Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8KH5

Cryo-EM structure of the GPR174-Gs complex bound to endogenous lysoPS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0032703biological_processnegative regulation of interleukin-2 production
A0034451cellular_componentcentriolar satellite
A0035025biological_processpositive regulation of Rho protein signal transduction
A0043029biological_processT cell homeostasis
A0043231cellular_componentintracellular membrane-bounded organelle
A0045125molecular_functionbioactive lipid receptor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0001750cellular_componentphotoreceptor outer segment
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
C0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
C0007265biological_processRas protein signal transduction
C0008283biological_processcell population proliferation
C0016020cellular_componentmembrane
C0030159molecular_functionsignaling receptor complex adaptor activity
C0044877molecular_functionprotein-containing complex binding
C0045202cellular_componentsynapse
C0050909biological_processsensory perception of taste
C0051020molecular_functionGTPase binding
C0060041biological_processretina development in camera-type eye
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
C0097381cellular_componentphotoreceptor disc membrane
C1903561cellular_componentextracellular vesicle
D0005515molecular_functionprotein binding
D0005834cellular_componentheterotrimeric G-protein complex
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
D0016020cellular_componentmembrane
D0031681molecular_functionG-protein beta-subunit binding
D0048144biological_processfibroblast proliferation
D0070062cellular_componentextracellular exosome
D0071380biological_processcellular response to prostaglandin E stimulus
D0071870biological_processcellular response to catecholamine stimulus
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
CLEU70-SER84
CILE157-ILE171
CLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
DALA2
BSER54
BTHR204
BASP223
BLEU302
BPHE376

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
DSER68
ASER113-ASP134
ACYS204-MET231

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
DSER68

site_idSWS_FT_FI4
Number of Residues58
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AARG75-CYS91
AARG156-SER182
AASP253-VAL269

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AMET92-ILE112

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
ALEU135-LEU155

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AVAL183-TYR203

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AILE232-LEU252

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AILE270-VAL290

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN4
AASN164

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon