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7TRY

Cryo-EM structure of corticotropin releasing factor receptor 2 bound to Urocortin 1 and coupled with heterotrimeric G11 protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001501biological_processskeletal system development
A0001508biological_processaction potential
A0001664molecular_functionG protein-coupled receptor binding
A0001750cellular_componentphotoreceptor outer segment
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0007207biological_processphospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
A0007208biological_processphospholipase C-activating serotonin receptor signaling pathway
A0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
A0007507biological_processheart development
A0007603biological_processphototransduction, visible light
A0008217biological_processregulation of blood pressure
A0009649biological_processentrainment of circadian clock
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0030234molecular_functionenzyme regulator activity
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0032024biological_processpositive regulation of insulin secretion
A0045202cellular_componentsynapse
A0045634biological_processregulation of melanocyte differentiation
A0046872molecular_functionmetal ion binding
A0048066biological_processdevelopmental pigmentation
A0060158biological_processphospholipase C-activating dopamine receptor signaling pathway
A0070062cellular_componentextracellular exosome
A0071467biological_processcellular response to pH
A0086100biological_processendothelin receptor signaling pathway
A1904888biological_processcranial skeletal system development
A1990806biological_processligand-gated ion channel 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
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
P0004888molecular_functiontransmembrane signaling receptor activity
P0004930molecular_functionG protein-coupled receptor activity
P0007166biological_processcell surface receptor signaling pathway
P0007186biological_processG protein-coupled receptor signaling pathway
P0016020cellular_componentmembrane
U0005179molecular_functionhormone activity
U0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00511
Number of Residues16
DetailsCRF Corticotropin-releasing factor family signature. PsLSIdlTFhLLRtlL
ChainResidueDetails
UPRO3-LEU18

site_idPS00649
Number of Residues26
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnttLDqigtCWprSaagalverpCP
ChainResidueDetails
PCYS40-PRO65

site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFFVsVFYCFfNgeV
ChainResidueDetails
PGLN351-VAL366

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 Residues30
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues13
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Valine amide","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35061538","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P27600","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Deamidated glutamine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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