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7Y89

Structure of the GPR17-Gi complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
C0000287molecular_functionmagnesium ion binding
C0001664molecular_functionG protein-coupled receptor binding
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005813cellular_componentcentrosome
C0005834cellular_componentheterotrimeric G-protein complex
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005938cellular_componentcell cortex
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
C0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
C0016020cellular_componentmembrane
C0019001molecular_functionguanyl nucleotide binding
C0019003molecular_functionGDP binding
C0030496cellular_componentmidbody
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0031749molecular_functionD2 dopamine receptor binding
C0031821molecular_functionG protein-coupled serotonin receptor binding
C0043434biological_processresponse to peptide hormone
C0043949biological_processregulation of cAMP-mediated signaling
C0046872molecular_functionmetal ion binding
C0051301biological_processcell division
C0060236biological_processregulation of mitotic spindle organization
C0070062cellular_componentextracellular exosome
C0072678biological_processT cell migration
C1904322biological_processcellular response to forskolin
C1904778biological_processpositive regulation of protein localization to cell cortex
G0005834cellular_componentheterotrimeric G-protein complex
G0007186biological_processG protein-coupled receptor signaling pathway
G0031681molecular_functionG-protein beta-subunit binding
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIyFLTCISADRFLaI
ChainResidueDetails
AALA145-ILE161

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
APHE65-ILE85
CASN269

site_idSWS_FT_FI2
Number of Residues41
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AARG86-THR92
AALA155-TYR175
AARG245-LYS260

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
APRO93-PRO113

site_idSWS_FT_FI4
Number of Residues71
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ATHR114-ARG133
ASER197-VAL223
AASN282-ARG308

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU134-SER154

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AALA176-VAL196

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
ASER224-ILE244

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AALA261-VAL281

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AILE309-ALA329

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN204
AASN282

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PDB entries from 2024-07-24

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