Class B/2 (secretin family receptors) (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Class B/2 (Secretin family receptors)" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">This family is known as Family B (secretin-receptor family, family 2) G-protein-coupled receptors. Family B GPCRs include secretin, calcitonin, parathyroid hormone/parathyroid hormone-related peptides and vasoactive intestinal peptide receptors; all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway (Harmar AJ, 2001). View original pathway at:[http://www.reactome.org/PathwayBrowser/#DIAGRAM=373080 Reactome].</Comment> <Comment Source="Reactome-Converter">Pathway is converted from Reactome ID: 373080</Comment> <Comment Source="Reactome-version">Reactome version: 65</Comment> <Comment Source="Reactome Author">Reactome Author: Jassal, Bijay</Comment> <BiopaxRef>a1f</BiopaxRef> <Attribute Key="reactome_id" Value="373080" /> <Graphics BoardWidth="2454.0" BoardHeight="1682.0" /> <DataNode TextLabel="ADM(95-146) " GraphId="a04e1" Type="Protein" GroupRef="ab36f"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-420062" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="942.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P35318" /> </DataNode> <DataNode TextLabel="GLP-1:GLP-1R:Heterotrimeric G(s):GDP" GraphId="a1a62" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="604.0" CenterY="704.0" Width="122.0" Height="50.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-422310" /> </DataNode> <DataNode TextLabel="CRH" GraphId="a1cb8" Type="Protein"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="1206.0" CenterY="54.0" Width="34.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P06850" /> </DataNode> <DataNode TextLabel="PTH1R " GraphId="a1d80" Type="Protein" GroupRef="fa3e7"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-420503" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1202.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q03431" /> </DataNode> <DataNode TextLabel="PTCH1 " GraphId="a2556" Type="Protein" GroupRef="c73f3"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-445134" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1322.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13635" /> </DataNode> <DataNode TextLabel="WNT9B " GraphId="a2764" Type="Protein" GroupRef="bf57d"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-517468" /> <Attribute Key="copies_num" Value="15" /> <Graphics CenterX="660.0" CenterY="1542.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O14905" /> </DataNode> <DataNode TextLabel="RAMP3 " GraphId="a282b" Type="Protein" GroupRef="a4e3e"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-420147" /> <Attribute Key="copies_num" Value="3" /> <Graphics CenterX="100.0" CenterY="1082.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O60896" /> </DataNode> <DataNode TextLabel="VIP(125-152)" GraphId="a2c10" Type="Protein"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="1143.5" CenterY="752.5" Width="93.0" Height="29.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01282" /> </DataNode> <DataNode TextLabel="FZD5 " GraphId="a31e2" Type="Protein" GroupRef="bf57d"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-517468" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="660.0" CenterY="1122.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13467" /> </DataNode> <DataNode TextLabel="SCTR " GraphId="a37d9" Type="Protein" GroupRef="ee783"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-420082" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="1080.0" CenterY="1442.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P47872" /> </DataNode> <DataNode TextLabel="CALCB(82-118) " GraphId="a5994" Type="Protein" GroupRef="ea57d"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-419795" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1182.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P10092" /> </DataNode> <DataNode TextLabel="AMY1-3:IAPP(34-70)" GraphId="a5ad4" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="487.5" CenterY="131.0" Width="113.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-420147" /> </DataNode> <DataNode TextLabel="PTCH2 " GraphId="a5bbf" Type="Protein" GroupRef="a8eb3"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-445147" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="380.0" CenterY="1422.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y6C5" /> </DataNode> <DataNode TextLabel="CRH,UCN,UCN2,UCN3" GraphId="a602c" Type="Complex"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="1337.5" CenterY="77.5" Width="155.0" Height="21.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-8937627" /> </DataNode> <DataNode TextLabel="FZD5 " GraphId="a6b69" Type="Protein" GroupRef="fba92"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-517388" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="660.0" CenterY="882.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13467" /> </DataNode> <DataNode TextLabel="WNT6 " GraphId="a6cca" Type="Protein" GroupRef="fe098"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-517409" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1182.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y6F9" /> </DataNode> <DataNode TextLabel="GNB3 " GraphId="a73df" Type="Protein" GroupRef="bb7c2"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-422310" /> <Attribute Key="copies_num" Value="205" /> <Graphics 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<DataNode TextLabel="GNB5 " GraphId="a8166" Type="Protein" GroupRef="b8908"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-422314" /> <Attribute Key="copies_num" Value="243" /> <Graphics CenterX="800.0" CenterY="1482.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O14775" /> </DataNode> <DataNode TextLabel="GNG4 " GraphId="a829a" Type="Protein" GroupRef="b8908"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-422314" /> <Attribute Key="copies_num" Value="87" /> <Graphics CenterX="800.0" CenterY="1242.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P50150" /> </DataNode> <DataNode TextLabel="RAMP1 " GraphId="a84d9" Type="Protein" GroupRef="a4e3e"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" 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<Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-422314" /> <Attribute Key="copies_num" Value="22" /> <Graphics CenterX="800.0" CenterY="1142.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff" /> <Xref Database="ChEBI" ID="CHEBI:17552" /> </DataNode> <DataNode TextLabel="GIPR:GIP(52-93)" GraphId="a9ebe" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Graphics CenterX="338.0" CenterY="697.5" Width="108.0" Height="25.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-420229" /> </DataNode> <DataNode TextLabel="GNG8 " GraphId="aa2a3" Type="Protein" GroupRef="bb7c2"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-422310" /> <Attribute Key="copies_num" Value="135" /> <Graphics CenterX="940.0" CenterY="1062.0" Width="100.0" Height="20.0" ZOrder="32768" 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<Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-420258" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="1080.0" CenterY="942.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P01286" /> </DataNode> <DataNode TextLabel="FZD2 " GraphId="aa6f2" Type="Protein" GroupRef="fba92"> <Attribute Key="cellular_location" Value="plasma membrane" /> <Attribute Key="complex_id" Value="R-HSA-517388" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="660.0" CenterY="962.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14332" /> </DataNode> <DataNode TextLabel="CGRP ligands" GraphId="aa7bb" Type="Complex"> <Attribute Key="cellular_location" Value="extracellular region" /> <Graphics CenterX="603.5" CenterY="72.0" Width="87.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" 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<Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1342.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P10092" /> </DataNode> <DataNode TextLabel="PTHLH " GraphId="b64c8" Type="Protein" GroupRef="fa3e7"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-420503" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1242.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P12272" /> </DataNode> <DataNode TextLabel="WNT2 " GraphId="b786e" Type="Protein" GroupRef="fe098"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-517409" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1082.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref 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<Attribute Key="complex_id" Value="R-HSA-444765" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="1080.0" CenterY="1502.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9UHX3" /> </DataNode> <DataNode TextLabel="WNT6 " GraphId="ba072" Type="Protein" GroupRef="bf57d"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-517468" /> <Attribute Key="copies_num" Value="9" /> <Graphics CenterX="660.0" CenterY="1422.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y6F9" /> </DataNode> <DataNode TextLabel="WNT8B " GraphId="ba0fa" Type="Protein" GroupRef="bf57d"> <Attribute Key="cellular_location" Value="extracellular region" /> <Attribute Key="complex_id" Value="R-HSA-517468" /> <Attribute Key="copies_num" Value="13" /> <Graphics CenterX="660.0" CenterY="1502.0" Width="100.0" Height="20.0" 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This provides a path to calcium-regulated kinases and phosphatases, GEFs, MAP kinase cassettes and other proteins that mediate cellular responses ranging from granule secretion, integrin activation, and aggregation in platelets. Gq participates in many other signalling events including direct interaction with RhoGEFs that stimulate RhoA activity and inhibition of PI3K. Both in vitro and in vivo, the G-protein Gq seems to be the predominant mediator of the activation of platelets. Moreover, G alpha (q) can stimulate the activation of Burton tyrosine kinase (Ma Y C et al. 1998). 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These peptides exert their effects through binding and activation of two class B/Secretin family of GPCRs, CRHR1 and CRHR2 (aka CRFR1 and CRFR2 respectively). The corticotropin-releasing factor-binding protein (CRHBP) can bind to CRH with high affinity, inactivating it. CRHBP is expressed in the brains of all species examined to date but is uniquely expressed in human liver and placenta. In the brain, CRHBP is located in pituitary corticotropes, where it is under positive glucocorticoid control, and is likely to locally modulate CRH-induced ACTH secretion (Behan et al. 1993, Behan et al. 1995).</Comment> <BiopaxRef>efc</BiopaxRef> <BiopaxRef>f23</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1234.0" Y="32.0" /> <Point X="1299.0" Y="32.0" /> <Anchor Position="0.0" Shape="None" GraphId="f2d07" /> <Anchor Position="0.99" Shape="None" GraphId="f002d" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8937613" /> </Interaction> <Interaction GraphId="a3d4d"> <Comment Source="Reactome">Growth hormone-releasing hormone (GHRH, somatocrinin, growth hormone-releasing factor) (Gubler U et al, 1983) is released from neurosecretory cells in the hypothalamus and along with the inhibitory peptide, somatostatin, mediates the neuroendocrine regulation of pituitary growth hormone synthesis and secretion. The GHRH receptor (Gaylinn BD et al, 1993) is expressed in the pituitary gland and mediates the activity of GHRH. Downstream signalling is mediated by coupling to the G protein alpha s subunit, which stimulates adenylyl cyclase which increases intracellular cAMP levels (Mayo KE, 1992).</Comment> <BiopaxRef>b0e</BiopaxRef> <BiopaxRef>e9d</BiopaxRef> <BiopaxRef>f46</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="914.0" Y="723.0" /> <Point X="978.0" Y="713.0" /> <Anchor Position="0.0" Shape="None" GraphId="b11c3" /> <Anchor Position="0.99" Shape="None" GraphId="a8bf1" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420243" /> </Interaction> <Interaction GraphId="a416f"> <Comment Source="Reactome">The calcitonin gene-related peptides alpha-CGRP and beta-CGRP (Morris HR et al, 1984, Steenbergh PH et al, 1985 respectively) are members of the calcitonin family of peptides and are produced in both peripheral and central neurons. They are the most potent peptide vasodilators and can function in the transmission of pain. Their effects are mediated by binding to the CGRP1 receptor (CL) (Aiyar N et al, 1996). CGRP receptors are complexes between CL and receptor activity modifying protein 1 (RAMP1) (Kuwasako K et al, 2004). 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It is synthesized and secreted from endocrine cells in the small intestine. GIP induces insulin secretion, which is primarily stimulated by hyperosmolarity of glucose in the duodenum. Gastric inhibitory polypeptide receptors are found on beta-cells in the pancreas (Volz A et al, 1995). Their effects are mediated by coupling to the G protein alpha s subunit, which stimulates adenylyl cyclase which can increase intracellular cAMP levels (Bollag RJ et al, 2000).</Comment> <BiopaxRef>d10</BiopaxRef> <BiopaxRef>ba5</BiopaxRef> <BiopaxRef>b7e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="270.0" Y="725.0" /> <Point X="319.0" Y="713.0" /> <Anchor Position="0.0" Shape="None" GraphId="ed181" /> <Anchor Position="0.99" Shape="None" GraphId="f550f" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420274" /> </Interaction> <Interaction GraphId="ce563"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="898.0" Y="711.0" GraphRef="e0c93" RelX="-0.01818181818181818" RelY="1.0" /> <Point X="914.0" Y="723.0" GraphRef="b11c3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420243" /> </Interaction> <Interaction GraphId="cea03"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="194.0" Y="116.0" GraphRef="ac234" RelX="0.5900000000000034" RelY="0.0799999999999983" /> <Point X="183.0" Y="137.0" GraphRef="ba112" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-419843" /> </Interaction> <Interaction GraphId="cfb7b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1395.0" Y="123.0" GraphRef="e754e" RelX="0.0" RelY="-1.0" /> <Point X="1394.0" Y="104.0" GraphRef="b713b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8937631" /> </Interaction> <Interaction GraphId="d0189"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2297.0" Y="114.0" GraphRef="b7529" RelX="0.6199999999998909" RelY="0.1700000000000017" /> <Point X="2325.0" Y="117.0" GraphRef="ad341" RelX="-0.008849557522123894" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-201708" /> </Interaction> <Interaction GraphId="d3f5c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="708.0" Y="739.0" GraphRef="ed7a0" RelX="0.0" RelY="-1.0" /> <Point X="732.0" Y="723.0" GraphRef="ca9c6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420123" /> </Interaction> <Interaction GraphId="d411d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1928.0" Y="128.0" GraphRef="cbd14" RelX="0.9775280898876404" RelY="-0.03225806451612903" /> <Point X="1962.0" Y="181.0" GraphRef="a0a7f" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-445124" /> </Interaction> <Interaction GraphId="d5640"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1381.0" Y="751.0" GraphRef="e0797" RelX="0.0" RelY="-1.0" /> <Point X="1390.0" Y="734.0" GraphRef="cbe53" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420131" /> </Interaction> <Interaction GraphId="d5dd9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2121.0" Y="711.0" GraphRef="e9f64" RelX="0.5500000000001819" RelY="-0.12000000000000455" /> <Point X="2144.0" Y="708.0" GraphRef="d2499" RelX="-0.010101010101010102" RelY="1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444773" /> </Interaction> <Interaction GraphId="d7f20"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="109.0" Y="136.0" GraphRef="b943b" RelX="1.0" RelY="0.0" /> <Point X="135.0" Y="108.0" GraphRef="f6b4f" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-419843" /> </Interaction> <Interaction GraphId="d98ec"> <Comment Source="Reactome">Corticoliberin (CRH, aka corticotropin-releasing factor CRF) is a 41-amino acid amino peptide which, together with CRH-related peptides such as the urocortins (UCNs), plays a role in coordinating endocrine, autonomic and behavioral responses to stress. These peptides exert their effects through binding and activation of two class B/Secretin family of GPCRs, CRHR1 and CRHR2 (aka CRFR1 and CRFR2 respectively). The activity of these receptors is mediated by coupling to the G protein alpha s subunit, stimulating adenylyl cyclase which increases intracellular cAMP levels (Donaldson et al. 1996). CRH and UCN bind with highest affinity to both CRHR1 and CRHR2 receptors but CRHR2-beta receptors can also bind UCN2 and UCN3 (Pal et al. 2010).</Comment> <BiopaxRef>d2a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1394.0" Y="104.0" /> <Point X="1461.0" Y="114.0" /> <Anchor Position="0.0" Shape="None" GraphId="b713b" /> <Anchor Position="0.99" Shape="None" GraphId="fad0a" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8937631" /> </Interaction> <Interaction GraphId="da0c2"> <Comment Source="Reactome">Glucagon-like peptide 2 (GLP-2) (Drucker DJ 1999) is a 33-aa proglucagon-derived peptide produced by intestinal enteroendocrine cells. GLP-2 stimulates intestinal growth. The effects of GLP-2 are mediated by the GLP2 receptor (Munroe DG et al, 1999), which can couple with G protein alpha s subunit that activates adenylyl cyclase (Koehler JA et al, 2005).</Comment> <BiopaxRef>ce2</BiopaxRef> <BiopaxRef>d8e</BiopaxRef> <BiopaxRef>a88</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="732.0" Y="723.0" /> <Point X="781.0" Y="714.0" /> <Anchor Position="0.0" Shape="None" GraphId="ca9c6" /> <Anchor Position="0.99" Shape="None" GraphId="ccae5" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420123" /> </Interaction> <Interaction GraphId="dc379"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="573.0" Y="732.0" GraphRef="a62eb" RelX="0.5800000000000409" RelY="-0.15999999999996817" /> <Point X="604.0" Y="729.0" GraphRef="a1a62" RelX="0.0" RelY="1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-381612" /> </Interaction> <Interaction GraphId="dddb2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="67.0" Y="738.0" GraphRef="c4e1c" RelX="0.0" RelY="-1.0" /> <Point X="72.0" Y="722.0" GraphRef="f1172" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-163625" /> </Interaction> <Interaction GraphId="dee12"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="463.0" Y="110.0" GraphRef="fc343" RelX="0.7699999999999818" RelY="0.09000000000000341" /> <Point X="487.0" Y="113.0" GraphRef="a5ad4" RelX="-0.008849557522123894" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420265" /> </Interaction> <Interaction GraphId="e1219"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="385.0" Y="134.0" GraphRef="f7b16" RelX="0.9649122807017544" RelY="0.0" /> <Point X="386.0" Y="101.0" GraphRef="f18a9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420265" /> </Interaction> <Interaction GraphId="e1bd2"> <Comment Source="Reactome">Glucagon-like Peptide-1 is synthesized in intestinal L-cells in response to the presence of glucose and fatty acids absorbed from the intestine. Most GLP-1 is the GLP-1 (7-36) amidated form; some GLP-1 is the GLP-1 (7-37) form. GLP-1 circulates to the pancreas where it binds the Glucagon-like Peptide-1 Receptor (GLP-1R), a G-protein coupled receptor located on the plasma membrane of beta cells. GLP-1R is a seven-pass transmembrane protein and a member of the B family of GPCRs, which have N-terminal extracellular domains of 100-150 amino acids. GLP-1 interacts with the extracellular N-terminal region of GLP-1R.</Comment> <BiopaxRef>e1b</BiopaxRef> <BiopaxRef>a41</BiopaxRef> <BiopaxRef>f0d</BiopaxRef> <BiopaxRef>c17</BiopaxRef> <BiopaxRef>cf7</BiopaxRef> <BiopaxRef>eca</BiopaxRef> <BiopaxRef>acc</BiopaxRef> <BiopaxRef>e8b</BiopaxRef> <BiopaxRef>c7d</BiopaxRef> <BiopaxRef>fda</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="515.0" Y="748.0" /> <Point X="573.0" Y="732.0" /> <Anchor Position="0.0" Shape="None" GraphId="bd498" /> <Anchor Position="0.99" Shape="None" GraphId="a62eb" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-381612" /> </Interaction> <Interaction GraphId="e1f70"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1260.0" Y="113.0" GraphRef="d282a" RelX="0.7400000000000091" RelY="0.21999999999999886" /> <Point X="1240.0" Y="134.0" GraphRef="e0006" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420173" /> </Interaction> <Interaction GraphId="e2493"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="723.0" Y="698.0" GraphRef="bac00" RelX="1.0" RelY="0.0" /> <Point X="732.0" Y="723.0" GraphRef="ca9c6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420123" /> </Interaction> <Interaction GraphId="e3a53"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1608.0" Y="694.0" GraphRef="c5e0c" RelX="0.9487179487179487" RelY="0.0" /> <Point X="1620.0" Y="716.0" GraphRef="bce89" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420202" /> </Interaction> <Interaction GraphId="e49dc"> <Comment Source="Reactome">The pituitary adenylate cyclase-activating peptide (PACAP) (Ohkubo S et al, 1992) is a peptide hormone similar to vasoactive intestinal peptide (VIP). PACAP functions as a hypophysiotropic hormone, neurotransmitter and neuromodulator. Three active peptides are cleaved from the precursor protein; PACAP-related peptide, PACAP-27 and PACAP-38. The effects of the PACAP peptides are mediated by the PACAP receptor (Ogi K et al, 1993). This receptor is predominantly expressed in the CNS. The activity of the receptor is mediated by coupling with the G protein alpha s subunit, which stimulates adenylyl cyclase which increases intracellular cAMP levels (Ogi K et al, 1993).</Comment> <BiopaxRef>b8e</BiopaxRef> <BiopaxRef>b39</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1390.0" Y="734.0" /> <Point X="1454.0" Y="722.0" /> <Anchor Position="0.0" Shape="None" GraphId="cbe53" /> <Anchor Position="0.99" Shape="None" GraphId="f926e" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420131" /> </Interaction> <Interaction GraphId="e5419"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="697.0" Y="113.0" GraphRef="dcc73" RelX="0.4700000000000273" RelY="0.09999999999999432" /> <Point X="700.0" Y="131.0" GraphRef="cc9e4" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420127" /> </Interaction> <Interaction GraphId="e55d0"> <Comment Source="Reactome">Intermedin (AM2) (Roh J et al, 2004) and adrenomedullin (AM) (Kitamura K et al, 1993) belong to the calcitonin peptide hormone family and are important for cardiovascular and respiratory regulation. The functional adrenomedullin receptor AM1 is composed of the calcitonin gene-related peptide receptor (CGPR) and receptor activity modifying protein 2 (RAMP2) (Kamitani S et al, 1999). AM1 receptor can bind either of these peptide hormones and its activity is mediated by coupling with the G protein alpha s subunit which stimulates adenylyl cyclase and increases intracellular cAMP levels (Aiyar N et al, 2001). The function of the AM2 receptor (formed by the combination of CGPR and RAMP3) is very similar to that of AM1.</Comment> <BiopaxRef>ba3</BiopaxRef> <BiopaxRef>d05</BiopaxRef> <BiopaxRef>d3e</BiopaxRef> <BiopaxRef>f9e</BiopaxRef> <BiopaxRef>d98</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="931.0" Y="96.0" /> <Point X="987.0" Y="112.0" /> <Anchor Position="0.0" Shape="None" GraphId="e77a3" /> <Anchor Position="0.99" Shape="None" GraphId="f19e3" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420214" /> </Interaction> <Interaction GraphId="e6763"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="529.0" Y="703.0" GraphRef="c329b" RelX="1.0" RelY="0.0" /> <Point X="515.0" Y="748.0" GraphRef="bd498" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-381612" /> </Interaction> <Interaction GraphId="e793b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1147.0" Y="50.0" GraphRef="fe2ad" RelX="1.0" RelY="0.0" /> <Point X="1186.0" Y="91.0" GraphRef="ac286" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420173" /> </Interaction> <Interaction GraphId="e95c2"> <Comment Source="Reactome">Corticoliberin (CRH, aka corticotropin-releasing factor CRF) is a 41-amino acid amino peptide which, together with CRH-related peptides such as the urocortins (UCNs), play a role in coordinating endocrine, autonomic and behavioural responses to stress. These peptides exert their effects through binding and activation of two class B/Secretin family of GPCRs, CRHR1 and CRHR2 (aka CRFR1 and CRFR2 respectively). The activity of these receptors is mediated by coupling to the G protein alpha s subunit, stimulating adenylyl cyclase which increases intracellular cAMP levels (Donaldson et al. 1996). CRH and UCN bind with highest affinity to both CRHR1 and CRHR2-alpha receptors (Donaldson et al. 1996, Pioszak et al. 2008, Pal et al. 2010).</Comment> <BiopaxRef>df7</BiopaxRef> <BiopaxRef>af9</BiopaxRef> <BiopaxRef>d2a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1186.0" Y="91.0" /> <Point X="1260.0" Y="113.0" /> <Anchor Position="0.0" Shape="None" GraphId="ac286" /> <Anchor Position="0.99" Shape="None" GraphId="d282a" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420173" /> </Interaction> <Interaction GraphId="e982b"> <Comment Source="Reactome">The EGF-TM7 receptors are within the family B Adhesion (LNB) receptor subclass. They are characterised by long N-teminal extracellular domains containing multiple epidermal growth factor (EGF)-like domains. CD97 and EMR2 interact with the glycosaminoglycan chondroitin sulfate (CS).</Comment> <BiopaxRef>ec4</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2066.0" Y="723.0" /> <Point X="2121.0" Y="711.0" /> <Anchor Position="0.0" Shape="None" GraphId="a84a6" /> <Anchor Position="0.99" Shape="None" GraphId="e9f64" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444773" /> </Interaction> <Interaction GraphId="eaa98"> <Comment Source="Reactome">Secretin (SCT) (Whitmore TE et al, 2000) is a peptide hormone belonging to the glucagon peptide hormone family and is produced in the duodenum. Its primary effect is to regulate the pH of the duodenal contents via the control of gastric acid secretion and buffering with bicarbonate. These effects are mediated by the SCT receptor (Patel DR et al, 1995). The receptor activity is mediated by coupling to G protein alpha s subunits, which stimulate adenylyl cyclase which increases intracellular cAMP levels (Patel DR et al, 1995).</Comment> <BiopaxRef>b5c</BiopaxRef> <BiopaxRef>bd4</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1620.0" Y="716.0" /> <Point X="1663.0" Y="710.0" /> <Anchor Position="0.0" Shape="None" GraphId="bce89" /> <Anchor Position="0.99" Shape="None" GraphId="d6e3e" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420202" /> </Interaction> <Interaction GraphId="eab47"> <Comment Source="Reactome">The CALC1 gene produces a prepropeptide from which calcitonin (CT) is a cleavage product (Nelkin BD et al, 1984). CT is a polypeptide hormone that is produced in the thyroid gland. It acts to reduce blood calcium, opposing the effects of parathyroid hormone. The CT receptor (Gorn AH et al, 1992) binds CT and mediates its actions. The ligand:receptor complex couples to the G protein alpha s subunit, which stimulates adenylyl cyclase and increases intracellular cAMP levels (Gorn AH et al, 1992).</Comment> <BiopaxRef>d25</BiopaxRef> <BiopaxRef>d1b</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="135.0" Y="108.0" /> <Point X="194.0" Y="116.0" /> <Anchor Position="0.0" Shape="None" GraphId="f6b4f" /> <Anchor Position="0.99" Shape="None" GraphId="ac234" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-419843" /> </Interaction> <Interaction GraphId="ec89f"> <Comment Source="Reactome">The highly conserved Wnt signaling proteins play critical roles in guiding pattern formation, cell fate decision, and morphogenetic movement during animal development. They bind to the Frizzled (FZD) family of seven-pass transmembrane proteins and initiate at least three different intracellular signaling pathways. Historically they were considered to be family B GPCRs but more recent phylogenetic classifications put them into a class of their own (e.g. Schioth &amp; Fredriksson 2005). FZD members have been demonstrated to signal via Gi/o (Slusarski et al. 1997) but this is not considered to be the primary signaling mechanism for these receptors (Hsieh 2004). Instead they signal through the canonical/beta-catenin pathway, the planar cell polarity (PCP) pathway and the Wnt/Ca2+ pathway. The canonical/beta-catenin pathway requires a co-receptor protein known as LDL5 or LDL6 (Tamai et al. 2000). &lt;br&gt;Most Wnt signaling has been attributed to the activation of FZD receptors but there is evidence of FZD-independent signaling (Mikels &amp; Nusse 2006). Much Wnt research has used indirect evidence to infer the involvement of FZD receptors (e.g. Gazit et al. 1999) but there is some direct evidence of Wnt-FZD binding (Hsieh et al. 1999; Mikels &amp; Nusse 2006).</Comment> <BiopaxRef>cc5</BiopaxRef> <BiopaxRef>d00</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2235.0" Y="97.0" /> <Point X="2297.0" Y="114.0" /> <Anchor Position="0.0" Shape="None" GraphId="aa3c9" /> <Anchor Position="0.99" Shape="None" GraphId="b7529" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-201708" /> </Interaction> <Interaction GraphId="ede2c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1879.0" Y="678.0" GraphRef="f262a" RelX="0.7300000000000182" RelY="0.12000000000000455" /> <Point X="1902.0" Y="681.0" GraphRef="bf444" RelX="-0.011764705882352941" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-879674" /> </Interaction> <Interaction GraphId="ef13a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1636.0" Y="75.0" GraphRef="f8b24" RelX="-0.010101010101010102" RelY="0.9428571428571428" /> <Point X="1655.0" Y="96.0" GraphRef="c61d6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420489" /> </Interaction> <Interaction GraphId="efd54"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="915.0" Y="67.0" GraphRef="e1a87" RelX="0.9733333333333334" RelY="0.0" /> <Point X="931.0" Y="96.0" GraphRef="e77a3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420214" /> </Interaction> <Interaction GraphId="f031b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1461.0" Y="114.0" GraphRef="fad0a" RelX="0.6700000000000728" RelY="0.09999999999999432" /> <Point X="1443.0" Y="135.0" GraphRef="e197d" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8937631" /> </Interaction> <Interaction GraphId="f1880"> <Comment Source="Reactome">CD55 (or Decay Accelerating Factor; DAF) is a member of the regulators of complement activation (RCA) family. It protects host cells from complement system attack by binding to C3b and C4b preventing formation of the membrane attack complex. CD97 is a member of the Adhesion class or LNB subfamily of family B GPCRs, characterized by long N-terminal regions containing domains contain multiple tandem epidermal growth factor (EGF)-like repeats in their N-termini (Foord et al. 2002). CD97 is constitutively expressed on granulocytes and monocytes and is rapidly up-regulated on activated T and B cells. It is known to have many splice forms containing different numbers of EGF domains, consequently binding CD55 with differing affinities. The highest affinity variant has three EGF domains. The leukocyte-restricted expression pattern of CD97, and the presence of both CD97 and CD55 in arthritic joints suggest a possible role in adhesion and signaling within the inflammatory and immune responses (Lin et al. 2001).</Comment> <BiopaxRef>be5</BiopaxRef> <BiopaxRef>ece</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1806.0" Y="666.0" /> <Point X="1879.0" Y="678.0" /> <Anchor Position="0.0" Shape="None" GraphId="f7ed2" /> <Anchor Position="0.99" Shape="None" GraphId="f262a" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-879674" /> </Interaction> <Interaction GraphId="f1a6b"> <Comment Source="Reactome">Parathyroid hormone (PTH) (Hendy GN et al, 1981), parathyroid hormone-related protein (PTHrP) (Suva LJ et al, 1987) and tuberoinfundibular peptide of thirty-nine residues (TIP39) (Hansen IA et al, 2002; Della Penna K et al, 2003) are endogenous ligands for the parathyroid hormone 1 and 2 receptors. These peptide hormones play a key role in controlling blood Ca(2+) concentration and endochondral bone formation. PTH1 is the classical PTH receptor 1 (Schipani E et al, 1993; Schneider H et al, 1993) and is expressed in high levels in bone and kidney. It regulates calcium ion homeostasis through activation of adenylate cyclase and phospholipase C. PTH receptor 2 (Usdin TB et al, 1995) is most abundant in brain and testes and potently activated by PTH. The activity of these receptors is mediated by G proteins which activate adenylyl cyclase (Schneider H et al, 1994; Offermanns S et al, 1996; Behar V et al, 1996).</Comment> <BiopaxRef>adb</BiopaxRef> <BiopaxRef>f4f</BiopaxRef> <BiopaxRef>dad</BiopaxRef> <BiopaxRef>a3b</BiopaxRef> <BiopaxRef>de4</BiopaxRef> <BiopaxRef>d20</BiopaxRef> <BiopaxRef>df1</BiopaxRef> <BiopaxRef>a9f</BiopaxRef> <BiopaxRef>b08</BiopaxRef> <BiopaxRef>d68</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1655.0" Y="96.0" /> <Point X="1710.0" Y="108.0" /> <Anchor Position="0.0" Shape="None" GraphId="c61d6" /> <Anchor Position="0.99" Shape="None" GraphId="dfc3c" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420489" /> </Interaction> <Interaction GraphId="f1d08"> <Comment Source="Reactome">Smoothened (Smo) is usually classified with family B GPCRs based on homology. There are indications that it can signal via G-proteins Gi and G12/13 (Ruiz-Gomez, 2007) but this role is poorly understood. It's better characterised physiological role is as the transducer of hedgehog (HH) signaling. In this capacity Smo is not acting as a receptor, but as part of a signaling cascade. &lt;br&gt; &lt;br&gt; The Hedgehog(HH)/Smo signalling pathway was identified as a key component of Drosophila development and subsequently found to be conserved in all meatazoans. Most of the functions attributed to Smo are associated with development such as digit patterning in the chick limb bud and left–right asymmetry of vertebrate embryos. In addition, Smo appears to be involved in homeostasis; deregulated Smo signaling is implicated in tumorogenesis (Ruiz-Gomez, 2007). &lt;br&gt; &lt;br&gt; The ligand of the 12 transmembrane-domain receptor Patched (Ptc) is Hedgehog(HH) but in the absence of HH, Ptc binds Smo (Stone et al. 1996) which consequently becomes internalised into endosomes, where it associates with Costal-2 (Cos2), and lysosomes, where it is degraded. This 'inactivates' Smo by preventing the formation of an active Smo signaling complex at the plasma membrane. Internalised Smo:Cos2 forms a complex with protein kinase A (PKA), casein kinase I (CKI) glycogen synthase kinase-3 (GSK3) and Cucurbitus interruptus (Ci), a transcriptional regulator, enabling phosphorylation of Ci and subsequent processing to a transcriptional repressor form (CiR). When HH binds to Ptc, it does not bind Smo, allowing Smo to undergo a conformational change, exposing a new surface in its cytoplasmic tail. This causes PKA, CKI and GSK3 to dissociate from Smo:Cos2 complexes, so that Ci is no longer phosphorylated or processed to CiR. Accumulating Smo is phosphorylated instead and assumes a third conformational state. Phosphorylated Smo trafficks to the plasma membrane (Denef et al. 2000) and assembles into a signalling complex that promotes the phosphorylation of Fused (Fu) and Cos2. Phosphorylated Cos2 dissociates from membranes and recruits Fu to Sufu (Suppressor of Fused), which produces the activated form of Ci (CiA), probably through phosphorylation of Sufu (Hooper &amp; Scott, 2005).</Comment> <BiopaxRef>cb8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1962.0" Y="181.0" /> <Point X="2038.0" Y="149.0" /> <Anchor Position="0.0" Shape="None" GraphId="a0a7f" /> <Anchor Position="0.99" Shape="None" GraphId="b1dff" /> <Anchor Position="0.5" Shape="None" GraphId="fd53e" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-445124" /> </Interaction> <Interaction GraphId="f3114"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1710.0" Y="108.0" GraphRef="dfc3c" RelX="0.5499999999999545" RelY="0.12000000000000455" /> <Point X="1697.0" Y="136.0" GraphRef="fb586" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420489" /> </Interaction> <Interaction GraphId="f4115"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1454.0" Y="722.0" GraphRef="f926e" RelX="0.6400000000001" RelY="-0.12000000000000455" /> <Point X="1433.0" Y="701.0" GraphRef="b3492" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420131" /> </Interaction> <Interaction GraphId="f5cf0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1223.0" Y="54.0" GraphRef="a1cb8" RelX="1.0" RelY="0.0" /> <Point X="1234.0" Y="32.0" GraphRef="f2d07" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-8937613" /> </Interaction> <Interaction GraphId="f685e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1828.0" Y="684.0" GraphRef="cdfdc" RelX="0.0" RelY="-1.0" /> <Point X="1806.0" Y="666.0" GraphRef="f7ed2" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-879674" /> </Interaction> <Interaction GraphId="f6f4c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1231.0" Y="715.0" GraphRef="b8cb3" RelX="0.40000000000009095" RelY="-0.12000000000000455" /> <Point X="1260.0" Y="712.0" GraphRef="b2dfb" RelX="-0.009708737864077669" RelY="1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420233" /> </Interaction> <Interaction GraphId="f7fc4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2072.0" Y="697.0" GraphRef="e2599" RelX="0.9726027397260274" RelY="0.0" /> <Point X="2066.0" Y="723.0" GraphRef="a84a6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-444773" /> </Interaction> <Interaction GraphId="f8978"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="253.0" Y="737.0" GraphRef="ef188" RelX="-0.012048192771084338" RelY="-1.0" /> <Point X="270.0" Y="725.0" GraphRef="ed181" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420274" /> </Interaction> <Interaction GraphId="f8a3d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="520.0" Y="783.0" GraphRef="e0ce0" RelX="1.0" RelY="0.0" /> <Point X="515.0" Y="748.0" GraphRef="bd498" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-381612" /> </Interaction> <Interaction GraphId="fa2e6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2205.0" Y="85.0" GraphRef="c2743" RelX="0.9512195121951219" RelY="0.0" /> <Point X="2235.0" Y="97.0" GraphRef="aa3c9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-201708" /> </Interaction> <Interaction GraphId="fc574"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="987.0" Y="112.0" GraphRef="f19e3" RelX="0.5599999999999454" RelY="0.1599999999999966" /> <Point X="1018.0" Y="115.0" GraphRef="c81c5" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420214" /> </Interaction> <Interaction GraphId="fceca"> <Comment Source="Reactome">Vasoactive intestinal peptide (VIP) (Tsukada T et al, 1985) belongs to the glucagon hormone family and is expressed in many parts of the human body. VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial muscle contraction and increases glycogenolysis. It also relaxes the smooth muscle of trachea, stomach and gall bladder. The effects of VIP are mediated by the VIP receptors of which there are two, 1 and 2 (Sreedharan SP et al, 1993 and Svodoba M et al, 1994 respectively). The actions of the receptor are mediated by coupling with the G protein alpha s subunit, which stimulates adenylyl cyclase which increases intracellular cAMP levels (Sreedharan SP et al, 1993).</Comment> <BiopaxRef>c52</BiopaxRef> <BiopaxRef>ae3</BiopaxRef> <BiopaxRef>d27</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1191.0" Y="727.0" /> <Point X="1231.0" Y="715.0" /> <Anchor Position="0.0" Shape="None" GraphId="f57f5" /> <Anchor Position="0.99" Shape="None" GraphId="b8cb3" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420233" /> </Interaction> <Interaction GraphId="fd1bd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="896.0" Y="735.0" GraphRef="fdb62" RelX="-0.022222222222222223" RelY="-1.0" /> <Point X="914.0" Y="723.0" GraphRef="b11c3" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-420243" /> </Interaction> <Interaction GraphId="fecbf"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2237.0" Y="141.0" GraphRef="ef4ad" RelX="0.9770114942528736" RelY="-0.02857142857142857" /> <Point X="2235.0" Y="97.0" GraphRef="aa3c9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-201708" /> </Interaction> <Interaction GraphId="ff0de"> <Comment Source="Reactome">Glucagon (Thomsen J et al, 1972) is an important peptide hormone produced by the pancreas. It is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin. Glucagon, together with glucagon-like peptide 1 (GLP-1) and glucagon-like peptide 2 (GLP-2), are peptide hormones encoded by a single common prohormone precursor, proglucagon.The glucagon receptor (Lok S et al, 1994) plays a central role in regulating the level of blood glucose by controlling the rate of hepatic glucose production and insulin secretion. 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<Group GroupId="bf57d" GraphId="f0f85" Style="Complex"> <Attribute Key="complex_id" Value="R-HSA-517468" /> </Group> <Group GroupId="aac4b" GraphId="f8bf4" Style="Complex"> <Attribute Key="complex_id" Value="R-HSA-420087" /> </Group> <Group GroupId="c73f3" GraphId="fbce5"> <Attribute Key="complex_id" Value="R-HSA-445134" /> </Group> <Group GroupId="a4e3e" GraphId="ff068" Style="Complex"> <Attribute Key="complex_id" Value="R-HSA-420147" /> </Group> <InfoBox CenterX="0.0" CenterY="0.0" /> <Biopax> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="ba3"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">14615490</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Intermedin is a calcitonin/calcitonin gene-related peptide family peptide acting through the calcitonin receptor-like 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<bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Aiyar N, Disa J, Pullen M, Nambi P.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="d68"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8770894</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The human PTH2 receptor: binding and signal transduction properties of the stably expressed recombinant receptor.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Behar V, Pines M, Nakamoto C, Greenberg Z, Bisello A, Stueckle SM, Bessalle R, Usdin TB, Chorev M, Rosenblatt M, Suva LJ.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" 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pancreas.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Doyle ME, Egan JM.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="af7"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">19212139</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Functions and regulatory mechanisms of Gq-signaling pathways.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Mizuno N, Itoh H.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="df8"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">6609312</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Isolation and characterization of human calcitonin gene-related peptide.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Morris HR, Panico M, Etienne T, Tippins J, Girgis SI, MacIntyre I.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="acc"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">18287102</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Runge S, Thøgersen H, Madsen K, Lau J, Rudolph R.</bp:AUTHORS> 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Jakob O, Wortmann S, Arzberger T, Allolio B, Blind E.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="b08"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8732687</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">G alpha q family members couple parathyroid hormone (PTH)/PTH-related peptide and calcitonin receptors to phospholipase C in COS-7 cells.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Offermanns S, Iida-Klein A, Segre GV, Simon MI.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="fda"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15569269</bp:ID> <bp:DB 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H, Qin F, Ding KH, Isales CM.</bp:AUTHORS> </bp:PublicationXref> </Biopax> </Pathway>

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Return to Class B/2 (secretin family receptors) (Homo sapiens).