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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7VQX

Cryo-EM structure of human vasoactive intestinal polypeptide receptor 2 (VIP2R) in complex with PACAP27 and Gs

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007606biological_processsensory perception of chemical stimulus
A0010856molecular_functionadenylate cyclase activator activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031698molecular_functionbeta-2 adrenergic receptor binding
A0031748molecular_functionD1 dopamine receptor binding
A0031852molecular_functionmu-type opioid receptor binding
A0035255molecular_functionionotropic glutamate receptor binding
A0046872molecular_functionmetal ion binding
A0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
B0001750cellular_componentphotoreceptor outer segment
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
L0005179molecular_functionhormone activity
L0005184molecular_functionneuropeptide hormone activity
L0005576cellular_componentextracellular region
R0001634molecular_functionpituitary adenylate cyclase-activating polypeptide receptor activity
R0004888molecular_functiontransmembrane signaling receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0004999molecular_functionvasoactive intestinal polypeptide receptor activity
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007166biological_processcell surface receptor signaling pathway
R0007186biological_processG protein-coupled receptor signaling pathway
R0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007267biological_processcell-cell signaling
R0008528molecular_functionG protein-coupled peptide receptor activity
R0016020cellular_componentmembrane
R0017046molecular_functionpeptide hormone binding
Functional Information from PROSITE/UniProt
site_idPS00260
Number of Residues23
DetailsGLUCAGON Glucagon / GIP / secretin / VIP family signature. HSDGIFtDSYsryrkqmaVKKYL
ChainResidueDetails
LHIS1-LEU23
site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CsgvWDnit.CWrpAnvgetvtvpCP
ChainResidueDetails
RCYS52-PRO76
site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLVVaVLYCFlNseV
ChainResidueDetails
RGLN367-VAL382
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
BVAL327-GLY341
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues26
DetailsPeptide: {"description":"Pituitary adenylate cyclase-activating polypeptide 27","featureId":"PRO_0000011489"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues8
DetailsRegion: {"description":"Important for receptor binding","evidences":[{"source":"PubMed","id":"17470806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Leucine amide","evidences":[{"source":"PubMed","id":"2302217","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues147
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues17
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"35477937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VQX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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