 2004). 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<Xref Database="Uniprot-TrEMBL" ID="P02647" /> </DataNode> <DataNode TextLabel="APOA4 " GraphId="c80df" Type="Protein" GroupRef="a047d"> <Graphics CenterX="1200.0" CenterY="1510.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P06727" /> </DataNode> <DataNode TextLabel="APOA2" GraphId="f78d6" Type="Protein" GroupRef="a047d"> <Graphics CenterX="1200.0" CenterY="1530.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02652" /> </DataNode> <DataNode TextLabel="APOC2 " GraphId="bc25a" Type="Protein" GroupRef="a047d"> <Graphics CenterX="1200.0" CenterY="1550.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02655" /> </DataNode> <DataNode TextLabel="APOC3 " GraphId="b49cd" Type="Protein" GroupRef="a047d"> <Graphics CenterX="1200.0" CenterY="1570.0" Width="80.0" Height="20.0" ZOrder="32768" 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CenterY="3070.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16113" /> </DataNode> <DataNode TextLabel="TAGs " GraphId="c421b" Type="Metabolite" GroupRef="bca72"> <Graphics CenterX="1640.0" CenterY="3090.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17855" /> </DataNode> <DataNode TextLabel="APOA4 " GraphId="ad95b" Type="Protein" GroupRef="bca72"> <Graphics CenterX="1640.0" CenterY="3110.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P06727" /> </DataNode> <DataNode TextLabel="APOC2 " GraphId="b8480" Type="Protein" GroupRef="bca72"> <Graphics CenterX="1640.0" CenterY="3130.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02655" /> </DataNode> <DataNode TextLabel="APOC3 " GraphId="b399e" Type="Protein" GroupRef="bca72"> <Graphics CenterX="1640.0" CenterY="3150.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02656" /> </DataNode> <DataNode TextLabel="APOB" GraphId="bf8da" Type="Protein" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3190.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P04114" /> </DataNode> <DataNode TextLabel="PL " GraphId="c6110" Type="Metabolite" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3210.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16247" /> </DataNode> <DataNode TextLabel="APOA1" GraphId="e0985" Type="Protein" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3230.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02647" /> </DataNode> <DataNode TextLabel="APOA2" GraphId="c254c" Type="Protein" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3250.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02652" /> </DataNode> <DataNode TextLabel="atR-LINA " GraphId="e250e" Type="Metabolite" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3290.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:70762" /> </DataNode> <DataNode TextLabel="atR-OLEA " GraphId="cf2ec" Type="Metabolite" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3310.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:70760" /> </DataNode> <DataNode TextLabel="atR-PALM " GraphId="d8115" Type="Metabolite" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3330.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17616" /> </DataNode> <DataNode TextLabel="atR-STEA " GraphId="fc225" Type="Metabolite" GroupRef="c88f8"> <Graphics CenterX="1640.0" CenterY="3350.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:70761" /> </DataNode> <DataNode TextLabel="LRPs" GraphId="bd158" Type="Protein"> <Graphics CenterX="299.0" CenterY="847.0" Width="36.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161047" /> </DataNode> <DataNode TextLabel="CR" GraphId="d87b8" Type="Complex"> <Graphics CenterX="280.5" CenterY="1096.0" Width="25.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161439" /> </DataNode> <DataNode TextLabel="APOE " GraphId="b6c2a" Type="Protein" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02649" /> </DataNode> <DataNode TextLabel="CHEST " GraphId="dc9c7" Type="Metabolite" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17002" /> </DataNode> <DataNode TextLabel="CHOL " GraphId="e1353" Type="Metabolite" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1450.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16113" /> </DataNode> <DataNode TextLabel="TAGs " GraphId="f3f4a" Type="Metabolite" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1470.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17855" /> </DataNode> <DataNode TextLabel="APOA4 " GraphId="d0e94" Type="Protein" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1490.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P06727" /> </DataNode> <DataNode TextLabel="APOC2 " GraphId="c4235" Type="Protein" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1510.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02655" /> </DataNode> <DataNode TextLabel="APOC3 " GraphId="a136b" Type="Protein" GroupRef="afd37"> <Graphics CenterX="1750.0" CenterY="1530.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02656" /> </DataNode> <DataNode TextLabel="APOB" GraphId="b608b" Type="Protein" GroupRef="e1f73"> <Graphics CenterX="1750.0" CenterY="1570.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P04114" /> </DataNode> <DataNode TextLabel="PL " GraphId="f74cf" Type="Metabolite" GroupRef="e1f73"> <Graphics CenterX="1750.0" CenterY="1590.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16247" /> </DataNode> <DataNode TextLabel="APOA1" GraphId="e0ace" Type="Protein" GroupRef="e1f73"> <Graphics CenterX="1750.0" CenterY="1610.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02647" /> </DataNode> <DataNode TextLabel="APOA2" GraphId="de8f6" Type="Protein" GroupRef="e1f73"> <Graphics CenterX="1750.0" CenterY="1630.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02652" /> </DataNode> <DataNode TextLabel="H+" GraphId="a624c" Type="Metabolite"> <Graphics CenterX="279.0" CenterY="1038.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="RBP1" GraphId="f3c93" Type="Protein"> <Graphics CenterX="553.5" CenterY="1038.0" Width="39.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P09455" /> </DataNode> <DataNode TextLabel="RBP1&#xA;atROL" GraphId="d2553" Type="Complex"> <Graphics CenterX="628.5" CenterY="1070.0" Width="77.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160558" /> </DataNode> <DataNode TextLabel="RBP1 " GraphId="a1f8a" Type="Protein" GroupRef="de0f2"> <Graphics CenterX="1860.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P09455" /> </DataNode> <DataNode TextLabel="atROL " GraphId="d9562" Type="Metabolite" GroupRef="de0f2"> <Graphics CenterX="1860.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="LRAT" GraphId="d590c" Type="Protein"> <Graphics CenterX="666.5" CenterY="930.0" Width="39.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O95237" /> </DataNode> <DataNode TextLabel="RBP4&#xA;atROL" GraphId="ba1c1" Type="Complex"> <Graphics CenterX="949.5" CenterY="1131.0" Width="77.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160786" /> </DataNode> <DataNode TextLabel="atROL " GraphId="daf7a" Type="Metabolite" GroupRef="a67c8"> <Graphics CenterX="1970.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="RBP4" GraphId="e0491" Type="Protein" GroupRef="a67c8"> <Graphics CenterX="1970.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02753" /> </DataNode> <DataNode TextLabel="TTR&#xA;RBP4&#xA;atROL" GraphId="b4f1c" Type="Complex"> <Graphics CenterX="948.5" CenterY="997.0" Width="105.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161464" /> </DataNode> <DataNode TextLabel="atROL " GraphId="c5637" Type="Metabolite" GroupRef="f53d2"> <Graphics CenterX="2080.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="RBP4" GraphId="e63ce" Type="Protein" GroupRef="f53d2"> <Graphics CenterX="2080.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02753" /> </DataNode> <DataNode TextLabel="TTR " GraphId="a553c" Type="Protein" GroupRef="fa9f7"> <Graphics CenterX="2080.0" CenterY="1470.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02766" /> </DataNode> <DataNode TextLabel="REH" GraphId="adccd"> <Graphics CenterX="757.5" CenterY="1151.0" Width="33.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160374" /> </DataNode> <DataNode TextLabel="RBP1" GraphId="df1e8" Type="Protein"> <Graphics CenterX="748.5" CenterY="948.0" Width="39.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P09455" /> </DataNode> <DataNode TextLabel="H2O" GraphId="d0c1e" Type="Metabolite"> <Graphics CenterX="269.5" CenterY="967.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="APOE" GraphId="c0d18" Type="Protein"> <Graphics CenterX="193.0" CenterY="1101.0" Width="38.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02649" /> </DataNode> <DataNode TextLabel="STRA6" GraphId="ad432" Type="Protein"> <Graphics CenterX="935.5" CenterY="897.0" Width="47.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BX79" /> </DataNode> <DataNode TextLabel="TTR&#xA;RBP4&#xA;atROL&#xA;STRA6" GraphId="c8e6f" Type="Complex"> <Graphics CenterX="1089.5" CenterY="896.0" Width="109.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161016" /> </DataNode> <DataNode TextLabel="atROL " GraphId="c77cf" Type="Metabolite" GroupRef="ea5b7"> <Graphics CenterX="2190.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="RBP4" GraphId="bbb15" Type="Protein" GroupRef="ea5b7"> <Graphics CenterX="2190.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02753" /> </DataNode> <DataNode TextLabel="TTR " GraphId="a6ff7" Type="Protein" GroupRef="a5a59"> <Graphics CenterX="2190.0" CenterY="1470.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02766" /> </DataNode> <DataNode TextLabel="STRA6 " GraphId="bd7ee" Type="Protein" GroupRef="a5a59"> <Graphics CenterX="2190.0" CenterY="1490.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BX79" /> </DataNode> <DataNode TextLabel="TTR&#xA;RBP4&#xA;STRA6" GraphId="fc98a" Type="Complex"> <Graphics CenterX="1290.5" CenterY="896.0" Width="109.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160434" /> </DataNode> <DataNode TextLabel="RBP4" GraphId="c0182" Type="Protein" GroupRef="fb3ea"> <Graphics CenterX="2300.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02753" /> </DataNode> <DataNode TextLabel="TTR " GraphId="cb1b8" Type="Protein" GroupRef="e34ac"> <Graphics CenterX="2300.0" CenterY="1450.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P02766" /> </DataNode> <DataNode TextLabel="STRA6 " GraphId="cf635" Type="Protein" GroupRef="e34ac"> <Graphics CenterX="2300.0" CenterY="1470.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BX79" /> </DataNode> <DataNode TextLabel="RBP1" GraphId="ebbca" Type="Protein"> <Graphics CenterX="1138.5" CenterY="793.0" Width="39.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P09455" /> </DataNode> <DataNode TextLabel="LRAT" GraphId="e39f1" Type="Protein"> <Graphics CenterX="1095.5" CenterY="723.0" Width="39.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O95237" /> </DataNode> <DataNode TextLabel="11cROL" GraphId="bc5c5" Type="Metabolite"> <Graphics CenterX="1149.0" CenterY="446.0" Width="62.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16302" /> </DataNode> <DataNode TextLabel="RPE65" GraphId="cd6e1" Type="Protein"> <BiopaxRef>dd5</BiopaxRef> <Graphics CenterX="929.5" CenterY="541.0" Width="47.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q16518" /> </DataNode> <DataNode TextLabel="MYO7A" GraphId="c544c" Type="Protein"> <Graphics CenterX="1132.5" CenterY="541.0" Width="51.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13402" /> </DataNode> <DataNode TextLabel="H+" GraphId="a737c" Type="Metabolite"> <Graphics CenterX="996.0" CenterY="486.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="RLBP1&#xA;11cROL" GraphId="f36db" Type="Complex"> <Graphics CenterX="1305.0" CenterY="443.0" Width="94.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160715" /> </DataNode> <DataNode TextLabel="11cROL " GraphId="ba4f0" Type="Metabolite" GroupRef="b811e"> <Graphics CenterX="2410.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16302" /> </DataNode> <DataNode TextLabel="RLBP1 " GraphId="cb633" Type="Protein" GroupRef="b811e"> <Graphics CenterX="2410.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="RLBP1&#xA;11cRAL" GraphId="ad7c1" Type="Complex"> <Graphics CenterX="1595.5" CenterY="443.0" Width="93.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161180" /> </DataNode> <DataNode TextLabel="11cRAL " GraphId="d92be" Type="Metabolite" GroupRef="e05ea"> <Graphics CenterX="2520.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16066" /> </DataNode> <DataNode TextLabel="RLBP1 " GraphId="a3269" Type="Protein" GroupRef="e05ea"> <BiopaxRef>dd4</BiopaxRef> <Graphics CenterX="2520.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="RDH10/11" GraphId="e6bba" Type="Protein"> <Graphics CenterX="1420.5" CenterY="475.0" Width="73.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160646" /> </DataNode> <DataNode TextLabel="H+" GraphId="cde7f" Type="Metabolite"> <Graphics CenterX="1483.0" CenterY="403.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="NADPH" GraphId="aee5f" Type="Metabolite"> <Graphics CenterX="1542.5" CenterY="407.0" Width="59.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16474" /> </DataNode> <DataNode TextLabel="NADP+" GraphId="eddb5" Type="Metabolite"> <Graphics CenterX="1293.0" CenterY="400.0" Width="60.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18009" /> </DataNode> <DataNode TextLabel="NAD+" GraphId="b887b" Type="Metabolite"> <Graphics CenterX="1299.5" CenterY="596.0" Width="53.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15846" /> </DataNode> <DataNode TextLabel="NADH" GraphId="efe8b" Type="Metabolite"> <Graphics CenterX="1611.0" CenterY="548.0" Width="52.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16908" /> </DataNode> <DataNode TextLabel="RDH5" GraphId="f2d7b" Type="Protein"> <Graphics CenterX="1429.5" CenterY="535.0" Width="43.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q92781" /> </DataNode> <DataNode TextLabel="H+" GraphId="e13bf" Type="Metabolite"> <Graphics CenterX="1590.0" CenterY="601.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="11cRAL" GraphId="fcea9" Type="Metabolite"> <Graphics CenterX="1796.5" CenterY="314.0" Width="61.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16066" /> </DataNode> <DataNode TextLabel="RHO" GraphId="b8a3e" Type="Protein"> <Graphics CenterX="1800.5" CenterY="387.0" Width="35.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P08100" /> </DataNode> <DataNode TextLabel="RHO&#xA;11cRAL" GraphId="e4d1e" Type="Complex"> <Graphics CenterX="1960.5" CenterY="387.0" Width="83.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160981" /> </DataNode> <DataNode TextLabel="RHO " GraphId="af0d7" Type="Protein" GroupRef="f6875"> <Graphics CenterX="2630.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P08100" /> </DataNode> <DataNode TextLabel="11cRAL " GraphId="da5a6" Type="Metabolite" GroupRef="f6875"> <Graphics CenterX="2630.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16066" /> </DataNode> <DataNode TextLabel="MII" GraphId="b5aa2" Type="Complex"> <Graphics CenterX="2089.5" CenterY="387.0" Width="25.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161020" /> </DataNode> <DataNode TextLabel="atRAL " GraphId="d82ea" Type="Metabolite" GroupRef="ae647"> <Graphics CenterX="2740.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17898" /> </DataNode> <DataNode TextLabel="RHO " GraphId="a5931" Type="Protein" GroupRef="ae647"> <Graphics CenterX="2740.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P08100" /> </DataNode> <DataNode TextLabel="Photon" GraphId="d9f9b"> <Graphics CenterX="2039.0" CenterY="119.0" Width="48.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_18935" /> </DataNode> <DataNode TextLabel="atRAL" GraphId="c87d1" Type="Metabolite"> <Graphics CenterX="2421.0" CenterY="504.0" Width="50.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17898" /> </DataNode> <DataNode TextLabel="ATP" GraphId="ed58c" Type="Metabolite"> <Graphics CenterX="2424.0" CenterY="559.0" Width="40.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15422" /> </DataNode> <DataNode TextLabel="H2O" GraphId="bf393" Type="Metabolite"> <Graphics CenterX="2427.5" CenterY="596.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="ADP" GraphId="a2369" Type="Metabolite"> <Graphics CenterX="2351.5" CenterY="661.0" Width="41.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16761" /> </DataNode> <DataNode TextLabel="Pi" GraphId="b7f6b" Type="Metabolite"> <Graphics CenterX="2398.5" CenterY="672.0" Width="27.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18367" /> </DataNode> <DataNode TextLabel="ABCA4" GraphId="d839d" Type="Protein"> <Graphics CenterX="2356.0" CenterY="502.0" Width="48.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P78363" /> </DataNode> <DataNode TextLabel="atRAL" GraphId="b4cb7" Type="Metabolite"> <Graphics CenterX="2483.0" CenterY="682.0" Width="50.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17898" /> </DataNode> <DataNode TextLabel="RDH12" GraphId="c23c8" Type="Protein"> <Graphics CenterX="2900.5" CenterY="936.0" Width="51.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96NR8" /> </DataNode> <DataNode TextLabel="H+" GraphId="c8002" Type="Metabolite"> <Graphics CenterX="2572.0" CenterY="810.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="NADPH" GraphId="bba04" Type="Metabolite"> <Graphics CenterX="2547.5" CenterY="765.0" Width="59.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16474" /> </DataNode> <DataNode TextLabel="NADP+" GraphId="c45b9" Type="Metabolite"> <Graphics CenterX="2576.0" CenterY="860.0" Width="60.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18009" /> </DataNode> <DataNode TextLabel="RLBP1&#xA;atROL" GraphId="ae947" Type="Complex"> <Graphics CenterX="1387.5" CenterY="997.0" Width="83.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161152" /> </DataNode> <DataNode TextLabel="atROL " GraphId="c86e2" Type="Metabolite" GroupRef="bab85"> <Graphics CenterX="2850.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="RLBP1 " GraphId="e5b12" Type="Protein" GroupRef="bab85"> <BiopaxRef>dd4</BiopaxRef> <Graphics CenterX="2850.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="atROL isomerase" GraphId="f3799"> <Graphics CenterX="1302.0" CenterY="1049.0" Width="106.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160708" /> </DataNode> <DataNode TextLabel="RLBP1&#xA;11cROL" GraphId="dc72e" Type="Complex"> <Graphics CenterX="1178.0" CenterY="1078.0" Width="94.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160715" /> </DataNode> <DataNode TextLabel="11cROL " GraphId="bd920" Type="Metabolite" GroupRef="ecf7c"> <Graphics CenterX="2960.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16302" /> </DataNode> <DataNode TextLabel="RLBP1 " GraphId="a6d9e" Type="Protein" GroupRef="ecf7c"> <Graphics CenterX="2960.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="11cRPALM" GraphId="c6d5b" Type="Metabolite"> <Graphics CenterX="1261.0" CenterY="1241.0" Width="78.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16254" /> </DataNode> <DataNode TextLabel="H2O" GraphId="f6f88" Type="Metabolite"> <Graphics CenterX="1264.5" CenterY="1286.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="REH" GraphId="a4802"> <Graphics CenterX="1357.5" CenterY="1344.0" Width="33.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161495" /> </DataNode> <DataNode TextLabel="PALM" GraphId="bdc58" Type="Metabolite"> <Graphics CenterX="1441.0" CenterY="1215.0" Width="48.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15756" /> </DataNode> <DataNode TextLabel="H+" GraphId="b293e" Type="Metabolite"> <Graphics CenterX="1449.0" CenterY="1316.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="RLBP1&#xA;11cROL" GraphId="b0e6b" Type="Complex"> <Graphics CenterX="1858.0" CenterY="1293.0" Width="94.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160715" /> </DataNode> <DataNode TextLabel="11cROL " GraphId="f27b8" Type="Metabolite" GroupRef="b276a"> <Graphics CenterX="3070.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16302" /> </DataNode> <DataNode TextLabel="RLBP1 " GraphId="fde6d" Type="Protein" GroupRef="b276a"> <Graphics CenterX="3070.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="RLBP1" GraphId="a6071" Type="Protein"> <BiopaxRef>dd4</BiopaxRef> <Graphics CenterX="1731.5" CenterY="1266.0" Width="45.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="11cRDH" GraphId="e4240"> <Graphics CenterX="1938.5" CenterY="1247.0" Width="57.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160753" /> </DataNode> <DataNode TextLabel="RLBP1&#xA;11cRAL" GraphId="c6bc6" Type="Complex"> <Graphics CenterX="2072.5" CenterY="1294.0" Width="93.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161180" /> </DataNode> <DataNode TextLabel="11cRAL " GraphId="ab429" Type="Metabolite" GroupRef="c1668"> <Graphics CenterX="3180.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16066" /> </DataNode> <DataNode TextLabel="RLBP1 " GraphId="f830d" Type="Protein" GroupRef="c1668"> <BiopaxRef>dd4</BiopaxRef> <Graphics CenterX="3180.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12271" /> </DataNode> <DataNode TextLabel="NADP+" GraphId="a1b31" Type="Metabolite"> <Graphics CenterX="1874.0" CenterY="1330.0" Width="60.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18009" /> </DataNode> <DataNode TextLabel="NADPH" GraphId="b4b6b" Type="Metabolite"> <Graphics CenterX="2015.5" CenterY="1264.0" Width="59.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16474" /> </DataNode> <DataNode TextLabel="H+" GraphId="cfa7c" Type="Metabolite"> <Graphics CenterX="2012.0" CenterY="1319.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="Cone apo-opsins" GraphId="c2088" Type="Protein"> <Graphics CenterX="2111.0" CenterY="1349.0" Width="108.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160347" /> </DataNode> <DataNode TextLabel="Cone opsins&#xA;11cRAL" GraphId="f8bfd" Type="Complex"> <Graphics CenterX="2234.5" CenterY="1351.0" Width="127.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161031" /> </DataNode> <DataNode TextLabel="OPN1LW " GraphId="ebf6f" Type="Protein" GroupRef="e830f"> <Graphics CenterX="3290.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P04000" /> </DataNode> <DataNode TextLabel="11cRAL " GraphId="c5c8a" Type="Metabolite" GroupRef="e830f"> <Graphics CenterX="3290.0" CenterY="1450.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16066" /> </DataNode> <DataNode TextLabel="OPN1MW " GraphId="a4d3c" Type="Protein" GroupRef="a13b4"> <Graphics CenterX="3290.0" CenterY="1490.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P04001" /> </DataNode> <DataNode TextLabel="OPN1SW " GraphId="a4e60" Type="Protein" GroupRef="ab1f9"> <Graphics CenterX="3290.0" CenterY="1530.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P03999" /> </DataNode> <DataNode TextLabel="Cone opsins&#xA;atRAL" GraphId="c3224" Type="Complex"> <Graphics CenterX="2317.0" CenterY="1279.0" Width="116.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_161282" /> </DataNode> <DataNode TextLabel="OPN1LW " GraphId="e70b0" Type="Protein" GroupRef="dfa1b"> <Graphics CenterX="3400.0" CenterY="1430.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P04000" /> </DataNode> <DataNode TextLabel="atRAL " GraphId="ffa33" Type="Metabolite" GroupRef="dfa1b"> <Graphics CenterX="3400.0" CenterY="1450.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17898" /> </DataNode> <DataNode TextLabel="OPN1MW " GraphId="c6886" Type="Protein" GroupRef="b747a"> <Graphics CenterX="3400.0" CenterY="1490.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P04001" /> </DataNode> <DataNode TextLabel="OPN1SW " GraphId="b9028" Type="Protein" GroupRef="f0eaf"> <Graphics CenterX="3400.0" CenterY="1530.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P03999" /> </DataNode> <DataNode TextLabel="Photon" GraphId="ec1c7"> <Graphics CenterX="2387.0" CenterY="1327.0" Width="48.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_18935" /> </DataNode> <DataNode TextLabel="H2O" GraphId="c7b4c" Type="Metabolite"> <Graphics CenterX="2231.5" CenterY="1280.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="atRAL" GraphId="d3ffc" Type="Metabolite"> <Graphics CenterX="2258.0" CenterY="1143.0" Width="50.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17898" /> </DataNode> <DataNode TextLabel="NADP+" GraphId="c5a60" Type="Metabolite"> <Graphics CenterX="2040.0" CenterY="1178.0" Width="60.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18009" /> </DataNode> <DataNode TextLabel="NADPH" GraphId="f643a" Type="Metabolite"> <Graphics CenterX="2205.5" CenterY="1170.0" Width="59.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16474" /> </DataNode> <DataNode TextLabel="H+" GraphId="c6d0d" Type="Metabolite"> <Graphics CenterX="2201.0" CenterY="1110.0" Width="36.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15378" /> </DataNode> <DataNode TextLabel="NRPE" GraphId="c8252" Type="Metabolite"> <Graphics CenterX="2205.0" CenterY="933.0" Width="48.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:71063" /> </DataNode> <DataNode TextLabel="NRPE" GraphId="bc88a" Type="Metabolite"> <Graphics CenterX="2433.0" CenterY="816.0" Width="48.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:71063" /> </DataNode> <DataNode TextLabel="A2PE" GraphId="b8183" Type="Metabolite"> <Graphics CenterX="1923.5" CenterY="934.0" Width="47.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:52592" /> </DataNode> <DataNode TextLabel="H2O" GraphId="a1a99" Type="Metabolite"> <Graphics CenterX="1912.5" CenterY="854.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="ABCA4" GraphId="f553a" Type="Protein"> <Graphics CenterX="2354.0" CenterY="781.0" Width="48.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P78363" /> </DataNode> <DataNode TextLabel="atRAL" GraphId="f37e3" Type="Metabolite"> <Graphics CenterX="2170.0" CenterY="784.0" Width="50.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17898" /> </DataNode> <DataNode TextLabel="Pi" GraphId="ece0f" Type="Metabolite"> <Graphics CenterX="2455.5" CenterY="901.0" Width="27.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:18367" /> </DataNode> <DataNode TextLabel="ADP" GraphId="f10fc" Type="Metabolite"> <Graphics CenterX="2460.5" CenterY="863.0" Width="41.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16761" /> </DataNode> <DataNode TextLabel="ATP" GraphId="f1ea7" Type="Metabolite"> <Graphics CenterX="2296.0" CenterY="853.0" Width="40.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15422" /> </DataNode> <DataNode TextLabel="H2O" GraphId="ef808" Type="Metabolite"> <Graphics CenterX="2266.5" CenterY="883.0" Width="43.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15377" /> </DataNode> <DataNode TextLabel="NAPEPLD" GraphId="d11de" Type="Protein"> <Graphics CenterX="1854.0" CenterY="932.0" Width="62.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q6IQ20" /> </DataNode> <DataNode TextLabel="A2E" GraphId="bcca3" Type="Metabolite"> <Graphics CenterX="1809.0" CenterY="995.0" Width="40.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:71980" /> </DataNode> <DataNode TextLabel="A2E" GraphId="cb96a" Type="Metabolite"> <Graphics CenterX="1580.0" CenterY="862.0" Width="40.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:71980" /> </DataNode> <DataNode TextLabel="NREH" GraphId="b7744"> <Graphics CenterX="272.0" CenterY="998.0" Width="42.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_160866" /> </DataNode> <DataNode TextLabel="atROL" GraphId="bcf69" Type="Metabolite"> <Graphics CenterX="412.5" CenterY="1081.0" Width="51.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="atROL" GraphId="fa378" Type="Metabolite"> <Graphics CenterX="561.5" CenterY="1109.0" Width="51.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17336" /> </DataNode> <DataNode TextLabel="11cROL" GraphId="d4063" Type="Metabolite"> <Graphics CenterX="1724.0" CenterY="1328.0" Width="62.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" 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GroupRef="b8b06"> <Graphics CenterX="3840.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:15996" /> </DataNode> <DataNode TextLabel="N-" GraphId="f9dab" Type="Protein" GroupRef="b8b06"> <Graphics CenterX="3840.0" CenterY="1450.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P11488" /> </DataNode> <DataNode TextLabel="N-" GraphId="f857e" Type="Protein" GroupRef="b8b06"> <Graphics CenterX="3840.0" CenterY="1470.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P11488" /> </DataNode> <DataNode TextLabel="N-" GraphId="b719c" Type="Protein" GroupRef="b8b06"> <Graphics CenterX="3840.0" CenterY="1490.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P11488" /> </DataNode> <DataNode TextLabel="N-" 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<DataNode TextLabel="PDE6A" GraphId="ded8f" Type="Protein" GroupRef="c9ae2"> <BiopaxRef>a8e</BiopaxRef> <Graphics CenterX="4060.0" CenterY="1570.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P16499" /> </DataNode> <DataNode TextLabel="PDE6B" GraphId="c211a" Type="Protein" GroupRef="c9ae2"> <BiopaxRef>a2e</BiopaxRef> <BiopaxRef>d83</BiopaxRef> <Graphics CenterX="4060.0" CenterY="1590.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P35913" /> </DataNode> <DataNode TextLabel="PDE6G " GraphId="ed9e4" Type="Protein" GroupRef="c9ae2"> <BiopaxRef>d3c</BiopaxRef> <BiopaxRef>f70</BiopaxRef> <Graphics CenterX="4060.0" CenterY="1610.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P18545" /> </DataNode> <DataNode TextLabel="H2O" GraphId="f9172" Type="Metabolite"> <Graphics CenterX="2979.5" 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<Graphics CenterX="4170.0" CenterY="1450.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14028" /> </DataNode> <DataNode TextLabel="cGMP " GraphId="f70d0" Type="Metabolite" GroupRef="c97db"> <Graphics CenterX="4170.0" CenterY="1470.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:16356" /> </DataNode> <DataNode TextLabel="CNG channel" GraphId="ae270" Type="Complex"> <BiopaxRef>fcc</BiopaxRef> <Graphics CenterX="3011.5" CenterY="149.0" Width="83.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="REACT_165342" /> </DataNode> <DataNode TextLabel="CNGA1 " GraphId="c4dcf" Type="Protein" GroupRef="b2a61"> <Graphics CenterX="4280.0" CenterY="1410.0" Width="80.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29973" /> </DataNode> <DataNode TextLabel="CNGB1 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TextLabel="Ca2+" GraphId="fc88a" Type="Metabolite"> <Graphics CenterX="3340.0" CenterY="228.0" Width="50.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:29108" /> </DataNode> <DataNode TextLabel="K+" GraphId="db986" Type="Metabolite"> <Graphics CenterX="3430.5" CenterY="210.0" Width="35.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:29103" /> </DataNode> <DataNode TextLabel="K+" GraphId="b5232" Type="Metabolite"> <Graphics CenterX="3469.5" CenterY="70.0" Width="35.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:29103" /> </DataNode> <DataNode TextLabel="SLC24A1" GraphId="b90b6" Type="Protein"> <Graphics CenterX="3377.5" CenterY="150.0" Width="61.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O60721" /> </DataNode> <DataNode TextLabel="Na+" 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It is thought to be phospholipase B (Rigtrup et al. 1994).</Comment> <BiopaxRef>bb7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="82.0" Y="371.0" /> <Point X="159.0" Y="371.0" /> <Anchor Position="0.0" Shape="None" GraphId="c3886" /> <Anchor Position="0.99" Shape="None" GraphId="a7d38" /> <Anchor Position="0.5" Shape="None" GraphId="b8e36" /> </Graphics> <Xref Database="Reactome" ID="REACT_25063" /> </Interaction> <Interaction GraphId="df9b8"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="58.0" Y="325.0" GraphRef="c353d" RelX="0.25" RelY="1.2" /> <Point X="82.0" Y="371.0" GraphRef="c3886" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25063" /> </Interaction> <Interaction GraphId="d85b2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="87.0" Y="353.0" GraphRef="fd197" RelX="-0.20930232558139536" RelY="1.2" /> <Point X="82.0" Y="371.0" GraphRef="c3886" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25063" /> </Interaction> <Interaction GraphId="a7085"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="159.0" Y="371.0" GraphRef="a7d38" RelX="0.7699999999999818" RelY="0.0" /> <Point X="169.0" Y="384.0" GraphRef="f6bde" RelX="-0.4583333333333333" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_25063" /> </Interaction> <Interaction GraphId="b3482"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="159.0" Y="371.0" GraphRef="a7d38" RelX="0.7699999999999818" RelY="0.0" /> <Point X="213.0" Y="393.0" GraphRef="a0e29" RelX="-1.1176470588235294" RelY="-0.6666666666666666" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_25063" /> </Interaction> <Interaction GraphId="d1025"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="119.0" Y="393.0" GraphRef="b46b6" RelX="-0.08108108108108109" RelY="-1.2727272727272727" /> <Point X="119.0" Y="371.0" GraphRef="b8e36" RelX="-1.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_25063" /> </Interaction> <Interaction GraphId="ec522"> <Comment Source="Reactome">In enterocytes, the dominant retinol-binding protein is RBP2 (CRBPII) which is abundant and binds retinol faster than the cell membrane. So, even though lipophilic retinol can easily enter the cell membrane of bowel enterocytes, it is collected by the abundancy of RBP2 into the enterocyte cytosol where it is further processed (Inagami &amp; Ong 1997).</Comment> <BiopaxRef>b33</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="240.0" Y="441.0" /> <Point X="400.0" Y="442.0" /> <Anchor Position="0.0" Shape="None" GraphId="e9f85" /> </Graphics> <Xref Database="Reactome" ID="REACT_25146" /> </Interaction> <Interaction GraphId="f4af3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="240.0" Y="421.0" GraphRef="a0e29" RelX="-0.058823529411764705" RelY="1.2" /> <Point X="240.0" Y="441.0" GraphRef="e9f85" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25146" /> </Interaction> <Interaction GraphId="d207e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="207.0" Y="468.0" GraphRef="bf007" RelX="-23.102564102564102" RelY="-1.0909090909090908" /> <Point X="240.0" Y="441.0" GraphRef="e9f85" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25146" /> </Interaction> <Interaction GraphId="ca197"> <Comment Source="Reactome">As long as vitamin A is needed, beta-carotene-monooxygenase (BCMO1) catalyses the cleavage of carotenes, resulting mainly in retinal (Fierce et al. 2008).</Comment> <BiopaxRef>ba1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="150.0" Y="577.0" /> <Point X="212.0" Y="577.0" /> <Anchor Position="0.0" Shape="None" GraphId="a6cc1" /> <Anchor Position="0.5" Shape="None" GraphId="c74d5" /> </Graphics> <Xref Database="Reactome" ID="REACT_25117" /> </Interaction> <Interaction GraphId="e297d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="128.0" Y="577.0" GraphRef="cf732" RelX="1.1176470588235294" RelY="0.0" /> <Point X="150.0" Y="577.0" GraphRef="a6cc1" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25117" /> </Interaction> <Interaction GraphId="ea340"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="143.0" Y="567.0" GraphRef="d56c4" RelX="0.35294117647058826" RelY="1.2" /> <Point X="150.0" Y="577.0" GraphRef="a6cc1" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25117" /> </Interaction> <Interaction GraphId="a6044"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="171.0" Y="599.0" GraphRef="ee131" RelX="-0.023255813953488372" RelY="-1.2727272727272727" /> <Point X="171.0" Y="577.0" GraphRef="c74d5" RelX="-10.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_25117" /> </Interaction> <Interaction GraphId="bbc89"> <Comment Source="Reactome">In enterocytes, all-trans-retinal (atRAL) binds to RBP2 (CRBPII) for stabilisation, metabolism and transport (Fierce et al. 2008).</Comment> <BiopaxRef>ba1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="240.0" Y="523.0" /> <Point X="266.0" Y="529.0" /> <Anchor Position="0.0" Shape="None" GraphId="a3881" /> </Graphics> <Xref Database="Reactome" ID="REACT_160101" /> </Interaction> <Interaction GraphId="bb721"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="207.0" Y="496.0" GraphRef="bf007" RelX="-23.102564102564102" RelY="1.4545454545454546" /> <Point X="240.0" Y="523.0" GraphRef="a3881" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160101" /> </Interaction> <Interaction GraphId="a6732"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="240.0" Y="560.0" GraphRef="d3ffc" RelX="-80.72" RelY="-38.86666666666667" /> <Point X="240.0" Y="523.0" GraphRef="a3881" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160101" /> </Interaction> <Interaction GraphId="d8c77"> <Comment Source="Reactome">Although the enzyme catalysing retinal reduction in human enterocytes is not identified, the best candidate is retinol dehydrogenase 11 (RDH11, RalR1). It is expressed in the intestine, has a basic pH optimum, and localises to the ER membrane where LRAT catalyses the next step in the pathway. However, RDH11 catalyses retinal reduction to retinol &lt;i&gt;in vitro&lt;/i&gt; and uses NADPH as cofactor (Fierce et al. 2008).</Comment> <BiopaxRef>ba1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="343.0" Y="498.0" /> <Point X="386.0" Y="498.0" /> <Anchor Position="0.0" Shape="None" GraphId="de2ed" /> <Anchor Position="0.99" Shape="None" GraphId="f0dbb" /> <Anchor Position="0.5" Shape="None" GraphId="be2c2" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="d6b0a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="311.0" Y="498.0" GraphRef="c6d0d" RelX="-105.0" RelY="-40.8" /> <Point X="343.0" Y="498.0" GraphRef="de2ed" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="b771b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="317.0000000000002" Y="478.0" GraphRef="f643a" RelX="-64.01694915254237" RelY="-46.13333333333333" /> <Point X="343.0" Y="498.0" GraphRef="de2ed" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="b0e90"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="309.0" Y="529.0" GraphRef="ed60a" RelX="0.2631578947368421" RelY="-1.2727272727272727" /> <Point X="343.0" Y="498.0" GraphRef="de2ed" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="b53d5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="386.0" Y="498.0" GraphRef="f0dbb" RelX="0.4300000000000068" RelY="0.0" /> <Point X="407.0" Y="517.0" GraphRef="c5a60" RelX="-54.43333333333333" RelY="-44.06666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="a2951"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="386.0" Y="498.0" GraphRef="f0dbb" RelX="0.4300000000000068" RelY="0.0" /> <Point X="430.0" Y="457.0" GraphRef="b52ba" RelX="-0.2987012987012987" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="f2f4f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="368.0" Y="479.0" GraphRef="ae0db" RelX="-0.0196078431372549" RelY="1.2727272727272727" /> <Point X="369.0" Y="498.0" GraphRef="be2c2" RelX="4.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_25000" /> </Interaction> <Interaction GraphId="fddd7"> <Comment Source="Reactome">Transfer of fatty acyl residues (FACYLs) from lecithin is the main way to esterify all-trans-retinol (atROL). Lecithin is a generic name for the yellowy-brown fatty substances in animals and tissues. It can be composed of phosphatidylcholines, phosphatidylethanolamines, and phosphatidylinositols. Fatty acyl transfer is catalyzed by Lecithin retinol acyltransferase (LRAT) and takes place near the endoplasmic reticulum membrane. The main fatty acyl moieties that are substrates for LRAT are palmitoyl, oleoyl, stearoyl and linoleoyl groups present in the A1 position of membrane phosphatidylcholine molecules. LRAT esterifies atROL with these acyl groups to form all-trans-retinyl esters (atREs). The aim is not storage but transport via chylomicrons (Ruiz et al. 1999).</Comment> <BiopaxRef>acc</BiopaxRef> <BiopaxRef>e5f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="536.0" Y="443.0" /> <Point X="612.0" Y="443.0" /> <Anchor Position="0.0" Shape="None" GraphId="bfcd3" /> <Anchor Position="0.99" Shape="None" GraphId="ff02d" /> <Anchor Position="0.5" Shape="None" GraphId="f4ce2" /> </Graphics> <Xref Database="Reactome" ID="REACT_25108" /> </Interaction> <Interaction GraphId="dfbcb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="483.0" Y="443.0" GraphRef="b52ba" RelX="1.077922077922078" RelY="0.0" /> <Point X="536.0" Y="443.0" GraphRef="bfcd3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25108" /> </Interaction> <Interaction GraphId="aa2c2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="516.0" Y="417.0" GraphRef="b46ff" RelX="-14.10344827586207" RelY="-23.666666666666668" /> <Point X="536.0" Y="443.0" GraphRef="bfcd3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_25108" /> </Interaction> <Interaction GraphId="c40e0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="612.0" Y="443.0" GraphRef="ff02d" RelX="0.7599999999999909" RelY="0.0" /> <Point X="656.0" Y="443.0" GraphRef="bcbf3" RelX="-1.1224489795918366" RelY="-0.06666666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_25108" /> </Interaction> <Interaction GraphId="b99de"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="612.0" Y="443.0" GraphRef="ff02d" RelX="0.7599999999999909" RelY="0.0" /> <Point X="643.0" Y="466.0" GraphRef="bf007" RelX="-0.7435897435897436" RelY="-1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_25108" /> </Interaction> <Interaction GraphId="d84c0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="568.0" Y="510.0" GraphRef="e39f1" RelX="-27.05128205128205" RelY="-19.363636363636363" /> <Point X="582.0" Y="443.0" GraphRef="f4ce2" RelX="8.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_25108" /> </Interaction> <Interaction GraphId="d4f03"> <Comment Source="Reactome">Chylomicrons (CM) are large (75–450 nm), spherical lipoprotein particles secreted by intestinal cells postprandially and transport dietary fat and fat-soluble vitamins in the lymphatic system (Nayak et al. 2001, During &amp; Harrison 2007). All-trans-retinyl esters (atREs) are packaged into nascent chylomicrons.</Comment> <BiopaxRef>f4d</BiopaxRef> <BiopaxRef>ea8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="735.0" Y="471.0" /> <Point X="783.0" Y="539.0" /> <Anchor Position="0.0" Shape="None" GraphId="b2f2c" /> </Graphics> <Xref Database="Reactome" ID="REACT_160145" /> </Interaction> <Interaction GraphId="be8eb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="711.0" Y="456.0" GraphRef="bcbf3" RelX="1.1224489795918366" RelY="0.8" /> <Point X="735.0" Y="471.0" GraphRef="b2f2c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160145" /> </Interaction> <Interaction GraphId="c36eb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="780.0" Y="456.0" GraphRef="e51ef" RelX="-0.76" RelY="1.2727272727272727" /> <Point X="735.0" Y="471.0" GraphRef="b2f2c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160145" /> </Interaction> <Interaction GraphId="ec0c5"> <Comment Source="Reactome">Nascent chylomicrons (CM) containing all-trans-retinyl esters (atREs) are secreted from intestinal cells and transported to the liver via the lymphatic system (Nayak et al. 2001, During &amp; Harrison 2007).</Comment> <BiopaxRef>ea8</BiopaxRef> <BiopaxRef>f4d</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="789.0" Y="567.0" /> <Point X="789.0" Y="684.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160215" /> </Interaction> <Interaction GraphId="e80a4"> <Comment Source="Reactome">Nascent chylomicrons (CMs) acquire copies of apolipoproteins C-II, C-III, and E from circulating spherical (mature) high-density lipoprotein particles, becoming mature chylomicrons (Havel et al. 1973, Bisgaier &amp; Glickman 1983). Here, this interaction is annotated to involve the transfer of a single copy of each lipoprotein, but a mature chylomicron in fact contains approximately 25 copies of apolipoprotein E and 180 copies of C apolipoproteins (Bhattacharya &amp; Redgrave 1981).</Comment> <BiopaxRef>b49</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="716.0" Y="698.0" /> <Point X="645.0" Y="698.0" /> <Anchor Position="0.0" Shape="None" GraphId="e67a1" /> <Anchor Position="0.99" Shape="None" GraphId="c87c7" /> </Graphics> <Xref Database="Reactome" ID="REACT_160168" /> </Interaction> <Interaction GraphId="e5738"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="731.0" Y="698.0" GraphRef="cc886" RelX="-1.054054054054054" RelY="0.0" /> <Point X="716.0" Y="698.0" GraphRef="e67a1" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160168" /> </Interaction> <Interaction GraphId="d048a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="740.0" Y="732.0" GraphRef="cc7f1" RelX="-0.2" RelY="-1.1666666666666667" /> <Point X="716.0" Y="698.0" GraphRef="e67a1" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160168" /> </Interaction> <Interaction GraphId="a1a6c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="645.0" Y="698.0" GraphRef="c87c7" RelX="-0.7100000000000364" RelY="0.0" /> <Point X="626.0" Y="729.0" GraphRef="ae235" RelX="0.12359550561797752" RelY="-1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160168" /> </Interaction> <Interaction GraphId="ecb99"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="645.0" Y="698.0" GraphRef="c87c7" RelX="-0.7100000000000364" RelY="0.0" /> <Point X="609.0" Y="698.0" GraphRef="abe53" RelX="1.0555555555555556" RelY="-0.09090909090909091" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160168" /> </Interaction> <Interaction GraphId="ecccf"> <Comment Source="Reactome">Lipoprotein lipase dimers (LPL:LPL) are tethered to heparan sulfate proteoglycans (HSPG) at endothelial cell surfaces (Fernandez-Borja et al. 1996; Peterson et al. 1992). Both syndecan 1 (Rosenberg et al. 1997) and perlecan (Goldberg 1996) HSPG molecules are capable of tethering LPL. The LPL enzyme catalyzes the hydrolysis and release of triacylglycerols (TG) associated with circulating chylomicrons to leave a CM remnant (CR). This reaction is annotated here as causing the hydrolysis and release of 50 molecules of TG. In vivo, the number is much larger, and TG depletion probably occurs in the course of multiple encounters between a chylomicron and endothelial LPL. This reaction is strongly activated by chylomicron-associated apo C-II protein both in vivo and in vitro (Jackson et al. 1986). Chylomicron-associated apoC-II protein inhibits LPL activity in vitro (Brown and Baginsky 1972), and recent studies have indicated a positive regulatory role for apoA-5 protein, though its molecular mechanism of action remains unclear (Marcais et al. 2005; Merkel and Heeren 2005). CRs can then be taken up by liver parenchymal cells in two ways; 1) directly by the LDL receptor or 2) apoE/HSPG-directed uptake by LDL receptor-related proteins.</Comment> <BiopaxRef>f66</BiopaxRef> <BiopaxRef>d65</BiopaxRef> <BiopaxRef>e0f</BiopaxRef> <BiopaxRef>b4b</BiopaxRef> <BiopaxRef>a1a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="495.0" Y="699.0" /> <Point X="405.0" Y="699.0" /> <Anchor Position="0.99" Shape="None" GraphId="b393d" /> <Anchor Position="0.5" Shape="None" GraphId="ba5a0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160186" /> </Interaction> <Interaction GraphId="a651b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="405.0" Y="699.0" GraphRef="b393d" RelX="-0.8999999999999773" RelY="0.0" /> <Point X="291.0" Y="764.0" GraphRef="d07f4" RelX="1.24" RelY="-0.6363636363636364" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160186" /> </Interaction> <Interaction GraphId="d26a1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="405.0" Y="699.0" GraphRef="b393d" RelX="-0.8999999999999773" RelY="0.0" /> <Point X="288.0" Y="699.0" GraphRef="c3a68" RelX="1.1395348837209303" RelY="-0.06666666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160186" /> </Interaction> <Interaction GraphId="f2fa0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="405.0" Y="699.0" GraphRef="b393d" RelX="-0.8999999999999773" RelY="0.0" /> <Point X="365.0" Y="680.0" GraphRef="cb6b3" RelX="1.1176470588235294" RelY="0.6666666666666666" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160186" /> </Interaction> <Interaction GraphId="a69e3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="455.0" Y="833.0" GraphRef="c5d74" RelX="-0.023255813953488372" RelY="-1.2727272727272727" /> <Point X="451.0" Y="699.0" GraphRef="ba5a0" RelX="1.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160186" /> </Interaction> <Interaction GraphId="a7730"> <Comment Source="Reactome">Chylomicron remnants (CRs) are "sieved" when they arrive at the liver by size, the appropriate sized remnants passing through the space of Disse. Once inside, CRs containing all-trans-retinyl esters (atREs) can be directly and rapidly taken up by liver parenchymal cells via the low-density lipoprotein receptor (LDLR) using apolipoprotein E (apoE) as a ligand. Internalization of remnants occur via endocytosis (see review D'Ambrosio et al. 2011). This reaction is inferred from uptake studies in mice (Yu et al. 2000). Defects in LDLR cause familial hypercholesterolemia (FH, MIM:143890), a common autosomal disease that affects about 1 in 500 people in most countries. Abnormal LDLR doesn't remove LDL from circulation resulting in high levels of LDL in blood, leading to early cardiovascular disease via atherosclerosis. The defect was first described by Brown and Goldstein (1974).</Comment> <BiopaxRef>b11</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="283.0" Y="785.0" /> <Point X="328.0" Y="891.0" /> <Anchor Position="0.5" Shape="None" GraphId="c5b03" /> </Graphics> <Xref Database="Reactome" ID="REACT_160308" /> </Interaction> <Interaction GraphId="f9d98"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="358.0" Y="851.0" GraphRef="b0f5c" RelX="-1.1578947368421053" RelY="0.0" /> <Point X="337.0" Y="851.0" GraphRef="c5b03" RelX="31.5" RelY="13.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160308" /> </Interaction> <Interaction GraphId="f9f2a"> <Comment Source="Reactome">When the low-density lipoprotein receptor (LDLR) is missing, saturated or inhibited, chylomicron remnants (CRs) containing all-trans-retinyl esters (atREs) bind apolioprotein E (apoE). ApoE, secreted by hepatocytes, acts as a high-affinity ligand for the LDL-related receptor protein (LRP) family. CR:atREs:apoE then binds to cell-surface heparan sulfate proteoglycan (HSPG), abundant in the space of Disse. HSPG/apoE binding plays a critical role in the capture of CR:atREs, ready for internalization via LRPs (Futamura et al. 2005, Yamauchi et al. 2008).</Comment> <BiopaxRef>dbd</BiopaxRef> <BiopaxRef>e00</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="183.0" Y="796.0" /> <Point X="206.0" Y="831.0" /> <Anchor Position="0.0" Shape="None" GraphId="d7e54" /> </Graphics> <Xref Database="Reactome" ID="REACT_160149" /> </Interaction> <Interaction GraphId="bc1cd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="260.0" Y="774.0" GraphRef="d07f4" RelX="-1.24" RelY="0.2727272727272727" /> <Point X="183.0" Y="796.0" GraphRef="d7e54" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160149" /> </Interaction> <Interaction GraphId="e1fe6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="137.0" Y="835.0" GraphRef="ce12a" RelX="0.4782608695652174" RelY="-1.2727272727272727" /> <Point X="183.0" Y="796.0" GraphRef="d7e54" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160149" /> </Interaction> <Interaction GraphId="b41ce"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="153.0" Y="785.0" GraphRef="d77d0" RelX="1.1578947368421053" RelY="0.45454545454545453" /> <Point X="183.0" Y="796.0" GraphRef="d7e54" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160149" /> </Interaction> <Interaction GraphId="e9874"> <Comment Source="Reactome">When the low-density lipoprotein receptor (LDLR) is missing, saturated or inhibited, chylomicron remnants (CRs) containing all-trans-retinyl esters (atREs) can be cleared from circulation by interaction with cell-surface heparan sulfate proteoglycan (HSPG) and secreted apolipoprotein E (apoE). This complex is then presented to LDL receptor-related proteins (LRPs; reviews May et al. 2007, Li et al. 2001, Hussain 2001) for internalization (Ji et al. 1993).</Comment> <BiopaxRef>b82</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="213.0" Y="859.0" /> <Point X="220.0" Y="909.0" /> <Anchor Position="0.5" Shape="None" GraphId="c24de" /> </Graphics> <Xref Database="Reactome" ID="REACT_160272" /> </Interaction> <Interaction GraphId="eb2f5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="278.0" Y="854.0" GraphRef="bd158" RelX="-1.1666666666666667" RelY="0.6363636363636364" /> <Point X="213.0" Y="882.0" GraphRef="c24de" RelX="-3.5" RelY="-2.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160272" /> </Interaction> <Interaction GraphId="ba81a"> <Comment Source="Reactome">Once inside liver parenchymal cells, all-trans-retinyl esters (atREs), are hydrolysed to all-trans-retinol (atROL) and fatty acids (FAs) by a neutral, all-trans-retinyl ester hydrolase (NREH). No NREH has been characterised yet although both acidic and neutral REH activity has been shown to be associated with endosomes and plasma membrane preparations from rodent livers (Harrison &amp; Gad 1989, Gad &amp; Harrison 1991, Hagen et al. 1999). As the acidity increases, early endosomes change to late endosomes and further hydrolysis of atREs is mediated by acid retinyl ester hydrolase (AREH). Like NREH, AREH has not yet been characterised (see refs above). The translocation mechanism of atROL to cytosol is unknown.</Comment> <BiopaxRef>e3c</BiopaxRef> <BiopaxRef>b9f</BiopaxRef> <BiopaxRef>e3d</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="326.0" Y="957.0" /> <Point X="325.0" Y="1077.0" /> <Anchor Position="0.0" Shape="None" GraphId="c55f7" /> <Anchor Position="0.99" Shape="None" GraphId="aec3e" /> <Anchor Position="0.5" Shape="None" GraphId="d5d48" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="ec845"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="326.0" Y="919.0" GraphRef="c64a0" RelX="-0.01639344262295082" RelY="1.2727272727272727" /> <Point X="326.0" Y="957.0" GraphRef="c55f7" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="baf17"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="294.0" Y="963.0" GraphRef="d0c1e" RelX="1.1395348837209303" RelY="-0.26666666666666666" /> <Point X="326.0" Y="957.0" GraphRef="c55f7" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="e2711"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="325.0" Y="1077.0" GraphRef="aec3e" RelX="-0.009999999999990905" RelY="1.2000000000000455" /> <Point X="296.0" Y="1090.0" GraphRef="d87b8" RelX="1.24" RelY="-0.5454545454545454" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="d904a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="325.0" Y="1077.0" GraphRef="aec3e" RelX="-0.009999999999990905" RelY="1.2000000000000455" /> <Point X="286.0" Y="1126.0" GraphRef="eb340" RelX="0.5135135135135135" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="ffd1f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="325.0" Y="1077.0" GraphRef="aec3e" RelX="-0.009999999999990905" RelY="1.2000000000000455" /> <Point X="296.0" Y="1056.0" GraphRef="a624c" RelX="0.9444444444444444" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="c8cf7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="325.0" Y="1077.0" GraphRef="aec3e" RelX="-0.009999999999990905" RelY="1.2000000000000455" /> <Point X="384.0" Y="1079.0" GraphRef="bcf69" RelX="-1.1176470588235294" RelY="-0.13333333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="e45e7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="296.0" Y="997.0" GraphRef="b7744" RelX="1.1428571428571428" RelY="-0.09090909090909091" /> <Point X="326.0" Y="997.0" GraphRef="d5d48" RelX="0.5" RelY="-20.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160239" /> </Interaction> <Interaction GraphId="e2a0c"> <Comment Source="Reactome">When the body is in a retinoid-sufficient state, all-trans-retinol (atROL) is transferred to hepatic stellate cells (HSCs) for storage. The transfer was established in rat experiments (Blomhoff et al. 1982, Blomhoff et al. 1984). The mechanism of transport is as yet unknown.</Comment> <BiopaxRef>d59</BiopaxRef> <BiopaxRef>a91</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="466.0" Y="1123.0" /> <Point X="509.0" Y="1109.0" /> <Anchor Position="0.99" Shape="None" GraphId="de0b6" /> </Graphics> <Xref Database="Reactome" ID="REACT_160107" /> </Interaction> <Interaction GraphId="c52f3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="509.0" Y="1109.0" GraphRef="de0b6" RelX="0.4300000000000068" RelY="-0.14000000000010004" /> <Point X="533.0" Y="1109.0" GraphRef="fa378" RelX="-1.1176470588235294" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160107" /> </Interaction> <Interaction GraphId="fca24"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="509.0" Y="1109.0" GraphRef="de0b6" RelX="0.4300000000000068" RelY="-0.14000000000010004" /> <Point X="466.0" Y="1070.0" GraphRef="f6c67" RelX="-25.974358974358974" RelY="34.18181818181818" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160107" /> </Interaction> <Interaction GraphId="bec6b"> <Comment Source="Reactome">All-trans-retinol (atROL) is stored in hepatic stellate cells (HSCs) in its esterified form. Before esterification takes place, atROL binds to cellular retinol-binding protein 1 (RBP1) (Folli et al. 2001). The resultant complex (RBP1:atROL) serves as a substrate for lecithin retinol acyltransferase (LRAT), the main enzyme responsible for the esterification of atROL. It is thought the binding of RBP1 serves to translocate atROL to the endoplasmic reticulum where LRAT is located.</Comment> <BiopaxRef>acc</BiopaxRef> <BiopaxRef>b58</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="564.0" Y="1071.0" /> <Point X="587.0" Y="1070.0" /> <Anchor Position="0.0" Shape="None" GraphId="bcba8" /> </Graphics> <Xref Database="Reactome" ID="REACT_160295" /> </Interaction> <Interaction GraphId="d7c14"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="562.0" Y="1091.0" GraphRef="fa378" RelX="0.0196078431372549" RelY="-1.2" /> <Point X="564.0" Y="1071.0" GraphRef="bcba8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160295" /> </Interaction> <Interaction GraphId="d0e0a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="556.0" Y="1052.0" GraphRef="f6c67" RelX="-21.358974358974358" RelY="32.54545454545455" /> <Point X="564.0" Y="1071.0" GraphRef="bcba8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160295" /> </Interaction> <Interaction GraphId="b649b"> <Comment Source="Reactome">All-trans-retinyl esters (atREs) are the main storage form of retinol in hepatic stellate cells (HSCs). Lecithin retinol acyltransferase (LRAT) mediates the esterification of all-trans-retinol (atROL) with a variety of fatty acyl groups (FACYLs) to form REs which are stored in lipid droplets in the cytosol. Cellular retinol-binding protein 1 (RBP1) is an effective donor of atROL for LRAT (Ruiz et al. 1999). </Comment> <BiopaxRef>acc</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="640.0" Y="976.0" /> <Point X="696.0" Y="976.0" /> <Anchor Position="0.0" Shape="None" GraphId="c961d" /> <Anchor Position="0.99" Shape="None" GraphId="f6449" /> <Anchor Position="0.5" Shape="None" GraphId="c6dee" /> </Graphics> <Xref Database="Reactome" ID="REACT_160247" /> </Interaction> <Interaction GraphId="acc0a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="629.0" Y="1056.0" GraphRef="d2553" RelX="0.012987012987012988" RelY="-1.2727272727272727" /> <Point X="640.0" Y="976.0" GraphRef="c961d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160247" /> </Interaction> <Interaction GraphId="ccbf9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="561.0" Y="976.0" GraphRef="b46ff" RelX="-12.551724137931034" RelY="13.6" /> <Point X="640.0" Y="976.0" GraphRef="c961d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160247" /> </Interaction> <Interaction GraphId="ecd62"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="696.0" Y="976.0" GraphRef="f6449" RelX="0.5599999999999454" RelY="0.0" /> <Point X="794.0" Y="1025.0" GraphRef="cadc5" RelX="-10.46938775510204" RelY="26.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160247" /> </Interaction> <Interaction GraphId="fea25"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="696.0" Y="976.0" GraphRef="f6449" RelX="0.5599999999999454" RelY="0.0" /> <Point X="726.0" Y="958.0" GraphRef="f6c67" RelX="-12.64102564102564" RelY="24.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160247" /> </Interaction> <Interaction GraphId="e7c65"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="666.0" Y="944.0" GraphRef="e39f1" RelX="-22.025641025641026" RelY="20.09090909090909" /> <Point X="667.0" Y="976.0" GraphRef="c6dee" RelX="-1.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160247" /> </Interaction> <Interaction GraphId="d78bc"> <Comment Source="Reactome">At the stellate cell surface, all-trans-retinol (atROL) binds to retinol binding protein 4 (RBP4, holo-RBP) (Kanai et al. 1968). atROL is insoluble in aqueous conditions and it's thought RBP4 picks up atROL from the outer leaflet of the plasma membrane. RBP4 is a 21 kDa protein secreted into the bloodstream by the liver in an atROL-dependent manner. Defects in RBP4 cause retinol-binding protein deficiency (RBP deficiency, MIM:180250), causing night vision problems and progressive atrophy of the retinal pigment epithelium (RPE) (Seeliger et al. 1999).</Comment> <BiopaxRef>a64</BiopaxRef> <BiopaxRef>abd</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="949.0" Y="1212.0" /> <Point X="949.0" Y="1145.0" /> <Anchor Position="0.0" Shape="None" GraphId="a27d4" /> </Graphics> <Xref Database="Reactome" ID="REACT_160244" /> </Interaction> <Interaction GraphId="ca218"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="938.0" Y="1209.0" GraphRef="c5724" RelX="1.1538461538461537" RelY="0.36363636363636365" /> <Point X="949.0" Y="1212.0" GraphRef="a27d4" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160244" /> </Interaction> <Interaction GraphId="d9e9f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="940.0" Y="1215.0" GraphRef="b7e2c" RelX="0.8431372549019608" RelY="-1.2" /> <Point X="949.0" Y="1212.0" GraphRef="a27d4" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160244" /> </Interaction> <Interaction GraphId="d1e29"> <Comment Source="Reactome">Once hydrolysed from all-trans-retinyl esters (atREs), all-trans-retinol (atROL) can either be esterified for storage or secreted into the bloodstream for transport to target tissues/organs (Kanai et al. 1968). The mechanism of secretion/efflux is currently unknown.</Comment> <BiopaxRef>a64</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="590.0" Y="1118.0" /> <Point X="890.0" Y="1226.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160307" /> </Interaction> <Interaction GraphId="d4be3"> <Comment Source="Reactome">In the bloodstream, circulating retinol binding protein 4 (RBP4, in complex with atROL), binds transthyretin (TTR, a 51 kDa protein) in a 1:1 molar complex (Naylor &amp; Newcomer, 1999). The resultant TTR:RBP4:atROL complex is larger and therefore less susceptible to glomerular filtration, maintaining normal levels of retinoid and RBP4 in the circulation. In TTR-deficient mice, plasma levels of atROL and RBP4 were observed to be 5% of wild type levels, highlighting the importance of TTR binding to RBP4:atROL (Episkopou et al. 1993). TTR is also a transporter for thyroxine in the brain (not shown here) (Herbert et al. 1986).</Comment> <BiopaxRef>cde</BiopaxRef> <BiopaxRef>cea</BiopaxRef> <BiopaxRef>d9b</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="949.0" Y="1049.0" /> <Point X="948.0" Y="1011.0" /> <Anchor Position="0.0" Shape="None" GraphId="e2024" /> </Graphics> <Xref Database="Reactome" ID="REACT_160076" /> </Interaction> <Interaction GraphId="aed99"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="949.0" Y="1117.0" GraphRef="ba1c1" RelX="-0.012987012987012988" RelY="-1.2727272727272727" /> <Point X="949.0" Y="1049.0" GraphRef="e2024" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160076" /> </Interaction> <Interaction GraphId="c32b9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="976.0" Y="1071.0" GraphRef="d5421" RelX="-0.28735632183908044" RelY="-1.2727272727272727" /> <Point X="949.0" Y="1049.0" GraphRef="e2024" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160076" /> </Interaction> <Interaction GraphId="f947d"> <Comment Source="Reactome">Retinyl esters (REs) are stored in lipid droplets (LDs) in hepatic stellate cells (HSCs) until there is a demand for retinoid by the body. Mobilization of atREs stores require lipases with retinyl ester hydrolase (REH) activity. At present, the identity of the REH mediating atRE mobilization is unknown (see reviews Shirakami et al. 2012, Schreiber et al. 2012). In studies performed with rat livers, Mello et al. found that the carboxylesterases ES4 and ES10 possessed REH activity and were localised to HSCs (Mello et al. 2008) but it's not confirmed that these are the actual REHs involved in retinoid mobilization. The human orthologue to these rat enzymes is presently unknown.</Comment> <BiopaxRef>ef8</BiopaxRef> <BiopaxRef>cb1</BiopaxRef> <BiopaxRef>b8b</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="789.0" Y="1109.0" /> <Point X="693.0" Y="1109.0" /> <Anchor Position="0.0" Shape="None" GraphId="ddc46" /> <Anchor Position="0.99" Shape="None" GraphId="cdfa5" /> <Anchor Position="0.5" Shape="None" GraphId="ec67d" /> </Graphics> <Xref Database="Reactome" ID="REACT_160160" /> </Interaction> <Interaction GraphId="d4d3d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="814.0" Y="1055.0" GraphRef="cadc5" RelX="-9.653061224489797" RelY="28.2" /> <Point X="789.0" Y="1109.0" GraphRef="ddc46" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160160" /> </Interaction> <Interaction GraphId="f2fac"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="808.0" Y="1121.0" GraphRef="ad5cd" RelX="-14.86046511627907" RelY="35.93333333333333" /> <Point X="789.0" Y="1109.0" GraphRef="ddc46" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160160" /> </Interaction> <Interaction GraphId="e1a98"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="693.0" Y="1109.0" GraphRef="cdfa5" RelX="-0.9600000000000364" RelY="0.0" /> <Point X="590.0" Y="1109.0" GraphRef="fa378" RelX="1.1176470588235294" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160160" /> </Interaction> <Interaction GraphId="ce582"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="693.0" Y="1109.0" GraphRef="cdfa5" RelX="-0.9600000000000364" RelY="0.0" /> <Point X="736.0" Y="1073.0" GraphRef="e41f6" RelX="-14.027027027027026" RelY="29.266666666666666" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160160" /> </Interaction> <Interaction GraphId="a7de5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="757.0" Y="1137.0" GraphRef="adccd" RelX="-0.030303030303030304" RelY="-1.2727272727272727" /> <Point X="757.0" Y="1109.0" GraphRef="ec67d" RelX="16.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160160" /> </Interaction> <Interaction GraphId="b9245"> <Comment Source="Reactome">Once inside liver parenchymal cells, all-trans-retinyl esters (atREs), are hydrolysed to all-trans-retinol (atROL) and fatty acids (FAs) by a neutral, all-trans-retinyl ester hydrolase (NREH). No NREH has been characterised yet although both acidic and neutral REH activity has been shown to be associated with endosomes and plasma membrane preparations from rodent livers (Harrison &amp; Gad 1989, Gad &amp; Harrison 1991, Hagen et al. 1999). As the acidity increases, early endosomes change to late endosomes and further hydrolysis of atREs is mediated by acid retinyl ester hydrolase (AREH). Like NREH, AREH has not yet been characterised (see refs above). The translocation mechanism of atROL to cytosol is unknown.</Comment> <BiopaxRef>e3c</BiopaxRef> <BiopaxRef>b9f</BiopaxRef> <BiopaxRef>e3d</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="957.0" /> <Point X="221.0" Y="1046.0" /> <Anchor Position="0.0" Shape="None" GraphId="cca8c" /> <Anchor Position="0.99" Shape="None" GraphId="a48e4" /> <Anchor Position="0.5" Shape="None" GraphId="e25ab" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="a0d15"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="245.0" Y="962.0" GraphRef="d0c1e" RelX="-1.1395348837209303" RelY="-0.3333333333333333" /> <Point X="221.0" Y="957.0" GraphRef="cca8c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="b3175"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="222.0" Y="937.0" GraphRef="c1ec9" RelX="-0.023255813953488372" RelY="1.2727272727272727" /> <Point X="221.0" Y="957.0" GraphRef="cca8c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="d08d3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="1046.0" GraphRef="a48e4" RelX="0.0" RelY="0.8900000000001" /> <Point X="265.0" Y="1085.0" GraphRef="d87b8" RelX="-1.24" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="c58d9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="1046.0" GraphRef="a48e4" RelX="0.0" RelY="0.8900000000001" /> <Point X="267.0" Y="1126.0" GraphRef="eb340" RelX="-0.5135135135135135" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="a5b56"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="1046.0" GraphRef="a48e4" RelX="0.0" RelY="0.8900000000001" /> <Point X="258.0" Y="1040.0" GraphRef="a624c" RelX="-1.1666666666666667" RelY="0.13333333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="ed919"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="1046.0" GraphRef="a48e4" RelX="0.0" RelY="0.8900000000001" /> <Point X="198.0" Y="1087.0" GraphRef="c0d18" RelX="0.2631578947368421" RelY="-1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="fa32a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="1046.0" GraphRef="a48e4" RelX="0.0" RelY="0.8900000000001" /> <Point X="131.0" Y="863.0" GraphRef="ce12a" RelX="0.21739130434782608" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="fe561"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="221.0" Y="1046.0" GraphRef="a48e4" RelX="0.0" RelY="0.8900000000001" /> <Point X="384.0" Y="1076.0" GraphRef="bcf69" RelX="-1.1176470588235294" RelY="-0.3333333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="d72e4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="248.0" Y="998.0" GraphRef="b7744" RelX="-1.1428571428571428" RelY="0.0" /> <Point X="221.0" Y="998.0" GraphRef="e25ab" RelX="0.0" RelY="-3.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160151" /> </Interaction> <Interaction GraphId="f34a1"> <Comment Source="Reactome">All-trans-retinol (atROL) circulates in the bloodstream in complex with transthyretin (TTR) and retinol- binding protein 4 (RBP4). The receptor Stimulated by retinoic acid gene 6 protein homologue (STRA6) acts as a high-affinity cell-surface receptor for the complex (Berry et al. 2012), removing atROL and transporting it into tissues expressing STRA6, including the eyes (Kawaguchi et al. 2007).</Comment> <BiopaxRef>e69</BiopaxRef> <BiopaxRef>c5f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="983.0" Y="896.0" /> <Point X="1032.0" Y="896.0" /> <Anchor Position="0.0" Shape="None" GraphId="ea1ec" /> </Graphics> <Xref Database="Reactome" ID="REACT_160313" /> </Interaction> <Interaction GraphId="f911f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="951.0" Y="983.0" GraphRef="b4f1c" RelX="0.047619047619047616" RelY="-1.2727272727272727" /> <Point X="983.0" Y="896.0" GraphRef="ea1ec" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160313" /> </Interaction> <Interaction GraphId="d1420"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="962.0" Y="896.0" GraphRef="ad432" RelX="1.127659574468085" RelY="-0.09090909090909091" /> <Point X="983.0" Y="896.0" GraphRef="ea1ec" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160313" /> </Interaction> <Interaction GraphId="ae8ea"> <Comment Source="Reactome">Stimulated by retinoic acid gene 6 protein homologue (STRA6) acts as a high-affinity cell-surface receptor for the TTR:RBP4:atROL complex (Berry et al. 2012). Once bound, STRA6 removes atROL and transports it into cells expressing STRA6 receptors, including eye (Kawaguchi et al. 2007). Defects in STRA6 cause microphthalmia syndromic type 9 (MCOPS9, Matthew-Wood syndrome or Spear syndrome; MIM:601186) (Chassaing et al. 2009). The uptake of atROL is driven by the conversion of atROL to retinyl ester (RE) by LRAT (Kawaguchi et al. 2011).</Comment> <BiopaxRef>c5f</BiopaxRef> <BiopaxRef>e69</BiopaxRef> <BiopaxRef>bbe</BiopaxRef> <BiopaxRef>c6f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1147.0" Y="896.0" /> <Point X="1207.0" Y="896.0" /> <Anchor Position="0.99" Shape="None" GraphId="efe19" /> </Graphics> <Xref Database="Reactome" ID="REACT_160278" /> </Interaction> <Interaction GraphId="b1a63"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1207.0" Y="896.0" GraphRef="efe19" RelX="0.599999999999909" RelY="0.0" /> <Point X="1233.0" Y="896.0" GraphRef="fc98a" RelX="-1.055045871559633" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160278" /> </Interaction> <Interaction GraphId="f15a0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1207.0" Y="896.0" GraphRef="efe19" RelX="0.599999999999909" RelY="0.0" /> <Point X="1207.0" Y="847.0" GraphRef="ae14a" RelX="-0.058823529411764705" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160278" /> </Interaction> <Interaction GraphId="ddbf8"> <Comment Source="Reactome">Once all-trans-retinol (atROL) enters the retinal pigment epithelium (RPE) and before esterification takes place, atROL binds to cellular retinol-binding protein 1 (RBP1) (Folli et al. 2001). The resultant complex (RBP1:atROL) serves as a substrate for lecithin retinol acyltransferase (LRAT), the main enzyme responsible for the esterification of atROL.</Comment> <BiopaxRef>b58</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1105.0" Y="829.0" /> <Point X="1070.0" Y="829.0" /> <Anchor Position="0.0" Shape="None" GraphId="f6e59" /> </Graphics> <Xref Database="Reactome" ID="REACT_160072" /> </Interaction> <Interaction GraphId="b2851"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1180.0" Y="829.0" GraphRef="ae14a" RelX="-1.1176470588235294" RelY="0.0" /> <Point X="1105.0" Y="829.0" GraphRef="f6e59" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160072" /> </Interaction> <Interaction GraphId="f8abc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1127.0" Y="807.0" GraphRef="f6c67" RelX="7.923076923076923" RelY="10.272727272727273" /> <Point X="1105.0" Y="829.0" GraphRef="f6e59" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160072" /> </Interaction> <Interaction GraphId="a0505"> <Comment Source="Reactome">Lecithin retinol acyltransferase (LRAT) mediates the esterification of all-trans-retinol (atROL) to form all-trans-retinyl esters (atREs). atREs are stored in lipid droplet form called retinosomes (Imanishi et al. 2004). Cellular retinol-binding protein 1 (RBP1) is an effective donor of atROL for LRAT (Ruiz et al. 1999). LRAT is an important enzyme required for the clearance of atROL as it drives the uptake of atROL from the bloodstream through the receptor STRA6 (Kawaguchi et al. 2011) and clearance of atROL from rod outer segments (ROS). In addition, the esterified form of atROL serves as substrate for RPE65.</Comment> <BiopaxRef>acc</BiopaxRef> <BiopaxRef>c6f</BiopaxRef> <BiopaxRef>e37</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1027.0" Y="754.0" /> <Point X="1026.0" Y="697.0" /> <Anchor Position="0.0" Shape="None" GraphId="d756c" /> <Anchor Position="0.99" Shape="None" GraphId="b8c0c" /> <Anchor Position="0.5" Shape="None" GraphId="d92b3" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="d33df"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1027.0" Y="815.0" GraphRef="c3e82" RelX="-0.03896103896103896" RelY="-1.2727272727272727" /> <Point X="1027.0" Y="754.0" GraphRef="d756c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="e5e64"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="957.0" Y="759.0" GraphRef="b46ff" RelX="1.103448275862069" RelY="-0.8666666666666667" /> <Point X="1027.0" Y="754.0" GraphRef="d756c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="a06d0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="957.0" Y="766.0" GraphRef="b46ff" RelX="1.103448275862069" RelY="-0.4" /> <Point X="1027.0" Y="754.0" GraphRef="d756c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="e75c9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1026.0" Y="697.0" GraphRef="b8c0c" RelX="-0.009999999999990905" RelY="-0.57000000000005" /> <Point X="1044.0" Y="650.0" GraphRef="cadc5" RelX="-0.2653061224489796" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="c5cbd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1026.0" Y="697.0" GraphRef="b8c0c" RelX="-0.009999999999990905" RelY="-0.57000000000005" /> <Point X="995.0" Y="695.0" GraphRef="f6c67" RelX="1.1538461538461537" RelY="0.09090909090909091" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="c1242"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1073.0" Y="723.0" GraphRef="e39f1" RelX="-1.1538461538461537" RelY="0.0" /> <Point X="1026.0" Y="723.0" GraphRef="d92b3" RelX="-0.5" RelY="-2.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160266" /> </Interaction> <Interaction GraphId="e761d"> <Comment Source="Reactome">All-trans-retinol esters (atREs) serve as substrates for retinoid isomerohydrolase (RPE65), located in retinal pigment epithelium (RPE) cells. RPE65 hydrolyses atREs to 11-cis-retinol (11cROL), thus performing an isomerase activity as well as hydrolysis. RPE65 is membrane-bound, this being dependent on the palmitylation of the residue Cys-112 (Takahashi et al. 2009). RPE65 normally undergoes a light-dependent translocation to become more concentrated in the central region of RPE cells. This translocation requires Unconventional myosin-VIIa (MYO7A or USH1B) (Lopes et al. 2011).</Comment> <BiopaxRef>f11</BiopaxRef> <BiopaxRef>db8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1059.0" Y="580.0" /> <Point X="1059.0" Y="510.0" /> <Anchor Position="0.0" Shape="None" GraphId="ee307" /> <Anchor Position="0.99" Shape="None" GraphId="d42c0" /> <Anchor Position="0.5" Shape="None" GraphId="d5d7a" /> <Anchor Position="0.5" Shape="None" GraphId="c370d" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="e3e6a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1103.0" Y="581.0" GraphRef="ad5cd" RelX="-1.1395348837209303" RelY="-0.06666666666666667" /> <Point X="1059.0" Y="580.0" GraphRef="ee307" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="ce02f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1052.0" Y="614.0" GraphRef="cadc5" RelX="0.061224489795918366" RelY="-1.2" /> <Point X="1059.0" Y="580.0" GraphRef="ee307" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="e8533"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1059.0" Y="510.0" GraphRef="d42c0" RelX="0.0" RelY="-0.6999999999999886" /> <Point X="1127.0" Y="464.0" GraphRef="bc5c5" RelX="-0.7096774193548387" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="a7a1f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1059.0" Y="510.0" GraphRef="d42c0" RelX="0.0" RelY="-0.6999999999999886" /> <Point X="1002.0" Y="616.0" GraphRef="e41f6" RelX="0.35135135135135137" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="e8ddb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1059.0" Y="510.0" GraphRef="d42c0" RelX="0.0" RelY="-0.6999999999999886" /> <Point X="1017.0" Y="492.0" GraphRef="c6d0d" RelX="-65.77777777777777" RelY="-41.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="a896c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="956.0" Y="541.0" GraphRef="cd6e1" RelX="1.127659574468085" RelY="0.0" /> <Point X="1059.0" Y="541.0" GraphRef="d5d7a" RelX="0.0" RelY="-4.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="fa157"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1104.0" Y="541.0" GraphRef="c544c" RelX="-1.1176470588235294" RelY="0.0" /> <Point X="1059.0" Y="541.0" GraphRef="c370d" RelX="0.0" RelY="-4.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160208" /> </Interaction> <Interaction GraphId="d2dae"> <Comment Source="Reactome">Using NADP+ as cofactor, several members of the short-chain dehydrogenases/reductases (SDR) family can (reversibly) catalyse the oxidation of 11-cis-retinol (11cROL) to 11-cis-retinal (11cRAL) in retinal pigment epithelium (RPE) cells. Retinol dehydrogenases 10 and 11 (RDH10 and 11) are two such members utilizing the cofactor NADP+ (Wu et al. 2002, Kedishvili et al. 2002 respectively). Cellular retinaldehyde-binding protein (RLBP1), the protein bound to 11cRAL in RPE, is not present in photoreceptor cells.</Comment> <BiopaxRef>e89</BiopaxRef> <BiopaxRef>ff3</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1391.0" Y="443.0" /> <Point X="1455.0" Y="443.0" /> <Anchor Position="0.0" Shape="None" GraphId="f7424" /> <Anchor Position="0.99" Shape="None" GraphId="b5b1b" /> <Anchor Position="0.5" Shape="None" GraphId="e6c3d" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="a99d9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1355.0" Y="443.0000000000001" GraphRef="b0e6b" RelX="-10.702127659574469" RelY="-77.27272727272727" /> <Point X="1391.0" Y="443.0" GraphRef="f7424" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="aab3a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1326.0" Y="413.0" GraphRef="c5a60" RelX="-23.8" RelY="-51.0" /> <Point X="1391.0" Y="443.0" GraphRef="f7424" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="f6ee4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1455.0" Y="443.0" GraphRef="b5b1b" RelX="0.6400000000001" RelY="0.0" /> <Point X="1546.0" Y="443.0" GraphRef="c6bc6" RelX="-11.32258064516129" RelY="-77.36363636363636" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="cf0b0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1455.0" Y="443.0" GraphRef="b5b1b" RelX="0.6400000000001" RelY="0.0" /> <Point X="1472.0" Y="421.0" GraphRef="c6d0d" RelX="-40.5" RelY="-45.93333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="aa016"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1455.0" Y="443.0" GraphRef="b5b1b" RelX="0.6400000000001" RelY="0.0" /> <Point X="1510.0" Y="419.0" GraphRef="f643a" RelX="-23.576271186440678" RelY="-50.06666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="f7bf6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1420.0" Y="461.0" GraphRef="e6bba" RelX="-0.0136986301369863" RelY="-1.2727272727272727" /> <Point X="1420.0" Y="443.0" GraphRef="e6c3d" RelX="-3.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160138" /> </Interaction> <Interaction GraphId="dd3db"> <Comment Source="Reactome">Another member of the short-chain dehydrogenases/reductases (SDR) family, RDH5, can (reversibly) catalyse the oxidation of 11-cis-retinol (11cROL) to 11-cis-retinal (11cRAL) in retinal pigment epithelium (RPE) cells using NAD+ as cofactor (Simon et al. 1996, Gonzalez-Fernandez et al. 1999). Cellular retinaldehyde-binding protein (RLBP1), the protein bound to 11cRAL in RPE, is not present in photoreceptor cells.</Comment> <BiopaxRef>f96</BiopaxRef> <BiopaxRef>e2c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1332.0" Y="565.0" /> <Point X="1543.0" Y="565.0" /> <Anchor Position="0.0" Shape="None" GraphId="e26f8" /> <Anchor Position="0.99" Shape="None" GraphId="de788" /> <Anchor Position="0.5" Shape="None" GraphId="e825b" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="c5b5a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1314.0" Y="578.0" GraphRef="b887b" RelX="0.5471698113207547" RelY="-1.2" /> <Point X="1332.0" Y="565.0" GraphRef="e26f8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="cb30a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1307.0" Y="457.0" GraphRef="b0e6b" RelX="-11.72340425531915" RelY="-76.0" /> <Point X="1332.0" Y="565.0" GraphRef="e26f8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="cefec"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1543.0" Y="565.0" GraphRef="de788" RelX="2.1100000000001273" RelY="0.0" /> <Point X="1582.0" Y="554.0" GraphRef="efe8b" RelX="-1.1153846153846154" RelY="0.4" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="c73eb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1543.0" Y="565.0" GraphRef="de788" RelX="2.1100000000001273" RelY="0.0" /> <Point X="1590.0" Y="457.0" GraphRef="c6bc6" RelX="-10.376344086021506" RelY="-76.0909090909091" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="d597b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1543.0" Y="565.0" GraphRef="de788" RelX="2.1100000000001273" RelY="0.0" /> <Point X="1569.0" Y="587.0" GraphRef="c6d0d" RelX="-35.111111111111114" RelY="-34.86666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="d0042"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1428.0" Y="549.0" GraphRef="f2d7b" RelX="-0.06976744186046512" RelY="1.2727272727272727" /> <Point X="1428.0" Y="565.0" GraphRef="e825b" RelX="-9.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160124" /> </Interaction> <Interaction GraphId="a9364"> <Comment Source="Reactome">Interphotoreceptor retinoid-binding protein (RBP3) is the major soluble protein in the interphotoreceptor matrix (IPM) (Liou et al. 1989, Fong &amp; Bridges 1988). It is thought to shuttle 11-cis-retinal (11cRAL) between retinal pigment epithelium (RPE) and photoreceptor outer segments during the visual cycle but the mechanism is poorly understood (Gonzalez-Fernandez &amp; Ghosh 2008). </Comment> <BiopaxRef>bd8</BiopaxRef> <BiopaxRef>b68</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1605.0" Y="429.0" /> <Point X="1763.0" Y="320.0" /> <Anchor Position="0.5" Shape="None" GraphId="ee0b1" /> </Graphics> <Xref Database="Reactome" ID="REACT_160302" /> </Interaction> <Interaction GraphId="eb19a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1695.0" Y="311.0" GraphRef="f5190" RelX="3.1025641025641026" RelY="-88.54545454545455" /> <Point X="1696.0" Y="335.0" GraphRef="ee0b1" RelX="12.0" RelY="-39.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160302" /> </Interaction> <Interaction GraphId="bfd6c"> <Comment Source="Reactome">Human opsin-2 is a G-protein coupled photoreceptor found in the disc membranes of rod outer segments (ROS) (Nathans &amp; Hogness 1984). It is an integral membrane protein and covalently binds the chromophore 11-cis-retinal (11cRAL) to form rhodopsin (RHO). Binding occurs via a protonated Schiff base linkage at Lys-296 (Fan et al. 2002) with Glu-113 at helix 3 serving as the counterion of the protonated Schiff base (Han et al. 1993). 11cRAL is completely embedded within the RHO structure. Opsins found in cone outer segments which bind 11cRAL are described in the cone visual cycle. Unlike other GPCRs in which direct ligand binding activates the receptor, rhodopsin is in an inactive state when bound to 11cRAL (which acts as an inverse agonist).</Comment> <BiopaxRef>c9d</BiopaxRef> <BiopaxRef>ae0</BiopaxRef> <BiopaxRef>c60</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1868.0" Y="368.0" /> <Point X="1916.0" Y="377.0" /> <Anchor Position="0.0" Shape="None" GraphId="b4c73" /> </Graphics> <Xref Database="Reactome" ID="REACT_160240" /> </Interaction> <Interaction GraphId="db5d9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1821.0" Y="382.0" GraphRef="b8a3e" RelX="1.1714285714285715" RelY="-0.45454545454545453" /> <Point X="1868.0" Y="368.0" GraphRef="b4c73" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160240" /> </Interaction> <Interaction GraphId="fd65f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1816.0" Y="332.0" GraphRef="fcea9" RelX="0.639344262295082" RelY="1.2" /> <Point X="1868.0" Y="368.0" GraphRef="b4c73" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160240" /> </Interaction> <Interaction GraphId="bbf5e"> <Comment Source="Reactome">The visual pigment rhodopsin consists of a seven transmembrane helix protein, opsin (RHO), to which an 11-cis-retinal (11cRAL) chromophore is bound as a protonated Schiff base (Hargrave et al. 1983, Nathans &amp; Hogness 1984, Ovchinnikov et al. 1983). The covalent bond between opsin and its retinal ligand, which is unique among G protein coupled receptors, helps to confer extraordinary stability in darkness (Baylor et al. 1984). 11cRAL is an inverse agonist, that quenches the weak ability of opsin to activate transducin G protein (Gt). Upon photon absorption, 11cRAL isomerizes in a few hundred femtoseconds (Schoenlein et al. 1991) and with a high quantum efficiency of 0.7 (Dartnall 1968). Then in the next few milliseconds, opsin undergoes a rearrangement in structure that renders it catalytically active (MII aka metarhodopsin II or R*) (Emeis et al. 1982). The isomerisation is a very fast photochemical process (femtoseconds) followed by slower events (Smith 2010).&lt;br&gt;&lt;br&gt;Mutations in RHO can give rise to autosomal dominant or recessive forms of retinitis pigmentosa or autosomal dominant congenital stationary night blindness (https://sph.uth.edu/retnet/). Retinitis pigmentosa is a progressive form of blindness marked by an initial degeneration of rods, followed by the secondary loss of cones.</Comment> <BiopaxRef>fe5</BiopaxRef> <BiopaxRef>c9d</BiopaxRef> <BiopaxRef>cf6</BiopaxRef> <BiopaxRef>e19</BiopaxRef> <BiopaxRef>ad1</BiopaxRef> <BiopaxRef>d98</BiopaxRef> <BiopaxRef>ba2</BiopaxRef> <BiopaxRef>c1c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2005.0" Y="386.0" /> <Point X="2074.0" Y="386.0" /> <Anchor Position="0.5" Shape="None" GraphId="f53b3" /> </Graphics> <Xref Database="Reactome" ID="REACT_160286" /> </Interaction> <Interaction GraphId="e7d8e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2039.0" Y="133.0" GraphRef="ec1c7" RelX="-14.5" RelY="-108.54545454545455" /> <Point X="2043.0" Y="386.0" GraphRef="f53b3" RelX="3.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160286" /> </Interaction> <Interaction GraphId="cb81a"> <Comment Source="Reactome">Rhodopsin (RHO) is localised to both the disc membrane and the plasma membrane of rod outer segments (ROS). All-trans-retinal (atRAL) released from rhodopsin during the bleaching process, needs to translocate to the cytosol for reduction to all-trans-retinol (atROL) via all-trans-retinol dehydrogenases. Although atRAL can diffuse through membranes unaided, there exists an ABC transporter on disc membranes which may facilitate the transport of excess atRAL. Retinal-specific ATP-binding cassette transporter (ABCA4, ABCR) is the only ABC transporter which mediates the transport of retinoids (Biswas &amp; Biswas 2000). Studies using bovine ABCA4 demonstrates atRAL transport (Sun et al. 1999). Human ABCR was found to be identical to the ABC transporter linked to Stargardt's disease type 1 (STGD1, MIM:248200), a cause of macular degeneration in childhood (Nasonkin et al. 1998).</Comment> <BiopaxRef>a59</BiopaxRef> <BiopaxRef>cfc</BiopaxRef> <BiopaxRef>a0f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2382.0" Y="567.0" /> <Point X="2376.0" Y="622.0" /> <Anchor Position="0.0" Shape="None" GraphId="b9b46" /> <Anchor Position="0.99" Shape="None" GraphId="dc105" /> <Anchor Position="0.5" Shape="None" GraphId="bfd1a" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="c5a56"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2411.0" Y="522.0" GraphRef="f37e3" RelX="9.64" RelY="-17.466666666666665" /> <Point X="2382.0" Y="567.0" GraphRef="b9b46" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="c7902"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2401.0" Y="562.0" GraphRef="c1c5f" RelX="-32.05" RelY="16.333333333333332" /> <Point X="2382.0" Y="567.0" GraphRef="b9b46" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="db6e7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2403.0" Y="582.0" GraphRef="ad5cd" RelX="59.325581395348834" RelY="0.0" /> <Point X="2382.0" Y="567.0" GraphRef="b9b46" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="be239"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2376.0" Y="622.0" GraphRef="dc105" RelX="-0.05999999999994543" RelY="0.5499999999999545" /> <Point X="2360.0" Y="643.0" GraphRef="f8f83" RelX="-43.24390243902439" RelY="21.066666666666666" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="c1186"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2376.0" Y="622.0" GraphRef="dc105" RelX="-0.05999999999994543" RelY="0.5499999999999545" /> <Point X="2391.0" Y="654.0" GraphRef="fb80d" RelX="-22.555555555555557" RelY="22.666666666666668" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="a48ce"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2376.0" Y="622.0" GraphRef="dc105" RelX="-0.05999999999994543" RelY="0.5499999999999545" /> <Point X="2455.0" Y="667.0" GraphRef="d3ffc" RelX="7.88" RelY="-31.733333333333334" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="b2f1a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2356.0" Y="516.0" GraphRef="f553a" RelX="0.08333333333333333" RelY="-24.09090909090909" /> <Point X="2356.0" Y="567.0" GraphRef="bfd1a" RelX="-23.0" RelY="-27.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_111189" /> </Interaction> <Interaction GraphId="a30ac"> <Comment Source="Reactome">The majority of all-trans-retinal (atRAL) simply diffuses across membranes into the cytosol. Experiments performed with mice rods demonstrate that atRAL diffusion is independent of assisted transport by ABCA4 (Mata et al. 2000, Blakeley et al. 2011).</Comment> <BiopaxRef>bc5</BiopaxRef> <BiopaxRef>c12</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2431.0" Y="522.0" /> <Point X="2483.0" Y="664.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160117" /> </Interaction> <Interaction GraphId="a8135"> <Comment Source="Reactome">The reversible, NADP(H)-dependent reduction of all-trans-retinal (atRAL) to all-trans-retinol (atROL) occurs in both rod and cone photoreceptor cells where multiple retinol dehydrogenases (RHDs) are located. RHDs belong to the short-chain dehydrogenase/reductase (SDR) superfamily. RDH12 (located in photoreceptor inner segments) is partially responsible, together with other RDHs, for mediating this reaction (Belyaeva et al. 2005).</Comment> <BiopaxRef>ddb</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2596.0" Y="735.0" /> <Point X="2626.0" Y="839.0" /> <Anchor Position="0.0" Shape="None" GraphId="cd45e" /> <Anchor Position="0.99" Shape="None" GraphId="b7370" /> <Anchor Position="0.5" Shape="None" GraphId="f2328" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="a4747"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2576.0" Y="792.0" GraphRef="c6d0d" RelX="20.833333333333332" RelY="-21.2" /> <Point X="2596.0" Y="735.0" GraphRef="cd45e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="f8e56"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2571.0" Y="747.0" GraphRef="f643a" RelX="12.389830508474576" RelY="-28.2" /> <Point X="2596.0" Y="735.0" GraphRef="cd45e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="f3ff6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2511.0" Y="693.0" GraphRef="d3ffc" RelX="10.12" RelY="-30.0" /> <Point X="2596.0" Y="735.0" GraphRef="cd45e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="c7f31"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2626.0" Y="839.0" GraphRef="b7370" RelX="0.3000000000001819" RelY="1.0399999999999636" /> <Point X="2595.0" Y="886.0" GraphRef="bd891" RelX="0.3333333333333333" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="de1e4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2626.0" Y="839.0" GraphRef="b7370" RelX="0.3000000000001819" RelY="1.0399999999999636" /> <Point X="2609.0" Y="847.0" GraphRef="c5a60" RelX="18.966666666666665" RelY="-22.066666666666666" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="cc2f7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2876.0" Y="922.0" GraphRef="c23c8" RelX="-0.9607843137254902" RelY="-1.2727272727272727" /> <Point X="2616.0" Y="802.0" GraphRef="f2328" RelX="5.0" RelY="15.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160140" /> </Interaction> <Interaction GraphId="ff0ab"> <Comment Source="Reactome">The reversible, NADP(H)-dependent reduction of all-trans-retinal (atRAL) to all-trans-retinol (atROL) occurs in both rod and cone photoreceptor cells where multiple retinol dehydrogenases (RHDs) are located. RHDs belong to the short-chain dehydrogenase/reductase (SDR) superfamily. RDH8 (located in photoreceptor outer segments) is partially responsible, together with other RDHs, for mediating this reaction. The activity for human RDH8 is inferred from a bovine experiment (Rattner et al. 2000).</Comment> <BiopaxRef>d8a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2482.0" Y="761.0" /> <Point X="2519.0" Y="852.0" /> <Anchor Position="0.0" Shape="None" GraphId="a1897" /> <Anchor Position="0.99" Shape="None" GraphId="ef7f1" /> <Anchor Position="0.5" Shape="None" GraphId="e10a0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="c8ddb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2482.0" Y="700.0" GraphRef="d3ffc" RelX="8.96" RelY="-29.533333333333335" /> <Point X="2482.0" Y="761.0" GraphRef="a1897" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="ba7e4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2551.0" Y="800.0" GraphRef="c6d0d" RelX="19.444444444444443" RelY="-20.666666666666668" /> <Point X="2482.0" Y="761.0" GraphRef="a1897" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="c2e1f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2515.0" Y="763.0" GraphRef="f643a" RelX="10.491525423728813" RelY="-27.133333333333333" /> <Point X="2482.0" Y="761.0" GraphRef="a1897" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="d0e17"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2519.0" Y="852.0" GraphRef="ef7f1" RelX="0.36999999999989086" RelY="0.9099999999999682" /> <Point X="2566.0" Y="886.0" GraphRef="bd891" RelX="-0.803921568627451" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="e1261"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2519.0" Y="852.0" GraphRef="ef7f1" RelX="0.36999999999989086" RelY="0.9099999999999682" /> <Point X="2543.0" Y="855.0" GraphRef="c5a60" RelX="16.766666666666666" RelY="-21.533333333333335" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="aee53"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2507.0" Y="920.0" GraphRef="a10ec" RelX="-0.06976744186046512" RelY="-1.2727272727272727" /> <Point X="2507.0" Y="824.0" GraphRef="e10a0" RelX="6.5" RelY="17.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160121" /> </Interaction> <Interaction GraphId="f1520"> <Comment Source="Reactome">Although interphotoreceptor retinoid-binding protein (RBP3, IRBP) (Fong &amp; Bridges 1988, Fong et al. 1990) is not required to move all-trans-retinol (atROL) from photoreceptor cells to the retinal pigment epithelium (RPE), it may function to regulate retinoid trafficking and possibly protect retinoids from biochemical damage. RBP3 is secreted by photoreceptor cells into the interphotoreceptor matrix (IPM), where, being a larger protein (135kDa) than the IPM space, becomes trapped (see mini-review Gonzalez-Fernandez &amp; Ghosh 2008). It is through this space that retinoids move between the RPE and photoreceptor outer segments during the retinoid cycle. Once atROL enters the RPE, it binds with RBP1.</Comment> <BiopaxRef>b68</BiopaxRef> <BiopaxRef>dcc</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2584.0" Y="922.0" /> <Point X="1237.0" Y="829.0" /> <Anchor Position="0.5" Shape="None" GraphId="b3d55" /> </Graphics> <Xref Database="Reactome" ID="REACT_160091" /> </Interaction> <Interaction GraphId="ff3af"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1700.0" Y="864.0" GraphRef="f5190" RelX="3.358974358974359" RelY="-38.27272727272727" /> <Point X="1699.0" Y="885.0" GraphRef="b3d55" RelX="-211.5" RelY="9.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160091" /> </Interaction> <Interaction GraphId="edfb0"> <Comment Source="Reactome">All-trans-retinol (atROL), the product of the reduction of all-trans-retinal (atRAL) released from rod and cone opsins, needs to be regenerated back to the visual chromophore 11-cis-retinal (11cRAL). For the regenerative steps, rods transports atROL back into the retinal pigment epithelium (RPE) while cones utilise Muller cells. Although interphotoreceptor retinoid-binding protein (RBP3, IRBP) (Fong &amp; Bridges 1988, Fong et al. 1990) is not thought to be required to move all-trans-retinol (atROL) from photoreceptor cells to the retinal pigment epithelium (RPE) or Muller cells, it may function to regulate retinoid trafficking and possibly protect retinoids from biochemical damage. RBP3 is secreted by photoreceptor cells into the interphotoreceptor matrix (IPM), where, being a larger protein (135kDa) than the IPM space, becomes trapped (see mini-review Gonzalez-Fernandez &amp; Ghosh 2008). It is through this space that retinoids move between Muller cells and cone photoreceptor outer segments during the cone retinoid cycle.</Comment> <BiopaxRef>b68</BiopaxRef> <BiopaxRef>dcc</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1975.0" Y="1126.0" /> <Point X="1555.0" Y="1014.0" /> <Anchor Position="0.5" Shape="None" GraphId="b7074" /> </Graphics> <Xref Database="Reactome" ID="REACT_160292" /> </Interaction> <Interaction GraphId="cb955"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1639.0" Y="1096.0" GraphRef="f5190" RelX="0.23076923076923078" RelY="-17.181818181818183" /> <Point X="1640.0" Y="1126.0" GraphRef="b7074" RelX="-125.0" RelY="56.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160292" /> </Interaction> <Interaction GraphId="c4c51"> <Comment Source="Reactome">The canonical rod retinoid (visual) cycle is too slow to account for the photosensitivity of cones in bright light conditions. Novel enzyme activities demonstrated in ground-squirrel and chicken retinas produce a novel pathway of chromophore regeneration specific for cones. The first reaction in Muller cells, the isomerization of all-trans-retinol (atROL) to 11-cis-retinol (11cROL), is mediated by an as-yet-uncharacterised atROL isomerase (Mata et al. 2002, Mata et al. 2005). This reaction is proposed to take place in all vertebrates including humans (Wang &amp; Kefalov 2009).</Comment> <BiopaxRef>f2c</BiopaxRef> <BiopaxRef>b93</BiopaxRef> <BiopaxRef>ee7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1343.0" Y="996.0" /> <Point X="1194.0" Y="1064.0" /> <Anchor Position="0.5" Shape="None" GraphId="f98c4" /> </Graphics> <Xref Database="Reactome" ID="REACT_160148" /> </Interaction> <Interaction GraphId="f14e2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1302.0" Y="1035.0" GraphRef="f3799" RelX="0.0" RelY="-1.2727272727272727" /> <Point X="1302.0" Y="995.0" GraphRef="f98c4" RelX="33.5" RelY="-35.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160148" /> </Interaction> <Interaction GraphId="b601c"> <Comment Source="Reactome">This human event has been inferred from an as-yet-uncharacterised protein which has been demonstrated to possess retinyl ester hydrolase (REH) activity in chicken retina to hydrolyse 11-cis-retinyl palmitate (11cRPALM) to 11-cis-retinol (11cROL) (Bustamante et al. 1995).</Comment> <BiopaxRef>aae</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1320.0" Y="1271.0" /> <Point X="1398.0" Y="1272.0" /> <Anchor Position="0.0" Shape="None" GraphId="a2998" /> <Anchor Position="0.99" Shape="None" GraphId="f3b12" /> <Anchor Position="0.5" Shape="None" GraphId="f5855" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="fe95f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1290.0" Y="1259.0" GraphRef="c6d5b" RelX="0.7435897435897436" RelY="1.2" /> <Point X="1320.0" Y="1271.0" GraphRef="a2998" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="b2a5b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1289.0" Y="1280.0" GraphRef="ad5cd" RelX="7.511627906976744" RelY="46.53333333333333" /> <Point X="1320.0" Y="1271.0" GraphRef="a2998" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="e5a5d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1398.0" Y="1272.0" GraphRef="f3b12" RelX="0.7799999999999727" RelY="0.009999999999990905" /> <Point X="1463.0" Y="1272.0" GraphRef="baa59" RelX="-1.096774193548387" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="d956c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1398.0" Y="1272.0" GraphRef="f3b12" RelX="0.7799999999999727" RelY="0.009999999999990905" /> <Point X="1431.0" Y="1298.0" GraphRef="c6d0d" RelX="-42.77777777777778" RelY="12.533333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="fc22f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1398.0" Y="1272.0" GraphRef="f3b12" RelX="0.7799999999999727" RelY="0.009999999999990905" /> <Point X="1429.0" Y="1233.0" GraphRef="bdc58" RelX="-0.5" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="db6f5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1357.0" Y="1330.0" GraphRef="a4802" RelX="-0.030303030303030304" RelY="-1.2727272727272727" /> <Point X="1357.0" Y="1272.0" GraphRef="f5855" RelX="-2.0" RelY="0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160228" /> </Interaction> <Interaction GraphId="de91f"> <Comment Source="Reactome">The transfer of 11-cis-retinol (11cROL) from Muller cells to cone photoreceptor cells is thought to be mediated by interphotoreceptor retinoid-binding protein RBP3 (Liou et al. 1989, Fong &amp; Bridges 1988) but the mechanism is poorly understood (Gonzalez-Fernandez &amp; Ghosh 2008). </Comment> <BiopaxRef>bd8</BiopaxRef> <BiopaxRef>b68</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1531.0" Y="1284.0" /> <Point X="1690.0" Y="1327.0" /> <Anchor Position="0.5" Shape="None" GraphId="d7cde" /> </Graphics> <Xref Database="Reactome" ID="REACT_160222" /> </Interaction> <Interaction GraphId="a1203"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1635.0" Y="1299.0" GraphRef="f5190" RelX="0.02564102564102564" RelY="1.2727272727272727" /> <Point X="1638.0" Y="1327.0" GraphRef="d7cde" RelX="27.5" RelY="21.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160222" /> </Interaction> <Interaction GraphId="c1236"> <Comment Source="Reactome">Cellular retinaldehyde-binding protein (RLBP1, CRALBP) (Intres et al. 1994) is abundant in retinal pigment epithelium (RPE) and Muller cells of the retina where it plays a role in sequestering 11-cis retinoids produced during the retinoid cycle. The natural ligands are 11-cis-retinol (11cROL) and 11-cis-retinal (11cRAL) (Crabb et al. 1998).</Comment> <BiopaxRef>ee3</BiopaxRef> <BiopaxRef>b00</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1764.0" Y="1286.0" /> <Point X="1808.0" Y="1292.0" /> <Anchor Position="0.0" Shape="None" GraphId="d9c4f" /> </Graphics> <Xref Database="Reactome" ID="REACT_160184" /> </Interaction> <Interaction GraphId="a8ff8"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1738.0" Y="1310.0" GraphRef="d4063" RelX="0.45161290322580644" RelY="-1.2" /> <Point X="1764.0" Y="1286.0" GraphRef="d9c4f" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160184" /> </Interaction> <Interaction GraphId="bb93c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1749.0" Y="1280.0" GraphRef="a6071" RelX="0.7777777777777778" RelY="1.2727272727272727" /> <Point X="1764.0" Y="1286.0" GraphRef="d9c4f" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160184" /> </Interaction> <Interaction GraphId="b43f4"> <Comment Source="Reactome">11-cis-specific retinol dehydrogenase (11cRDH) activity found in chicken retina mediates the oxidation of 11-cis-retinol (11cROL) to 11-cis-retinal (11cRAL) using NADP+ as cofactor (Mata et al. 2002). The chicken protein that possesses this activity has not yet been identified. The actual enzyme responsible remains to be identified in human, even as evidence exists for this activity and for the alternative retinoid (visual) cycle in cones (Wang &amp; Kefalov 2009). 11cRAL is the visual chromophore that is able to bind to opsins.</Comment> <BiopaxRef>ee7</BiopaxRef> <BiopaxRef>b93</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1919.0" Y="1293.0" /> <Point X="1972.0" Y="1293.0" /> <Anchor Position="0.0" Shape="None" GraphId="e8723" /> <Anchor Position="0.99" Shape="None" GraphId="a3f55" /> <Anchor Position="0.5" Shape="None" GraphId="e99f1" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="e4b42"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1908.0" Y="1293.0" GraphRef="b0e6b" RelX="1.0638297872340425" RelY="0.0" /> <Point X="1919.0" Y="1293.0" GraphRef="e8723" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="a92cc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1892.0" Y="1312.0" GraphRef="c5a60" RelX="-4.933333333333334" RelY="8.933333333333334" /> <Point X="1919.0" Y="1293.0" GraphRef="e8723" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="ba9a1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1972.0" Y="1293.0" GraphRef="a3f55" RelX="0.5299999999999727" RelY="0.0" /> <Point X="2023.0" Y="1293.0" GraphRef="c6bc6" RelX="-1.064516129032258" RelY="-0.09090909090909091" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="c0157"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1972.0" Y="1293.0" GraphRef="a3f55" RelX="0.5299999999999727" RelY="0.0" /> <Point X="1992.0" Y="1282.0" GraphRef="f643a" RelX="-7.237288135593221" RelY="7.466666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="f5a47"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1972.0" Y="1293.0" GraphRef="a3f55" RelX="0.5299999999999727" RelY="0.0" /> <Point X="1991.0" Y="1307.0" GraphRef="c6d0d" RelX="-11.666666666666666" RelY="13.133333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="ab297"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1938.0" Y="1261.0" GraphRef="e4240" RelX="-0.017543859649122806" RelY="1.2727272727272727" /> <Point X="1938.0" Y="1293.0" GraphRef="e99f1" RelX="-7.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160139" /> </Interaction> <Interaction GraphId="bfb9e"> <Comment Source="Reactome">Upon photon absorption, 11-cis-retinal (11cRAL) is isomerised to all-trans-retinal (atRAL). The structure of cone opsins which can ultimately activate G-proteins to initiate phototransduction is denoted as R* (Fan et al. 2002). R* is still bound to atRAL at this stage. The isomerisation is a very fast photochemical process (femtoseconds) (Schoenlein et al. 1991) followed by slower events described in the following reaction.</Comment> <BiopaxRef>c60</BiopaxRef> <BiopaxRef>fe5</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2270.0" Y="1337.0" /> <Point X="2316.0" Y="1293.0" /> <Anchor Position="0.5" Shape="None" GraphId="a9cd8" /> </Graphics> <Xref Database="Reactome" ID="REACT_160165" /> </Interaction> <Interaction GraphId="cc01f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2360.0" Y="1326.0" GraphRef="ec1c7" RelX="-1.125" RelY="-0.09090909090909091" /> <Point X="2316.0" Y="1326.0" GraphRef="a9cd8" RelX="23.0" RelY="11.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160165" /> </Interaction> <Interaction GraphId="bffc9"> <Comment Source="Reactome">After the very fast isomerisation of 11-cis-retinal (11cRAL) to all-trans-retinal (atRAL) by light stimulation, slower events lead to exposure of atRAL to the aqueous environment, resulting in the hydrolysis of the Schiff base linkage. Although other intermediate products are formed, the ultimate result is the release of atRAL from opsins, which returns to the apo-opsin form (Baumann &amp; Bender 1973). These series of slow decay reactions are called light bleaching of opsin and ends when atRAL, which can diffuse across membranes to the cytosol, is reduced to all-trans-retinol (atROL)</Comment> <BiopaxRef>b0e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2258.0" Y="1248.0" /> <Point X="2258.0" Y="1193.0" /> <Anchor Position="0.0" Shape="None" GraphId="a649d" /> <Anchor Position="0.99" Shape="None" GraphId="d8b3d" /> </Graphics> <Xref Database="Reactome" ID="REACT_160146" /> </Interaction> <Interaction GraphId="e46c7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2296.0" Y="1265.0" GraphRef="c3224" RelX="-0.3620689655172414" RelY="-1.2727272727272727" /> <Point X="2258.0" Y="1248.0" GraphRef="a649d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160146" /> </Interaction> <Interaction GraphId="be66b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2243.0" Y="1262.0" GraphRef="ad5cd" RelX="51.883720930232556" RelY="45.333333333333336" /> <Point X="2258.0" Y="1248.0" GraphRef="a649d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160146" /> </Interaction> <Interaction GraphId="ff53b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2258.0" Y="1193.0" GraphRef="d8b3d" RelX="0.0" RelY="-0.5499999999999545" /> <Point X="2121.0" Y="1335.0" GraphRef="c2088" RelX="0.18518518518518517" RelY="-1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160146" /> </Interaction> <Interaction GraphId="d1b27"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2258.0" Y="1193.0" GraphRef="d8b3d" RelX="0.0" RelY="-0.5499999999999545" /> <Point X="2258.0" Y="1161.0" GraphRef="d3ffc" RelX="0.0" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160146" /> </Interaction> <Interaction GraphId="cf132"> <Comment Source="Reactome">All-trans-retinal (atRAL) can diffuse across membranes to the cytosol and is reduced to all-trans-retinol (atROL) by the action of a short-chain dehydrogenase/reductase 3 using NADP+/NADPH as cofactor (Haeseleer et al. 1998).</Comment> <BiopaxRef>e2e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2175.0" Y="1142.0" /> <Point X="2066.0" Y="1142.0" /> <Anchor Position="0.0" Shape="None" GraphId="ae999" /> <Anchor Position="0.99" Shape="None" GraphId="ff07f" /> <Anchor Position="0.5" Shape="None" GraphId="d648a" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="c2cff"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2230.0" Y="1142.0" GraphRef="d3ffc" RelX="-1.12" RelY="-0.06666666666666667" /> <Point X="2175.0" Y="1142.0" GraphRef="ae999" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="fde5c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2188.0" Y="1152.0" GraphRef="f643a" RelX="-0.5932203389830508" RelY="-1.2" /> <Point X="2175.0" Y="1142.0" GraphRef="ae999" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="fd951"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2188.0" Y="1128.0" GraphRef="c6d0d" RelX="-0.7222222222222222" RelY="1.2" /> <Point X="2175.0" Y="1142.0" GraphRef="ae999" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="f5983"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2066.0" Y="1142.0" GraphRef="ff07f" RelX="-1.0900000000001455" RelY="0.0" /> <Point X="2032.0" Y="1132.0" GraphRef="a3aeb" RelX="1.1176470588235294" RelY="0.4" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="ea6d5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2066.0" Y="1142.0" GraphRef="ff07f" RelX="-1.0900000000001455" RelY="0.0" /> <Point X="2050.0" Y="1160.0" GraphRef="c5a60" RelX="0.3333333333333333" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="d4e6d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2137.0" Y="1104.0" GraphRef="aee82" RelX="-0.02040816326530612" RelY="1.2727272727272727" /> <Point X="2137.0" Y="1142.0" GraphRef="d648a" RelX="16.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160119" /> </Interaction> <Interaction GraphId="d4031"> <Comment Source="Reactome">Bovine studies (Beharry et al. 2004) have indicated NRPE to be the preferred substrate for ABCA4 (ABCR, rim protein, RmP) (Azarian et al. 1998), which acts an inward-directed retinoid flippase and facilitates the transfer of NRPE to the cytoplasmic side of the disc membrane. This transfer is essential to avoid build up of potentially toxic retinoid intermediates which are implicated in many retinal degenerative diseases (see review Tsybovsky et al. 2010). Defective ABCA4 cannot perform this function leading to impaired vision and blindness disorders such as Stargardt disease (MIM:248200).</Comment> <BiopaxRef>e78</BiopaxRef> <BiopaxRef>d72</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2326.0" Y="898.0" /> <Point X="2382.0" Y="898.0" /> <Anchor Position="0.0" Shape="None" GraphId="fc7fc" /> <Anchor Position="0.99" Shape="None" GraphId="d2f35" /> <Anchor Position="0.5" Shape="None" GraphId="e0062" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="e18de"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2306.0" Y="871.0" GraphRef="c1c5f" RelX="-36.8" RelY="36.93333333333333" /> <Point X="2326.0" Y="898.0" GraphRef="fc7fc" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="f8f2a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2291.0" Y="888.0" GraphRef="ad5cd" RelX="54.116279069767444" RelY="20.4" /> <Point X="2326.0" Y="898.0" GraphRef="fc7fc" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="c2959"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2232.0" Y="926.0" GraphRef="c8252" RelX="1.125" RelY="-0.4666666666666667" /> <Point X="2326.0" Y="898.0" GraphRef="fc7fc" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="ac9c1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2382.0" Y="898.0" GraphRef="d2f35" RelX="0.5599999999999454" RelY="0.0" /> <Point X="2423.0" Y="834.0" GraphRef="bc88a" RelX="-0.4166666666666667" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="f2bef"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2382.0" Y="898.0" GraphRef="d2f35" RelX="0.5599999999999454" RelY="0.0" /> <Point X="2439.0" Y="900.0" GraphRef="fb80d" RelX="-19.0" RelY="39.06666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="fcaa5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2382.0" Y="898.0" GraphRef="d2f35" RelX="0.5599999999999454" RelY="0.0" /> <Point X="2437.0" Y="872.0" GraphRef="f8f83" RelX="-39.48780487804878" RelY="36.333333333333336" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="fcb90"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2354.0" Y="795.0" GraphRef="f553a" RelX="0.0" RelY="1.2727272727272727" /> <Point X="2354.0" Y="898.0" GraphRef="e0062" RelX="0.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160211" /> </Interaction> <Interaction GraphId="e7570"> <Comment Source="Reactome">Once NRPE is "flipped" to the cytoplasmic side of disc membranes by the ABC transporter ABCA4, it can dissociate to all-trans-retinal (atRAL) and phosphatidylethanolamine (PE). atRAL is thus released to re-enter the retinoid cycle to reform the visual chromophore 11-cis-retinal (11cRAL) (Tsybovsky et al. 2010).</Comment> <BiopaxRef>b51</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2428.0" Y="798.0" /> <Point X="2407.0" Y="716.0" /> <Anchor Position="0.99" Shape="None" GraphId="cc297" /> </Graphics> <Xref Database="Reactome" ID="REACT_160267" /> </Interaction> <Interaction GraphId="aa514"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2407.0" Y="716.0" GraphRef="cc297" RelX="-0.21000000000003638" RelY="-0.8199999999999363" /> <Point X="2256.0" Y="772.0" GraphRef="e20b4" RelX="1.1764705882352942" RelY="-0.4666666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160267" /> </Interaction> <Interaction GraphId="edf1c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2407.0" Y="716.0" GraphRef="cc297" RelX="-0.21000000000003638" RelY="-0.8199999999999363" /> <Point X="2455.0" Y="693.0" GraphRef="d3ffc" RelX="7.88" RelY="-30.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160267" /> </Interaction> <Interaction GraphId="e2977"> <Comment Source="Reactome">In darkness, the G protein transducin (Gt) is attached to the disk membrane surface with a GDP bound to it and it is inactive. Gt is a heterotrimer of alpha1 (GNAT1) (van Dop et al. 1989, Fong 1992), beta1 (GNB1) (Codina et al. 1986) and gamma1 (GNGT1) (Tao et al. 1993) subunits. Photoactivated rhodopsin (MII or R*) catalyzes the exchange of GTP for GDP bound to Gt. Upon GTP/GDP exchange, Gt is released from MII and the Gt alpha with GTP bound (GNAT1 GTP) dissociates from Gt beta gamma subunits (GNB1:GNGT1). This mechanism was deciphered from bovine experiments (Pugh &amp; Lamb 1993). MII proceeds to activate additional Gt molecules, making this reaction the first amplification step in the phototransduction cascade. A single activated rhodopsin molecule activates tens of Gt molecules. Defects in GNAT1 cause the Nougaret type of autosomal dominant, congenital stationary night blindness (Dryja et al. 1996, CSNBAD3; MIM:610444) . Congenital stationary night blindness is a non progressive retinal disorder characterized by impaired night vision.</Comment> <BiopaxRef>d9c</BiopaxRef> <BiopaxRef>f61</BiopaxRef> <BiopaxRef>aef</BiopaxRef> <BiopaxRef>bae</BiopaxRef> <BiopaxRef>f95</BiopaxRef> <BiopaxRef>bf7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2213.0" Y="386.0" /> <Point X="2262.0" Y="386.0" /> <Anchor Position="0.0" Shape="None" GraphId="d29d9" /> <Anchor Position="0.99" Shape="None" GraphId="befb3" /> <Anchor Position="0.5" Shape="None" GraphId="d6051" /> </Graphics> <Xref Database="Reactome" ID="REACT_163833" /> </Interaction> <Interaction GraphId="d5393"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2198.0" Y="386.0" GraphRef="a0038" RelX="1.1111111111111112" RelY="-0.09090909090909091" /> <Point X="2213.0" Y="386.0" GraphRef="d29d9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163833" /> </Interaction> <Interaction GraphId="b509d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2205.0" Y="370.0" GraphRef="db2cb" RelX="-66.07317073170732" RelY="3.8" /> <Point X="2213.0" Y="386.0" GraphRef="d29d9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163833" /> </Interaction> <Interaction GraphId="a1346"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2262.0" Y="386.0" GraphRef="befb3" RelX="0.4899999999997817" RelY="0.0" /> <Point X="2288.0" Y="365.0" GraphRef="cc2ea" RelX="-1.1428571428571428" RelY="0.9333333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163833" /> </Interaction> <Interaction GraphId="eb06f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2262.0" Y="386.0" GraphRef="befb3" RelX="0.4899999999997817" RelY="0.0" /> <Point X="2293.0" Y="386.0" GraphRef="d6739" RelX="-1.1132075471698113" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163833" /> </Interaction> <Interaction GraphId="fe3a4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2105.0" Y="391.0" GraphRef="b5aa2" RelX="1.24" RelY="0.36363636363636365" /> <Point X="2238.0" Y="386.0" GraphRef="d6051" RelX="0.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163833" /> </Interaction> <Interaction GraphId="a7586"> <Comment Source="Reactome">Binding of transducin (Gt) to activated rhodopsin (MII) promotes the release of GDP from the Gt alpha subunit enabling a GTP (present in a higher concentration than GDP) to take its place. With GTP bound, Gt alpha (GNAT1-GTP) dissociates from the Gt beta:gamma subunits (GNB1:GNGT1) and from MII. MII is then available to bind and activate additional transducins. Transducin activation is the first amplifying step in visual transduction. Many findings came from bovine experiments (Pugh &amp; Lamb 1993, Fung &amp; Stryer 1980, Fung et al. 1981, Hofmann 1985).</Comment> <BiopaxRef>bf7</BiopaxRef> <BiopaxRef>e09</BiopaxRef> <BiopaxRef>b70</BiopaxRef> <BiopaxRef>ac4</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2352.0" Y="380.0" /> <Point X="2380.0" Y="373.0" /> <Anchor Position="0.99" Shape="None" GraphId="f9cae" /> </Graphics> <Xref Database="Reactome" ID="REACT_163674" /> </Interaction> <Interaction GraphId="c5d38"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2380.0" Y="373.0" GraphRef="f9cae" RelX="0.2800000000002001" RelY="-0.06999999999999318" /> <Point X="2424.0" Y="397.0" GraphRef="e7eb2" RelX="-0.5056179775280899" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163674" /> </Interaction> <Interaction GraphId="a9d87"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2380.0" Y="373.0" GraphRef="f9cae" RelX="0.2800000000002001" RelY="-0.06999999999999318" /> <Point X="2512.0" Y="373.0" GraphRef="ede94" RelX="-1.0731707317073171" RelY="-0.8181818181818182" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163674" /> </Interaction> <Interaction GraphId="ba5bf"> <Comment Source="Reactome">The membrane associated cGMP phosphodiesterase 6 (PDE6) is a tetramer of two catalytic chains, alpha (PDE6A or PDEA) (Pittler et al. 1990) and beta (PDE6B or PDEB) (Weber et al. 1991), and two inhibitory gamma chains (PDE6G or PDEG) (Tuteja et al. 1990). Binding of an activated transducin alpha subunit (GNAT1-GTP) to PDE-gamma relaxes the inhibitory effect of the gamma subunit thereby activating the associated alpha or beta catalytic subunit. Because the binding of GNAT1-GTP to PDE-gamma is one to one, there is no amplification associated with this step. Some forms of autosomal recessive retinitis pigmentosa and congenital stationary night blindness are caused by mutations in PDE6 (https://sph.uth.edu/retnet/).&lt;br&gt;</Comment> <BiopaxRef>a8e</BiopaxRef> <BiopaxRef>af4</BiopaxRef> <BiopaxRef>f70</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2663.0" Y="454.0" /> <Point X="2798.0" Y="403.0" /> <Anchor Position="0.0" Shape="None" GraphId="fa188" /> </Graphics> <Xref Database="Reactome" ID="REACT_163927" /> </Interaction> <Interaction GraphId="f4225"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2572.0" Y="396.0" GraphRef="ede94" RelX="0.3902439024390244" RelY="1.2727272727272727" /> <Point X="2663.0" Y="454.0" GraphRef="fa188" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163927" /> </Interaction> <Interaction GraphId="db77a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2635.0" Y="397.0" GraphRef="b6c00" RelX="0.25" RelY="1.2727272727272727" /> <Point X="2663.0" Y="454.0" GraphRef="fa188" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163927" /> </Interaction> <Interaction GraphId="ba53a"> <Comment Source="Reactome">Phosphodiesterase 6 (PDE6, Pittler et al. 1990, Tuteja et al. 1990, Weber et al. 1991) undergoes brief, spontaneous activations every few minutes to sustain a low, basal rate of 3',5' cyclic GMP (cGMP) hydrolysis to 5’ GMP (Cobbs 1991, Dawis et al. 1988, Hodgkin &amp; Nunn 1988, Rieke &amp; Baylor 1996, Wensel &amp; Stryer 1986). However, activated transducin (GNAT1 GTP) sustains PDE6 activation allowing it to hydrolyze cGMP at a rate limited only by diffusional access to substrate (Chader et al. 1974, Goridis &amp; Virmaux 1974, Miki et al. 1973). This event represents another amplification step in the phototransduction cascade wherein activated PDE6 hydrolyzes thousands of cGMP molecules per second. The decline in intracellular cGMP levels results in the closure of cyclic nucleotide gated cation channels (CNG channels). Mutations in the PDE6 subunits can cause retinitis pigmentosa or congenital stationary night blindness (https://sph.uth.edu/retnet/).</Comment> <BiopaxRef>af4</BiopaxRef> <BiopaxRef>f70</BiopaxRef> <BiopaxRef>a8e</BiopaxRef> <BiopaxRef>a55</BiopaxRef> <BiopaxRef>ef9</BiopaxRef> <BiopaxRef>e21</BiopaxRef> <BiopaxRef>c3d</BiopaxRef> <BiopaxRef>ea5</BiopaxRef> <BiopaxRef>fdb</BiopaxRef> <BiopaxRef>d38</BiopaxRef> <BiopaxRef>c1f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3008.0" Y="276.0" /> <Point X="2789.0" Y="276.0" /> <Anchor Position="0.0" Shape="None" GraphId="ec344" /> <Anchor Position="0.5" Shape="None" GraphId="f7a4b" /> </Graphics> <Xref Database="Reactome" ID="REACT_163760" /> </Interaction> <Interaction GraphId="fee2a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2990.0" Y="296.0" GraphRef="ad5cd" RelX="86.62790697674419" RelY="-19.066666666666666" /> <Point X="3008.0" Y="276.0" GraphRef="ec344" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163760" /> </Interaction> <Interaction GraphId="c647e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3118.0" Y="276.0" GraphRef="c1cf8" RelX="-1.1224489795918366" RelY="0.0" /> <Point X="3008.0" Y="276.0" GraphRef="ec344" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163760" /> </Interaction> <Interaction GraphId="b14aa"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2825.0" Y="375.0" GraphRef="e2a72" RelX="-0.02564102564102564" RelY="-1.2727272727272727" /> <Point X="2825.0" Y="276.0" GraphRef="f7a4b" RelX="-73.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163760" /> </Interaction> <Interaction GraphId="fd2f6"> <Comment Source="Reactome">As cGMP is hydrolysed during the activation phase of phototransduction, its intracellular concentration decreases leading to the closure of CNG channel (the closed status is designated as CNG channel) (Dhallan et al. 1992, Chen et al. 1993). Channel closure reduces the inward flux of sodium and calcium (also known as the 'dark current') resulting in cell hyperpolarisation. Cooperative binding of cGMP to the CNG channel confers additional amplification to the phototransduction cascade (Pugh &amp; Lamb 1993, Yau &amp; Baylor 1989).</Comment> <BiopaxRef>d44</BiopaxRef> <BiopaxRef>cac</BiopaxRef> <BiopaxRef>bf7</BiopaxRef> <BiopaxRef>e7f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3125.0" Y="149.0" /> <Point X="3095.0" Y="148.0" /> <Anchor Position="0.99" Shape="None" GraphId="dac54" /> </Graphics> <Xref Database="Reactome" ID="REACT_163894" /> </Interaction> <Interaction GraphId="e799b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3095.0" Y="148.0" GraphRef="dac54" RelX="-0.3000000000001819" RelY="-0.009999999999990905" /> <Point X="3056.0" Y="148.0" GraphRef="ae270" RelX="1.072289156626506" RelY="-0.09090909090909091" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163894" /> </Interaction> <Interaction GraphId="bcc9c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3095.0" Y="148.0" GraphRef="dac54" RelX="-0.3000000000001819" RelY="-0.009999999999990905" /> <Point X="3118.0" Y="265.0" GraphRef="c1cf8" RelX="-1.1224489795918366" RelY="-0.7333333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163894" /> </Interaction> <Interaction GraphId="d4ee5"> <Comment Source="Reactome">The cGMP-gated (CNG) channels are heterotetramers of three alpha subunits (CNGA1) and one beta subunit (CNGB1). Although the subunits bear structural similarities to voltage-gated potassium channels, the rod channel is only weakly voltage sensitive (Chen et al. 1993). Opening occurs with cGMP bound and rarely occurs in the absence of cGMP (hence the closed state is designated as CNG channel and the open status is designated as cGMP:CNG channel). In darkness, cGMP concentration is relatively high and cGMP-gated cation (CNG) channels are open to allow the influx of cations into the rod outer segment. The inward current is composed mainly of Na+ ions, with lesser contributions from Ca2+ ions and Mg2+ ions (Dhallan et al. 1992). The channel is outwardly rectifying so that over physiological membrane potentials, the inward current is proportional to the number of channels open and is nearly independent of voltage. Mutations in the CNG channel subunits can cause a recessive form of retinitis pigmentosa (https://sph.uth.edu/retnet/).</Comment> <BiopaxRef>cac</BiopaxRef> <BiopaxRef>d44</BiopaxRef> <BiopaxRef>dac</BiopaxRef> <BiopaxRef>b57</BiopaxRef> <BiopaxRef>f02</BiopaxRef> <BiopaxRef>f42</BiopaxRef> <BiopaxRef>e35</BiopaxRef> <BiopaxRef>cb3</BiopaxRef> <BiopaxRef>eb4</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3282.0" Y="124.0" /> <Point X="3279.0" Y="180.0" /> <Anchor Position="0.0" Shape="None" GraphId="dcd76" /> <Anchor Position="0.99" Shape="None" GraphId="ae99b" /> <Anchor Position="0.5" Shape="None" GraphId="c794d" /> </Graphics> <Xref Database="Reactome" ID="REACT_163682" /> </Interaction> <Interaction GraphId="bc41a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3264.0" Y="112.0" GraphRef="ddfa0" RelX="-5.604651162790698" RelY="2.0" /> <Point X="3282.0" Y="124.0" GraphRef="dcd76" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163682" /> </Interaction> <Interaction GraphId="daa60"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3303.0" Y="106.0" GraphRef="d5eba" RelX="-8.88" RelY="0.6" /> <Point X="3282.0" Y="124.0" GraphRef="dcd76" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163682" /> </Interaction> <Interaction GraphId="d264e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3279.0" Y="180.0" GraphRef="ae99b" RelX="-0.03000000000020009" RelY="0.5600000000000023" /> <Point X="3265.0" Y="207.0" GraphRef="abfcd" RelX="-11.046511627906977" RelY="0.06666666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163682" /> </Interaction> <Interaction GraphId="b2e7e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3279.0" Y="180.0" GraphRef="ae99b" RelX="-0.03000000000020009" RelY="0.5600000000000023" /> <Point X="3320.0" Y="210.0" GraphRef="bee2f" RelX="31.8" RelY="-22.533333333333335" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163682" /> </Interaction> <Interaction GraphId="e1ef9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3250.0" Y="151.0" GraphRef="b54b5" RelX="1.050420168067227" RelY="0.0" /> <Point X="3282.0" Y="151.0" GraphRef="c794d" RelX="1.5" RelY="-1.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163682" /> </Interaction> <Interaction GraphId="e8e23"> <Comment Source="Reactome">Intracellular Ca2+ is extruded from the outer segment by a Na+/Ca2+, K+ exchanger (NCKX1 encoded by SLC24A1) (Tucker et al. 1998). Operation of the exchanger is electrogenic; 4 Na+ enter and 1 K+ exits for every Ca2+ removed for a net movement of 1 positive charge inward per duty cycle. In bright light, when all of the CNG channels are closed, the exchanger continues to remove Ca2+, reducing intracellular Ca2+ by an order of magnitude. Mutations in SLC24A1 can give rise to recessive congenital stationary night blindness (Riazuddin et al. 2010).</Comment> <BiopaxRef>d91</BiopaxRef> <BiopaxRef>bf5</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3445.0" Y="149.0" /> <Point X="3444.0" Y="149.0" /> <Anchor Position="0.0" Shape="None" GraphId="a37fe" /> <Anchor Position="0.99" Shape="None" GraphId="de2f2" /> <Anchor Position="0.5" Shape="None" GraphId="a3b4f" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="e5d43"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3433.0" Y="192.0" GraphRef="db986" RelX="0.14285714285714285" RelY="-1.2" /> <Point X="3445.0" Y="149.0" GraphRef="a37fe" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="ee988"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3397.0" Y="100.0" GraphRef="ddfa0" RelX="0.5813953488372093" RelY="1.2" /> <Point X="3445.0" Y="149.0" GraphRef="a37fe" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="c3b56"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3359.0" Y="210.0" GraphRef="bee2f" RelX="33.36" RelY="-22.533333333333335" /> <Point X="3445.0" Y="149.0" GraphRef="a37fe" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="fae01"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3444.0" Y="149.0" GraphRef="de2f2" RelX="-0.010000000000218279" RelY="0.0" /> <Point X="3464.0" Y="88.0" GraphRef="b5232" RelX="-0.3142857142857143" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="acef4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3444.0" Y="149.0" GraphRef="de2f2" RelX="-0.010000000000218279" RelY="0.0" /> <Point X="3486.0" Y="188.0" GraphRef="abfcd" RelX="-0.7674418604651163" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="e34ef"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3444.0" Y="149.0" GraphRef="de2f2" RelX="-0.010000000000218279" RelY="0.0" /> <Point X="3501.0" Y="115.0" GraphRef="d5eba" RelX="-0.96" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="ef067"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3411.0" Y="149.0" GraphRef="b90b6" RelX="1.098360655737705" RelY="-0.09090909090909091" /> <Point X="3442.0" Y="149.0" GraphRef="a3b4f" RelX="-2.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163982" /> </Interaction> <Interaction GraphId="c55b1"> <Comment Source="Reactome">All eukaryotic proteins synthesized in the cytosol are initiated by methionine (Met). For the maturation of many proteins, the removal of N-terminal Met is essential and is mediated by methionine-aminopeptidases (METAPs). In human, there are two forms, METAP1 and 2 (Arfin et al. 1995). These enzymes utilise 2 cobalt ions (Co2+) as cofactors (Addlagatta et al. 2005, Hu et al. 2006, Marino et al. 2007).</Comment> <BiopaxRef>ff6</BiopaxRef> <BiopaxRef>d60</BiopaxRef> <BiopaxRef>e94</BiopaxRef> <BiopaxRef>c9f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1894.0" Y="657.0" /> <Point X="1958.0" Y="656.0" /> <Anchor Position="0.99" Shape="None" GraphId="ad895" /> <Anchor Position="0.5" Shape="None" GraphId="b6d0b" /> </Graphics> <Xref Database="Reactome" ID="REACT_163720" /> </Interaction> <Interaction GraphId="bbd0d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1958.0" Y="656.0" GraphRef="ad895" RelX="0.6400000000001" RelY="-0.009999999999990905" /> <Point X="1980.0" Y="668.0" GraphRef="b35db" RelX="-0.8823529411764706" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163720" /> </Interaction> <Interaction GraphId="dd125"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1958.0" Y="656.0" GraphRef="ad895" RelX="0.6400000000001" RelY="-0.009999999999990905" /> <Point X="1979.0" Y="638.0" GraphRef="a9079" RelX="-0.42857142857142855" RelY="1.1666666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163720" /> </Interaction> <Interaction GraphId="a786a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1919.0" Y="685.0" GraphRef="c7a1f" RelX="-0.014084507042253521" RelY="-1.2727272727272727" /> <Point X="1920.0" Y="656.0" GraphRef="b6d0b" RelX="-6.0" RelY="-0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163720" /> </Interaction> <Interaction GraphId="a2bc2"> <Comment Source="Reactome">After removal of the N-terminal methionine (Met) residue, the enzymes glycylpeptide N-tetradecanoyltransferase 1 and 2 (NMT1 and 2) mediate the transfer of the myristoyl (MYS) group from myristoyl-CoA to the now N-terminal glycine (Gly) residue of transducin's alpha subunit (GNAT1) (Glover et al. 1997, Giang &amp; Cravatt 1998). Myristoylation is thought to aid enzyme function and localization. Evidence from chicken experiments suggest non-myristoylated proteins do not bind to membranes (Kamps et al. 1986). </Comment> <BiopaxRef>b2c</BiopaxRef> <BiopaxRef>dab</BiopaxRef> <BiopaxRef>df9</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2030.0" Y="576.0" /> <Point X="2107.0" Y="576.0" /> <Anchor Position="0.0" Shape="None" GraphId="f2405" /> <Anchor Position="0.99" Shape="None" GraphId="d5b87" /> <Anchor Position="0.5" Shape="None" GraphId="baf15" /> </Graphics> <Xref Database="Reactome" ID="REACT_163718" /> </Interaction> <Interaction GraphId="cdfd6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2011.0" Y="596.0" GraphRef="a9079" RelX="0.3333333333333333" RelY="-1.1666666666666667" /> <Point X="2030.0" Y="576.0" GraphRef="f2405" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163718" /> </Interaction> <Interaction GraphId="f5456"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2008.0" Y="568.0" GraphRef="f6b70" RelX="0.8285714285714286" RelY="1.2" /> <Point X="2030.0" Y="576.0" GraphRef="f2405" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163718" /> </Interaction> <Interaction GraphId="eed24"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2107.0" Y="576.0" GraphRef="d5b87" RelX="0.7699999999999818" RelY="0.0" /> <Point X="2113.0" Y="511.0" GraphRef="d290b" RelX="-0.03389830508474576" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163718" /> </Interaction> <Interaction GraphId="e4add"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2107.0" Y="576.0" GraphRef="d5b87" RelX="0.7699999999999818" RelY="0.0" /> <Point X="2135.0" Y="593.0" GraphRef="bf19b" RelX="-0.7096774193548387" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163718" /> </Interaction> <Interaction GraphId="a7350"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2069.0" Y="549.0" GraphRef="f5a59" RelX="0.0" RelY="1.2727272727272727" /> <Point X="2069.0" Y="576.0" GraphRef="baf15" RelX="0.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163718" /> </Interaction> <Interaction GraphId="b9ce5"> <Comment Source="Reactome">After removal of the N-terminal methionine (Met) residue, an unknown N-acyltransferase, similar to the enzymes glycylpeptide N-tetradecanoyltransferase 1 and 2 (NMT1 and 2), mediates the transfer of acyl groups from acyl-CoA to the now N-terminal glycine (Gly) residue of transducin's alpha subunit (GNAT1). The fatty acyl groups transferred are lauroyl (C12:0) and unsaturated myristoyl groups (C14:2 and C14:1). Myristoylation is thought to aid enzyme function and localization. This human event is inferred from bovine experiments demonstrating this activity (Kokame et al 1992).</Comment> <BiopaxRef>be8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2103.0" Y="653.0" /> <Point X="2175.0" Y="653.0" /> <Anchor Position="0.0" Shape="None" GraphId="b4dd3" /> <Anchor Position="0.99" Shape="None" GraphId="d90c1" /> <Anchor Position="0.5" Shape="None" GraphId="e359f" /> </Graphics> <Xref Database="Reactome" ID="REACT_163903" /> </Interaction> <Interaction GraphId="bcafa"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2042.0" Y="629.0" GraphRef="a9079" RelX="1.0714285714285714" RelY="0.6666666666666666" /> <Point X="2103.0" Y="653.0" GraphRef="b4dd3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163903" /> </Interaction> <Interaction GraphId="ec24c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2082.0" Y="668.0" GraphRef="eedfa" RelX="0.4492753623188406" RelY="-1.2" /> <Point X="2103.0" Y="653.0" GraphRef="b4dd3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163903" /> </Interaction> <Interaction GraphId="a127a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2175.0" Y="653.0" GraphRef="d90c1" RelX="0.7199999999997999" RelY="0.0" /> <Point X="2233.0" Y="511.0" GraphRef="ccce5" RelX="-0.10416666666666667" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163903" /> </Interaction> <Interaction GraphId="de56b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2175.0" Y="653.0" GraphRef="d90c1" RelX="0.7199999999997999" RelY="0.0" /> <Point X="2163.0" Y="629.0" GraphRef="bf19b" RelX="0.1935483870967742" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163903" /> </Interaction> <Interaction GraphId="e749e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2144.0" Y="673.0" GraphRef="a7788" RelX="-0.14606741573033707" RelY="-1.2727272727272727" /> <Point X="2133.0" Y="653.0" GraphRef="e359f" RelX="-6.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163903" /> </Interaction> <Interaction GraphId="f6e39"> <Comment Source="Reactome">Prenylation is the process of post-translational addition of hydrophobic groups to proteins and is thought to help anchor proteins to cellular membranes. Farnesylation is a type of prenylation, where a farnesyl group (donated from farnesyl diphosphate, FPP) is added to a cysteine residue on a protein. The enzyme mediating this transfer is farnesyltransferase (FNT). FNT is a heterodimer comprising an alpha subunit (common to another prenylating enzyme called geranylgeranyltransferase, GGT) and a unique beta subunit (Long et al. 2001, Bell et al. 2002, deSolms et al. 2003). This complex recognises the CAAX box (C is the cysteine, A is any aliphatic amino acid, and X determines which enzyme acts on the protein) at the C-terminus of the target protein, in this case, the gamma subunit of transducin (GNG1) (Omer at al. 1993).</Comment> <BiopaxRef>f99</BiopaxRef> <BiopaxRef>a45</BiopaxRef> <BiopaxRef>f75</BiopaxRef> <BiopaxRef>b1a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1809.0" Y="529.0" /> <Point X="1863.0" Y="529.0" /> <Anchor Position="0.0" Shape="None" GraphId="ded49" /> <Anchor Position="0.99" Shape="None" GraphId="a6a96" /> <Anchor Position="0.5" Shape="None" GraphId="c2a73" /> </Graphics> <Xref Database="Reactome" ID="REACT_163835" /> </Interaction> <Interaction GraphId="c40f9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1792.0" Y="511.0" GraphRef="f0bc8" RelX="0.3076923076923077" RelY="1.2727272727272727" /> <Point X="1809.0" Y="529.0" GraphRef="ded49" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163835" /> </Interaction> <Interaction GraphId="e0ad4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1797.0" Y="536.0" GraphRef="bd894" RelX="1.162162162162162" RelY="-0.6" /> <Point X="1809.0" Y="529.0" GraphRef="ded49" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163835" /> </Interaction> <Interaction GraphId="dc715"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1863.0" Y="529.0" GraphRef="a6a96" RelX="0.5399999999999636" RelY="0.0" /> <Point X="1895.0" Y="512.0" GraphRef="e22d3" RelX="-0.3894736842105263" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163835" /> </Interaction> <Interaction GraphId="d259a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1863.0" Y="529.0" GraphRef="a6a96" RelX="0.5399999999999636" RelY="0.0" /> <Point X="1880.0" Y="547.0" GraphRef="f7812" RelX="-85.52941176470588" RelY="14.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163835" /> </Interaction> <Interaction GraphId="d0721"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1834.0" Y="583.0" GraphRef="c489b" RelX="0.0" RelY="-1.2727272727272727" /> <Point X="1835.0" Y="529.0" GraphRef="c2a73" RelX="-1.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163835" /> </Interaction> <Interaction GraphId="d6eb3"> <Comment Source="Reactome">Activated rhodopsin (MII aka R*) must be deactivated to terminate the single photon response. Deactivation begins during the rising phase of the single photon response after MII binds rhodopsin kinase (GRK1), a serine/threonine protein kinase (Khani et al. 1996). GRK1 is activated by MII whereupon it phosphorylates MII at multiple serine and threonine sites on its C terminus. There are six serine and threonine residues that can be phosphorylated. Increasing phosphorylation progressively reduces the rate at which MII can activate transducin but full quenching requires the binding of arrestin (Burns &amp; Pugh 2010, Korenbrot 2012). Certain mutations in GRK1 cause Oguchi type 2 disease, a rare, recessive form of congenital stationary night blindness (https://sph.uth.edu/retnet/).</Comment> <BiopaxRef>a54</BiopaxRef> <BiopaxRef>d4d</BiopaxRef> <BiopaxRef>e1f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2554.0" Y="498.0" /> <Point X="2618.0" Y="498.0" /> <Anchor Position="0.0" Shape="None" GraphId="e5389" /> <Anchor Position="0.99" Shape="None" GraphId="a1f7b" /> <Anchor Position="0.5" Shape="None" GraphId="bbf6f" /> <Anchor Position="0.5" Shape="None" GraphId="cbdf2" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="ef529"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2105.0" Y="393.0" GraphRef="b5aa2" RelX="1.24" RelY="0.5454545454545454" /> <Point X="2554.0" Y="498.0" GraphRef="e5389" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="f7d34"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2515.0" Y="515.0" GraphRef="c1c5f" RelX="-26.35" RelY="13.2" /> <Point X="2554.0" Y="498.0" GraphRef="e5389" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="f358a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2618.0" Y="498.0" GraphRef="a1f7b" RelX="0.6399999999998727" RelY="0.0" /> <Point X="2651.0" Y="520.0" GraphRef="f8f83" RelX="-29.048780487804876" RelY="12.866666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="e685e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2618.0" Y="498.0" GraphRef="a1f7b" RelX="0.6399999999998727" RelY="0.0" /> <Point X="2661.0" Y="498.0" GraphRef="c2900" RelX="-1.0465116279069768" RelY="-0.05555555555555555" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="ad721"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2587.0" Y="559.0" GraphRef="cbede" RelX="-0.058823529411764705" RelY="-1.2727272727272727" /> <Point X="2580.0" Y="498.0" GraphRef="bbf6f" RelX="-6.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="a4046"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2652.0" Y="557.0" GraphRef="bc367" RelX="-0.52" RelY="-1.2727272727272727" /> <Point X="2580.0" Y="498.0" GraphRef="cbdf2" RelX="-6.0" RelY="0.0" ArrowHead="TBar" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="d9986"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2541.0" Y="530.0" GraphRef="bee2f" RelX="0.64" RelY="-1.2" /> <Point X="2580.0" Y="498.0" GraphRef="cbdf2" RelX="-6.0" RelY="0.0" ArrowHead="TBar" /> </Graphics> <Xref Database="Reactome" ID="REACT_163992" /> </Interaction> <Interaction GraphId="f7abe"> <Comment Source="Reactome">Although phosphorylation of activated rhodopsin (MII) reduces transducin activation, complete deactivation occurs only after arrestin (S-antigen or SAG, Yamaki et al. 1988) binds to and sterically caps MII. SAG is capable of binding unphosphorylated MII, but with very low probability. Binding affinity increases greatly upon phosphorylation. Binding of SAG generally occurs after MII has been phosphorylated ~3 times, and binding prevents further phosphorylation. Interestingly, rods express a small amount of a splice variant of SAG, P44, but its function is not yet known. Defects in SAG cause Oguchi type 1 disease (CSNBO1; MIM:258100), a recessive form of congenital stationary night blindness characterized by impaired scotopic vision (Fuchs et al. 1995).</Comment> <BiopaxRef>c25</BiopaxRef> <BiopaxRef>a94</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2828.0" Y="499.0" /> <Point X="2860.0" Y="499.0" /> <Anchor Position="0.0" Shape="None" GraphId="fe5cd" /> </Graphics> <Xref Database="Reactome" ID="REACT_163871" /> </Interaction> <Interaction GraphId="e56fb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2787.0" Y="533.0" GraphRef="d2f94" RelX="0.75" RelY="-1.2727272727272727" /> <Point X="2828.0" Y="499.0" GraphRef="fe5cd" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163871" /> </Interaction> <Interaction GraphId="d6603"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2796.0" Y="499.0" GraphRef="c2900" RelX="1.0465116279069768" RelY="0.0" /> <Point X="2828.0" Y="499.0" GraphRef="fe5cd" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163871" /> </Interaction> <Interaction GraphId="e026a"> <Comment Source="Reactome">Eventually the Schiff base linkage between all-trans-retinal (atRAL) and opsin is hydrolyzed. The atRAL repositions to an "exit" site within opsin and is reduced to all-trans-retinol (atROL) by retinol dehydrogenases RDH8 and RDH12 using NADPH as cofactor (see section on rod retinoid cycle), whereupon it exits the rod (Baumann &amp; Bender 1973).</Comment> <BiopaxRef>b0e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2933.0" Y="498.0" /> <Point X="2959.0" Y="498.0" /> <Anchor Position="0.99" Shape="None" GraphId="defbf" /> </Graphics> <Xref Database="Reactome" ID="REACT_163890" /> </Interaction> <Interaction GraphId="feba4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2959.0" Y="498.0" GraphRef="defbf" RelX="0.2600000000002183" RelY="0.0" /> <Point X="2440.0" Y="522.0" GraphRef="f37e3" RelX="10.8" RelY="-17.466666666666665" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163890" /> </Interaction> <Interaction GraphId="cebee"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2959.0" Y="498.0" GraphRef="defbf" RelX="0.2600000000002183" RelY="0.0" /> <Point X="2991.0" Y="498.0" GraphRef="d2835" RelX="-1.077922077922078" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163890" /> </Interaction> <Interaction GraphId="b9af5"> <Comment Source="Reactome">Loss of all-trans-retinal (atRAL) is followed by dissociation of arrestin (SAG) from p-RHO. RHO is then available for covalent binding to 11-cis-retinal (11cRAL), supplied by the retinal pigment epithelium, to regenerate rhodopsin. SAG is capable of binding weakly to rhodopsin, so the dissociation in some rhodopsins may occur after regeneration (Baumann &amp; Bender 1973).</Comment> <BiopaxRef>b0e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3074.0" Y="498.0" /> <Point X="3114.0" Y="498.0" /> <Anchor Position="0.99" Shape="None" GraphId="def65" /> </Graphics> <Xref Database="Reactome" ID="REACT_163954" /> </Interaction> <Interaction GraphId="fa6e4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3114.0" Y="498.0" GraphRef="def65" RelX="0.40000000000009095" RelY="0.0" /> <Point X="3147.0" Y="498.0" GraphRef="dc466" RelX="-1.0465116279069768" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163954" /> </Interaction> <Interaction GraphId="f2c60"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3114.0" Y="498.0" GraphRef="def65" RelX="0.40000000000009095" RelY="0.0" /> <Point X="2794.0" Y="546.0" GraphRef="d2f94" RelX="1.1875" RelY="-0.09090909090909091" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163954" /> </Interaction> <Interaction GraphId="ef169"> <Comment Source="Reactome">Protein phosphatase 2A removes the phosphates from phosphorylated rhodopsin (p MII) and phosphorylated opsin (p-RHO) (Fowles et al. 1989, Palczewski et al. 1989a,b). A Ca2+ dependent opsin phosphatase is also present (Kutuzov &amp; Bennett 1996). Serine/threonine protein phosphatases with EF hands (PPEF-1 and -2) that share homology with Drosophila retinal degeneration C (rdgC) are expressed in retina and may be responsible (Huang &amp; Honkanen 1998), there is no evidence for a physiological role in dephosphorylating rhodopsin. Once dephosphorylated, RHO can once again bind the chromophore 11 cis retinal (11cRAL), in readiness for the next photon response.&lt;br&gt;&lt;br&gt;</Comment> <BiopaxRef>fd3</BiopaxRef> <BiopaxRef>fec</BiopaxRef> <BiopaxRef>e23</BiopaxRef> <BiopaxRef>d51</BiopaxRef> <BiopaxRef>b1c</BiopaxRef> <BiopaxRef>c98</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3317.0" Y="499.0" /> <Point X="3388.0" Y="499.0" /> <Anchor Position="0.0" Shape="None" GraphId="d42d3" /> <Anchor Position="0.99" Shape="None" GraphId="b930f" /> <Anchor Position="0.5" Shape="None" GraphId="b9fbb" /> <Anchor Position="0.5" Shape="None" GraphId="f9a69" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="b98f5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3282.0" Y="498.0" GraphRef="dc466" RelX="1.0465116279069768" RelY="0.0" /> <Point X="3317.0" Y="499.0" GraphRef="d42d3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="acbe1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3284.0" Y="529.0" GraphRef="ad5cd" RelX="100.30232558139535" RelY="-3.533333333333333" /> <Point X="3317.0" Y="499.0" GraphRef="d42d3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="b569a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3388.0" Y="499.0" GraphRef="b930f" RelX="0.7100000000000364" RelY="0.0" /> <Point X="1804.0" Y="401.0" GraphRef="b8a3e" RelX="0.2" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="cd111"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3388.0" Y="499.0" GraphRef="b930f" RelX="0.7100000000000364" RelY="0.0" /> <Point X="3436.0" Y="529.0" GraphRef="fb80d" RelX="54.851851851851855" RelY="14.333333333333334" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="a2ec0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3333.0" Y="562.0" GraphRef="d5d38" RelX="0.03614457831325301" RelY="-1.2727272727272727" /> <Point X="3347.0" Y="499.0" GraphRef="b9fbb" RelX="-5.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="bb824"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3401.0" Y="552.0" GraphRef="bee2f" RelX="35.04" RelY="0.26666666666666666" /> <Point X="3347.0" Y="499.0" GraphRef="f9a69" RelX="-5.5" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163839" /> </Interaction> <Interaction GraphId="cc0b8"> <Comment Source="Reactome">Active Gt alpha (GNAT-GTP) can be inactivated by a slow, intrinsic GTPase activity that hydrolyses GTP to GDP. Once GNAT1 has GDP bound, it no longer binds to the gamma subunit of PDE6 (PDE6-gamma) that then resumes inhibition of the catalytic subunit of PDE6. The hydrolysis of GTP is accelerated by a GAP (GTPase accelerating protein) complex that consists of Regulator of G protein signaling 9 (RGS9-1, RGS9 isoform 3) (He et al. 1998, Zhang et al. 1999), Guanine nucleotide binding protein subunit beta 5, long form (GNB5) (Makino et al. 1999) and RGS9 anchoring protein (RGS9BP, aka R9AP) (Hu &amp; Wensel 1998). The affinity of GNAT GTP for the GAP complex is relatively low, but is increased significantly by the presence of PDE-gamma. Shutoff of Gt is the rate-limiting step in the recovery of the single photon response of rods (Chen et al. 2000, Krispel et al. 2006). Persons with defective GAP experience bradyopsia or "slow vision" in which there are difficulties in adjusting to changes in brightness and to tracking moving objects (Michaelides et al. 2010, Nishiguchi et al. 2004).</Comment> <BiopaxRef>fbd</BiopaxRef> <BiopaxRef>f29</BiopaxRef> <BiopaxRef>b1e</BiopaxRef> <BiopaxRef>f5a</BiopaxRef> <BiopaxRef>ac7</BiopaxRef> <BiopaxRef>b84</BiopaxRef> <BiopaxRef>ed3</BiopaxRef> <BiopaxRef>fe1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2930.0" Y="387.0" /> <Point X="2738.0" Y="344.0" /> <Anchor Position="0.0" Shape="None" GraphId="cf2c3" /> <Anchor Position="0.99" Shape="None" GraphId="d51e0" /> <Anchor Position="0.5" Shape="None" GraphId="ef20e" /> <Anchor Position="0.5" Shape="None" GraphId="aebad" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="b413c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2968.0" Y="332.0" GraphRef="ad5cd" RelX="85.6046511627907" RelY="-16.666666666666668" /> <Point X="2930.0" Y="387.0" GraphRef="cf2c3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="e2d44"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2888.0" Y="387.0" GraphRef="e2a72" RelX="1.0512820512820513" RelY="-0.18181818181818182" /> <Point X="2930.0" Y="387.0" GraphRef="cf2c3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="aa459"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2738.0" Y="344.0" GraphRef="d51e0" RelX="-1.9200000000000728" RelY="-0.4300000000000068" /> <Point X="2712.0" Y="323.0" GraphRef="fb80d" RelX="1.2222222222222223" RelY="0.6" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="ee57e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2738.0" Y="344.0" GraphRef="d51e0" RelX="-1.9200000000000728" RelY="-0.4300000000000068" /> <Point X="2653.0" Y="375.0" GraphRef="b6c00" RelX="1.15" RelY="-0.7272727272727273" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="cf0e9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2738.0" Y="344.0" GraphRef="d51e0" RelX="-1.9200000000000728" RelY="-0.4300000000000068" /> <Point X="2715.0" Y="372.0" GraphRef="f18e2" RelX="0.18072289156626506" RelY="-1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="e64bc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2883.0" Y="403.0" GraphRef="e2a72" RelX="0.9658119658119658" RelY="1.2727272727272727" /> <Point X="2941.0" Y="344.0" GraphRef="ef20e" RelX="107.0" RelY="-21.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="e889a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2996.0" Y="387.0" GraphRef="bda5c" RelX="-1.0625" RelY="0.0" /> <Point X="2941.0" Y="344.0" GraphRef="aebad" RelX="107.0" RelY="-21.5" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163662" /> </Interaction> <Interaction GraphId="df0ca"> <Comment Source="Reactome">In bovine experiments, phosphorylation of RGS9-1 (at Ser475, human site predicted to be at Ser478) by protein kinase C (PRKC, specifically the isozymes PRKCalpha and PRKCtheta) significantly decreased the affinity of RGS9-1 for its membrane anchor protein and GAP enhancer RGS9-1 anchor protein (R9S9BP). This represents a potential mechanism for feedback control of the photoresponse recovery in both rods and cones (Sokal et al. 2003, Balasubramanian et al. 2001, Hu et al. 2001).</Comment> <BiopaxRef>dd6</BiopaxRef> <BiopaxRef>b55</BiopaxRef> <BiopaxRef>ca7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3067.0" Y="345.0" /> <Point X="3198.0" Y="346.0" /> <Anchor Position="0.0" Shape="None" GraphId="bf1e5" /> <Anchor Position="0.99" Shape="None" GraphId="aa768" /> <Anchor Position="0.5" Shape="None" GraphId="efab2" /> </Graphics> <Xref Database="Reactome" ID="REACT_163640" /> </Interaction> <Interaction GraphId="cfddb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3055.0" Y="366.0" GraphRef="bda5c" RelX="0.16666666666666666" RelY="-1.1666666666666667" /> <Point X="3067.0" Y="345.0" GraphRef="bf1e5" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163640" /> </Interaction> <Interaction GraphId="f2a3a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3055.0" Y="335.0" GraphRef="c1c5f" RelX="0.65" RelY="1.2" /> <Point X="3067.0" Y="345.0" GraphRef="bf1e5" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163640" /> </Interaction> <Interaction GraphId="b5652"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3198.0" Y="346.0" GraphRef="aa768" RelX="1.3099999999999454" RelY="0.009999999999990905" /> <Point X="3223.0" Y="335.0" GraphRef="f8f83" RelX="-1.146341463414634" RelY="0.5333333333333333" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163640" /> </Interaction> <Interaction GraphId="b4b59"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3198.0" Y="346.0" GraphRef="aa768" RelX="1.3099999999999454" RelY="0.009999999999990905" /> <Point X="3225.0" Y="365.0" GraphRef="b66e3" RelX="-0.42342342342342343" RelY="-1.1666666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163640" /> </Interaction> <Interaction GraphId="dec32"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3144.0" Y="374.0" GraphRef="b02a3" RelX="-0.015873015873015872" RelY="-1.2727272727272727" /> <Point X="3144.0" Y="346.0" GraphRef="efab2" RelX="11.5" RelY="0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163640" /> </Interaction> <Interaction GraphId="a753d"> <Comment Source="Reactome">Once transducin alpha subunit (GNAT1) is deactivated by hydrolysis of bound GTP to GDP, it reassociates with transducin beta:gamma subunits (GNB1:GNGT1) to form inactive transducin (Gt-GDP). A stoichiometric overabundance of GNB1:GNGT1 facilitates the reassociation event. The details for this event were revealed in bovine experiments (Clark et al. 2006, Fung et al. 1981).</Comment> <BiopaxRef>e09</BiopaxRef> <BiopaxRef>edf</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2445.0" Y="326.0" /> <Point X="2167.0" Y="373.0" /> <Anchor Position="0.0" Shape="None" GraphId="fc55e" /> </Graphics> <Xref Database="Reactome" ID="REACT_163859" /> </Interaction> <Interaction GraphId="ddef2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2445.0" Y="369.0" GraphRef="e7eb2" RelX="-0.033707865168539325" RelY="-1.2727272727272727" /> <Point X="2445.0" Y="326.0" GraphRef="fc55e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163859" /> </Interaction> <Interaction GraphId="be2b5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2688.0" Y="372.0" GraphRef="f18e2" RelX="-0.46987951807228917" RelY="-1.2727272727272727" /> <Point X="2445.0" Y="326.0" GraphRef="fc55e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163859" /> </Interaction> <Interaction GraphId="fff6a"> <Comment Source="Reactome">The activity of guanylyl cyclases is regulated by Ca2+-binding, guanylyl cyclase-activating proteins (GCAPs). This regulation is the most important negative feedback mechanism triggered by Ca2+ in light. There are three GCAPs in humans; GUCA1A (Subbaraya et al. 1994), GUCA1B (Surguchov et al. 1997) and GUCA1C (Haeseleer et al. 1999). In darkness, when intracellular Ca2+ is relatively high, GCAPs suppress guanylate cyclase activity. But the light-induced fall in Ca2+ prompts Ca2+ to dissociate from GCAPs and be replaced by Mg2+, allowing the GCAPs to stimulate guanylate cyclase activity by an order of magnitude. Different GCAPs have different affinities for Ca2+. Defects in GCAP1 give rise to cone dystrophy and Lebers congenital amaurosis (https://sph.uth.edu/retnet/).&lt;br&gt;</Comment> <BiopaxRef>e56</BiopaxRef> <BiopaxRef>df0</BiopaxRef> <BiopaxRef>b77</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3398.0" Y="285.0" /> <Point X="3621.0" Y="371.0" /> <Anchor Position="0.0" Shape="None" GraphId="b927e" /> </Graphics> <Xref Database="Reactome" ID="REACT_163809" /> </Interaction> <Interaction GraphId="cef03"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3410.0" Y="370.0" GraphRef="ebf3c" RelX="-0.09523809523809523" RelY="-1.2727272727272727" /> <Point X="3398.0" Y="285.0" GraphRef="b927e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163809" /> </Interaction> <Interaction GraphId="bd7e2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3355.0" Y="246.0" GraphRef="bee2f" RelX="33.2" RelY="-20.133333333333333" /> <Point X="3398.0" Y="285.0" GraphRef="b927e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163809" /> </Interaction> <Interaction GraphId="b4b74"> <Comment Source="Reactome">The basal, "dark" levels of cGMP are restored as part of the recovery of light response by membrane guanylyl cyclases (GUCYs). Two variants, GUCY2D (Shyjan et al. 1992) and GUCY2F (Lowe et al. 1995), mediate the synthesis of cGMP from GTP. Unlike other membrane guanylyl cyclases, the rod types are not receptors for extracellular substances. Instead, GUCYs are regulated intracellularly by guanylyl cyclase activating proteins (GCAPs), this regulation being the most important negative feedback mechanism triggered by Ca2+ in light. There are three GCAPs in humans; GUCA1A, GUCA1B and GUCA1C (Subbaraya et al. 1994, Surguchov et al. 1997, Haeseleer et al. 1999). GCAPs are Ca2+ binding proteins. When Ca2+ concentration is high (in the "dark" condition), GCAPs bind Ca2+ and inhibit GUCYs. Conversely, when Ca2+ concentration is low (as in a light response), GCAPs release Ca2+ and bind Mg2+ in its place. With Mg2+ bound, GCAPs stimulate GUCY activity by an order of magnitude. This negative feedback operates rapidly to limit the amplitude and duration of the single photon response and to dampen the effects of spontaneous PDE activations. Mutations in GUCYD can give rise to Leber's congenital amaurosis or to cone-rod dystrophy (https://sph.uth.edu/retnet/).</Comment> <BiopaxRef>e7a</BiopaxRef> <BiopaxRef>e56</BiopaxRef> <BiopaxRef>b77</BiopaxRef> <BiopaxRef>df0</BiopaxRef> <BiopaxRef>bb6</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3536.0" Y="312.0" /> <Point X="3375.0" Y="313.0" /> <Anchor Position="0.99" Shape="None" GraphId="d4023" /> <Anchor Position="0.5" Shape="None" GraphId="b6de9" /> <Anchor Position="0.5" Shape="None" GraphId="eb0cd" /> <Anchor Position="0.5" Shape="None" GraphId="ca272" /> </Graphics> <Xref Database="Reactome" ID="REACT_163996" /> </Interaction> <Interaction GraphId="c89df"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3375.0" Y="313.0" GraphRef="d4023" RelX="-1.6100000000001273" RelY="0.009999999999990905" /> <Point X="3354.0" Y="327.0" GraphRef="f7812" RelX="1.1764705882352942" RelY="-0.6666666666666666" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163996" /> </Interaction> <Interaction GraphId="b8b67"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3375.0" Y="313.0" GraphRef="d4023" RelX="-1.6100000000001273" RelY="0.009999999999990905" /> <Point X="3173.0" Y="279.0" GraphRef="c1cf8" RelX="1.1224489795918366" RelY="0.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163996" /> </Interaction> <Interaction GraphId="ecc95"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3500.0" Y="370.0" GraphRef="d12d2" RelX="-0.02127659574468085" RelY="-1.2727272727272727" /> <Point X="3500.0" Y="312.0" GraphRef="b6de9" RelX="44.5" RelY="-0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_163996" /> </Interaction> <Interaction GraphId="f30cd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3602.0" Y="371.0" GraphRef="d49ff" RelX="-0.4936708860759494" RelY="-1.2727272727272727" /> <Point X="3500.0" Y="312.0" GraphRef="eb0cd" RelX="44.5" RelY="-0.5" ArrowHead="TBar" /> </Graphics> <Xref Database="Reactome" ID="REACT_163996" /> </Interaction> <Interaction GraphId="de26f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3425.0" Y="370.0" GraphRef="ebf3c" RelX="0.6190476190476191" RelY="-1.2727272727272727" /> <Point X="3500.0" Y="312.0" GraphRef="ca272" RelX="44.5" RelY="-0.5" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_163996" /> </Interaction> <Interaction GraphId="e6e17"> <Comment Source="Reactome">Once cGMP concentration is restored to "dark" levels, it binds cooperatively to the cGMP-gated cation channel (CNG channel), inducing opening through a conformational change in the channel (open status designated as cGMP:CNG channel here) (Chen et al 1993, Dhallan et al. 1992).</Comment> <BiopaxRef>cac</BiopaxRef> <BiopaxRef>d44</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3144.0" Y="238.0" /> <Point X="3181.0" Y="165.0" /> <Anchor Position="0.0" Shape="None" GraphId="e1023" /> </Graphics> <Xref Database="Reactome" ID="REACT_164008" /> </Interaction> <Interaction GraphId="ddd7d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3027.0" Y="163.0" GraphRef="ae270" RelX="0.37349397590361444" RelY="1.2727272727272727" /> <Point X="3144.0" Y="238.0" GraphRef="e1023" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_164008" /> </Interaction> <Interaction GraphId="aa67f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="3144.0" Y="258.0" GraphRef="c1cf8" RelX="-0.061224489795918366" RelY="-1.2" /> <Point X="3144.0" Y="238.0" GraphRef="e1023" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_164008" /> </Interaction> <Interaction GraphId="c3735"> <Comment Source="Reactome">RDH11 is the best-characterised enzyme that reduces all-trans-retinal (atRAL) to all-trans-retinol (atROL). In addition, several aldo-keto reductase (AKR) enzymes from subfamilies 1B and 1C also show all-trans-retinal (atRAL) reductase activity. AKR1B10 shows high reductase activity towards atRAL (Gallego et al. 2007, Ruiz et al. 2009) whereas AKR1C1, 1C3 and 1C4 all show much lower reductase activity towards arRAL (Ruiz et al. 2011).</Comment> <BiopaxRef>dcd</BiopaxRef> <BiopaxRef>cca</BiopaxRef> <BiopaxRef>b73</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="346.0" Y="522.0" /> <Point X="419.0" Y="482.0" /> <Anchor Position="0.0" Shape="None" GraphId="f1d1a" /> <Anchor Position="0.99" Shape="None" GraphId="c7493" /> <Anchor Position="0.5" Shape="None" GraphId="d6d6f" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="d6dfd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="311.0" Y="478.0" GraphRef="f643a" RelX="-64.22033898305085" RelY="-46.13333333333333" /> <Point X="346.0" Y="522.0" GraphRef="f1d1a" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="cb37d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="311.0" Y="505.0" GraphRef="c6d0d" RelX="-105.0" RelY="-40.333333333333336" /> <Point X="346.0" Y="522.0" GraphRef="f1d1a" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="b2bbc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="323.0" Y="529.0" GraphRef="ed60a" RelX="0.631578947368421" RelY="-1.2727272727272727" /> <Point X="346.0" Y="522.0" GraphRef="f1d1a" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="c623c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="419.0" Y="482.0" GraphRef="c7493" RelX="0.7300000000000182" RelY="-0.39999999999997726" /> <Point X="421.0" Y="517.0" GraphRef="c5a60" RelX="-53.96666666666667" RelY="-44.06666666666667" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="f7bca"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="419.0" Y="482.0" GraphRef="c7493" RelX="0.7300000000000182" RelY="-0.39999999999997726" /> <Point X="434.0" Y="457.0" GraphRef="b52ba" RelX="-0.19480519480519481" RelY="1.2727272727272727" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="ed35f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="366.0" Y="549.0" GraphRef="e7d05" RelX="-0.02564102564102564" RelY="-1.2727272727272727" /> <Point X="367.0" Y="522.0" GraphRef="d6d6f" RelX="-15.5" RelY="20.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160311" /> </Interaction> <Interaction GraphId="e747b"> <Comment Source="Reactome">All-trans-retinol (atROL) binds to cellular retinol-binding protein 1 (RBP1) (Folli et al. 2001). RBP1 is thought to be required for intracellular transport of atROL in the liver.</Comment> <BiopaxRef>b58</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="455.0" Y="1096.0" /> <Point X="441.0" Y="1123.0" /> <Anchor Position="0.0" Shape="None" GraphId="df504" /> </Graphics> <Xref Database="Reactome" ID="REACT_160275" /> </Interaction> <Interaction GraphId="b3d30"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="441.0" Y="1089.0" GraphRef="bcf69" RelX="1.1176470588235294" RelY="0.5333333333333333" /> <Point X="455.0" Y="1096.0" GraphRef="df504" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160275" /> </Interaction> <Interaction GraphId="b1ee1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="455.0" Y="1070.0" GraphRef="f6c67" RelX="-26.53846153846154" RelY="34.18181818181818" /> <Point X="455.0" Y="1096.0" GraphRef="df504" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160275" /> </Interaction> <Interaction GraphId="cd6d9"> <Comment Source="Reactome">In the disc membranes of photoreceptor outer segments, all-trans-retinal (atRAL) can spontaneously and reversibly react with phosphatidiylethanolamine (PE, cephalin; a phospholipid found in in membranes) to form a Schiff base product, N-retinylidene-phosphatidylethanolamine (NRPE) (Poincelot et al. 1969, Parish et al. 1998, Mata et al. 2000). Then, either NRPE is "flipped" over to the cytoplasmic side of disc membranes by ABCA4 where it can dissociate (thus releasing atRAL to re-enter the retinoid cycle) or it can condense with another atRAL to form a toxic diretinal compound. The route taken is determined by whether a functional ABCA4 protein is present or not.</Comment> <BiopaxRef>c2d</BiopaxRef> <BiopaxRef>c12</BiopaxRef> <BiopaxRef>cdf</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2205.0" Y="837.0" /> <Point X="2205.0" Y="915.0" /> <Anchor Position="0.0" Shape="None" GraphId="b4d78" /> </Graphics> <Xref Database="Reactome" ID="REACT_160285" /> </Interaction> <Interaction GraphId="d31b6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2227.0" Y="797.0" GraphRef="e20b4" RelX="-0.5294117647058824" RelY="1.2" /> <Point X="2205.0" Y="837.0" GraphRef="b4d78" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160285" /> </Interaction> <Interaction GraphId="ffe83"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2179.0" Y="802.0" GraphRef="f37e3" RelX="0.36" RelY="1.2" /> <Point X="2205.0" Y="837.0" GraphRef="b4d78" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160285" /> </Interaction> <Interaction GraphId="b8879"> <Comment Source="Reactome">A phosphatidyl-pyridinium bisretinoid compound, A2PE, is formed through condensation of N-retinylidene-PE (NRPE) and a second all-trans-retinol (atRAL) molecule (Parish et al. 1998, Mata et al. 2000). This most likely happens when atRAL is abundant. </Comment> <BiopaxRef>c12</BiopaxRef> <BiopaxRef>cdf</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2055.0" Y="883.0" /> <Point X="1974.0" Y="883.0" /> <Anchor Position="0.0" Shape="None" GraphId="b7d03" /> <Anchor Position="0.99" Shape="None" GraphId="e4a70" /> </Graphics> <Xref Database="Reactome" ID="REACT_160162" /> </Interaction> <Interaction GraphId="b6456"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2178.0" Y="925.0" GraphRef="c8252" RelX="-1.125" RelY="-0.5333333333333333" /> <Point X="2055.0" Y="883.0" GraphRef="b7d03" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160162" /> </Interaction> <Interaction GraphId="a7dff"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2152.0" Y="802.0" GraphRef="f37e3" RelX="-0.72" RelY="1.2" /> <Point X="2055.0" Y="883.0" GraphRef="b7d03" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160162" /> </Interaction> <Interaction GraphId="a4029"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1974.0" Y="883.0" GraphRef="e4a70" RelX="-0.8099999999999454" RelY="0.0" /> <Point X="1938.0" Y="916.0" GraphRef="b8183" RelX="0.6170212765957447" RelY="-1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160162" /> </Interaction> <Interaction GraphId="fee8f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1974.0" Y="883.0" GraphRef="e4a70" RelX="-0.8099999999999454" RelY="0.0" /> <Point X="1937.0" Y="864.0" GraphRef="ad5cd" RelX="37.651162790697676" RelY="18.8" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160162" /> </Interaction> <Interaction GraphId="b83b9"> <Comment Source="Reactome">The outer segment of photoreceptor cells is shed every 10-14 days to be completely replaced. The shed material is phagocytosed and transferred to the retinal pigment epithelium (RPE). Diretinoid-pyridinium-phosphatidylethanolamine (A2PE) can be hydrolysed to diretinoid-pyridinium-ethanolamine (A2E), a prominent constituent of lipofuscin (the material deposited in retinal tissue which accumulates over time and is implicated in macular degeneration). Evidence suggests this happens before transfer to RPE cells as part of the phagocytosed outer segment. A2E has been detected in outer segments (Ben-Shabat et al. 2002) and an N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (NAPEPLD) activity detected in rat, mouse and human proteins (Okamoto et al. 2004, Ueda et al. 2005, Wang et al. 2006). This activity has been shown to hydrolyse A2PE to A2E in bovine outer segments before phagocytosis and transfer to RPE cells, suggesting A2PE is hydrolysed to A2E in photoreceptor outer segment membranes (Sparrow et al. 2003, Salvador &amp; Giusto 1998).</Comment> <BiopaxRef>ac1</BiopaxRef> <BiopaxRef>fb0</BiopaxRef> <BiopaxRef>ac3</BiopaxRef> <BiopaxRef>d0a</BiopaxRef> <BiopaxRef>c5b</BiopaxRef> <BiopaxRef>ca5</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1876.0" Y="882.0" /> <Point X="1806.0" Y="882.0" /> <Anchor Position="0.0" Shape="None" GraphId="f3cc6" /> <Anchor Position="0.99" Shape="None" GraphId="dd209" /> <Anchor Position="0.5" Shape="None" GraphId="d9c2e" /> </Graphics> <Xref Database="Reactome" ID="REACT_160080" /> </Interaction> <Interaction GraphId="ae5b7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1909.0" Y="916.0" GraphRef="b8183" RelX="-0.6170212765957447" RelY="-1.2" /> <Point X="1876.0" Y="882.0" GraphRef="f3cc6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160080" /> </Interaction> <Interaction GraphId="faa08"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1892.0" Y="872.0" GraphRef="ad5cd" RelX="35.55813953488372" RelY="19.333333333333332" /> <Point X="1876.0" Y="882.0" GraphRef="f3cc6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160080" /> </Interaction> <Interaction GraphId="e6fea"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1806.0" Y="882.0" GraphRef="dd209" RelX="-0.7000000000000455" RelY="0.0" /> <Point X="1759.0" Y="918.0" GraphRef="dd4ae" RelX="1.15" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160080" /> </Interaction> <Interaction GraphId="fa620"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1806.0" Y="882.0" GraphRef="dd209" RelX="-0.7000000000000455" RelY="0.0" /> <Point X="1790.0" Y="839.0" GraphRef="deccb" RelX="0.3125" RelY="1.2" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="REACT_160080" /> </Interaction> <Interaction GraphId="fd74c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1853.0" Y="918.0" GraphRef="d11de" RelX="-0.03225806451612903" RelY="-1.2727272727272727" /> <Point X="1852.0" Y="882.0" GraphRef="d9c2e" RelX="11.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="REACT_160080" /> </Interaction> <Interaction GraphId="a3891"> <Comment Source="Reactome">Early experiments in frog and other species determined that the outer segments of photoreceptors are renewed by phagocytosis and transfer to retinal pigment eplithelial (RPE) cells for processing. A2E, formed in disc membranes of outer segments, is taken along with the phagolysosome (Young 1967, Young &amp; Bok 1969, Katz et al. 1986). Here, for simplicity, only A2E is shown in the phagolysosome.</Comment> <BiopaxRef>df3</BiopaxRef> <BiopaxRef>f87</BiopaxRef> <BiopaxRef>c3a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1751.0" Y="951.0" /> <Point X="1789.0" Y="977.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160187" /> </Interaction> <Interaction GraphId="c659e"> <Comment Source="Reactome">Once photoreceptor outer segments are phagocytosed, inclusive of A2E, they are delivered to retinal pigment epithelial (RPE) cells for disposal. However, A2E has been shown to be resistant to any sort of degradative enzyme thus accumulates in the RPE. The relationship between lipofuscin accumulation and retinal degeneration is illustrated by Stargardt disease type 1 (STGD1, MIM:248200) (Allikmets et al. 1997).</Comment> <BiopaxRef>bd7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1786.0" Y="994.0" /> <Point X="1590.0" Y="880.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_160092" /> </Interaction> <Interaction GraphId="de4ef"> <Comment Source="Reactome">As the channels reopen, rising Ca2+ levels result in binding of Ca2+ to calmodulin (CALM1). By targeting the beta subunit of the channel, CALM1:Ca2+ reduces the apparent affinity of the channel for cGMP (Chen et al. 1994, Hsu &amp; Molday 1993, Hsu &amp; Molday 1994).</Comment> <BiopaxRef>c87</BiopaxRef> <BiopaxRef>aac</BiopaxRef> <BiopaxRef>f56</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2931.0" Y="148.0" /> <Point X="2864.0" Y="148.0" /> <Anchor Position="0.0" Shape="None" GraphId="becce" /> </Graphics> <Xref Database="Reactome" ID="REACT_163913" /> </Interaction> <Interaction GraphId="d82f0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2967.0" Y="148.0" GraphRef="ae270" RelX="-1.072289156626506" RelY="-0.09090909090909091" /> <Point X="2931.0" Y="148.0" GraphRef="becce" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163913" /> </Interaction> <Interaction GraphId="afc60"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2984.0" Y="173.0" GraphRef="f83ee" RelX="-0.5116279069767442" RelY="-1.2727272727272727" /> <Point X="2931.0" Y="148.0" GraphRef="becce" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="REACT_163913" /> </Interaction> <Interaction GraphId="f664d"> <Comment Source="Reactome">A substantial fraction of rhodopsin kinase (GRK1) is bound to recoverin (RCVRN) in darkness, when internal Ca2+ levels are high. RCVRN is an EF-hand protein (Murakami et al. 1992) that functions as a myristoyl switch. With Ca2+ bound, the myristoyl group is exposed to attach RCVRN to the membrane. When Ca2+ levels drop with light exposure, Ca2+ dissociates from RCVRN and GRK1 is released. Higher levels of free GRK1 accelerate the phosphorylation and shutoff of photoexcited rhodopsin (MII). However, this feedback mechanism proceeds too slowly to impact the single photon response that was responsible for causing the fall in Ca2+. Instead, it operates during light adaptation, where the light-induced fall in Ca2+ primes the rod to release GRK1 to act after subsequent photoisomerizations of rhodopsin. RCVRN also serves as a Ca2+ buffer within the rod outer segment. 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