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7YDH

Cryo EM structure of CD97/miniG13 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0007266biological_processRho protein signal transduction
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
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
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
G0045202cellular_componentsynapse
G0048144biological_processfibroblast proliferation
G0070062cellular_componentextracellular exosome
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
R0004888molecular_functiontransmembrane signaling receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0007166biological_processcell surface receptor signaling pathway
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGAFLyLLHCLlNkkV
ChainResidueDetails
RGLN778-VAL793

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 Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P27601
ChainResidueDetails
AASN43
ASER47
AILE158
ACYS182
AARG188

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:12399457
ChainResidueDetails
AARG188
RARG643-ARG653
RTHR713-THR739
RASN790-ILE835

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:10747909
ChainResidueDetails
ASER3

site_idSWS_FT_FI4
Number of Residues39
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RGLU602-HIS620
RSER675-GLY691
RASP761-VAL766

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RTYR621-VAL642

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RTRP654-TYR674

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RPHE692-VAL712

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RILE740-PHE760

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RLEU767-LEU789

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000255|PROSITE-ProRule:PRU00098
ChainResidueDetails
RMET530

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER815
RSER818

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RTHR816
RTHR825

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER831

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
RSER833

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PDB entries from 2024-10-16

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