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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7FII

luteinizing hormone/choriogonadotropin receptor-chorionic gonadotropin-Gs complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
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
R0001541biological_processovarian follicle development
R0004930molecular_functionG protein-coupled receptor activity
R0004964molecular_functionluteinizing hormone receptor activity
R0005768cellular_componentendosome
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0007283biological_processspermatogenesis
R0008528molecular_functionG protein-coupled peptide receptor activity
R0008584biological_processmale gonad development
R0008585biological_processfemale gonad development
R0009755biological_processhormone-mediated signaling pathway
R0016020cellular_componentmembrane
R0016500molecular_functionprotein-hormone receptor activity
R0022602biological_processovulation cycle process
R0030539biological_processmale genitalia development
R0032870biological_processcellular response to hormone stimulus
R0032962biological_processpositive regulation of inositol trisphosphate biosynthetic process
R0034451cellular_componentcentriolar satellite
R0034698biological_processresponse to gonadotropin
R0035472molecular_functionchoriogonadotropin hormone receptor activity
R0038106molecular_functionchoriogonadotropin hormone binding
R0042700biological_processluteinizing hormone signaling pathway
R0046544biological_processdevelopment of secondary male sexual characteristics
R0050890biological_processcognition
R0060065biological_processuterus development
R0071371biological_processcellular response to gonadotropin stimulus
R0071373biological_processcellular response to luteinizing hormone stimulus
R0072520biological_processseminiferous tubule development
R0090030biological_processregulation of steroid hormone biosynthetic process
X0005179molecular_functionhormone activity
X0005576cellular_componentextracellular region
Y0005179molecular_functionhormone activity
Y0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. LSVyTLTVITLERWHtI
ChainResidueDetails
RLEU452-ILE468
site_idPS00261
Number of Residues7
DetailsGLYCO_HORMONE_BETA_1 Glycoprotein hormones beta chain signature 1. CAGYCpT
ChainResidueDetails
YCYS34-THR40
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
site_idPS00689
Number of Residues28
DetailsGLYCO_HORMONE_BETA_2 Glycoprotein hormones beta chain signature 2. AVAlsCqCalCrrstTDCggpkdh..PltC
ChainResidueDetails
YALA83-CYS110
site_idPS00779
Number of Residues13
DetailsGLYCO_HORMONE_ALPHA_1 Glycoprotein hormones alpha chain signature 1. CmGCCFSRAYPTP
ChainResidueDetails
XCYS28-PRO40
site_idPS00780
Number of Residues14
DetailsGLYCO_HORMONE_ALPHA_2 Glycoprotein hormones alpha chain signature 2. NHTaChCsTCyyHK
ChainResidueDetails
XASN78-LYS91
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues48
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues51
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues19
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues21
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues22
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues21
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues22
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues21
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"source":"PubMed","id":"11847099","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"15539429","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000036","evidences":[{"source":"PubMed","id":"15662415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24692546","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MQW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000037","evidences":[{"source":"PubMed","id":"15662415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24692546","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MQW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000042","evidences":[{"source":"PDB","id":"1HRP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000043","evidences":[{"source":"PDB","id":"1HRP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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