ID A0A2K6Q8W1_RHIRO Unreviewed; 699 AA.
AC A0A2K6Q8W1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Lutropin-choriogonadotropic hormone receptor {ECO:0000256|ARBA:ARBA00022266, ECO:0000256|RuleBase:RU361222};
GN Name=LHCGR {ECO:0000256|RuleBase:RU361222,
GN ECO:0000313|Ensembl:ENSRROP00000025220.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000025220.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000025220.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The
CC activity of this receptor is mediated by G proteins which activate
CC adenylate cyclase. {ECO:0000256|RuleBase:RU361222}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000256|RuleBase:RU361222}.
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DR RefSeq; XP_010370054.1; XM_010371752.1.
DR AlphaFoldDB; A0A2K6Q8W1; -.
DR STRING; 61622.ENSRROP00000025220; -.
DR Ensembl; ENSRROT00000049436.1; ENSRROP00000025220.1; ENSRROG00000036358.1.
DR GeneID; 104668945; -.
DR KEGG; rro:104668945; -.
DR CTD; 3973; -.
DR GeneTree; ENSGT00940000157364; -.
DR OMA; FFRSFTH; -.
DR OrthoDB; 1202285at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0038106; F:choriogonadotropin hormone binding; IEA:Ensembl.
DR GO; GO:0035472; F:choriogonadotropin hormone receptor activity; IEA:Ensembl.
DR GO; GO:0004964; F:luteinizing hormone receptor activity; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0046544; P:development of secondary male sexual characteristics; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0022602; P:ovulation cycle process; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0090030; P:regulation of steroid hormone biosynthetic process; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
DR CDD; cd15359; 7tmA_LHCGR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002131; Gphrmn_rcpt_fam.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002273; LSH_rcpt.
DR PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24372:SF1; LUTROPIN-CHORIOGONADOTROPIC HORMONE RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF13306; LRR_5; 2.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01144; LSHRECEPTOR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361222};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU361222};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361222};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361222};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361222};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU361222};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361222};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361222}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT CHAIN 23..699
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT /id="PRO_5014210787"
FT TRANSMEM 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 483..506
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 526..551
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 572..594
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 376..623
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 699 AA; 78554 MW; 6D3F7C7F62C0BC7A CRC64;
MKQRFSALQL LKLLLLLQPL LPRALREARC PEPCDCAPDG ALRCPGPTAG LTRLSLAYLP
VKVIPSQAFR GLNEVVKIEI SQIDSLERIE ANAFDNLLNL SEILIQNTKN LRYIEPGAFI
NLPRLQYLSI CNTGIRKFPD VTKILSSELN FILEICDNLH ITTIPGNAFQ GMNNESVTLK
LYGNGFEEVQ SHAFNGTTLI SLELKENIHL EKMHNGAFRG AMGPKILDIS STKLQALPSY
GLESIQTLIA TSSHSLKKLP SREKFANLLE ATLTYPSHCC AFRNLPTKEQ NFSLSISENF
SKQCESTVRK LDNKTFYSAM LAESELSGWD YEYGFCLPKT PRCAPEPDAF NPCEDIMGYD
FLRVLIWLIN ILAIMGNMTV LFVLLTSRYK LTVPRFLMCN LSFADFCMGL YLLLIASVDS
QTKGQYYNHA IDWQTGSGCS TAGFFTVFAS ELSVYTLTVI TLERWHTITY AIHLDQKLRL
RHAILIMLGG WLFSSLIAML PLVGVSNYMK VSICFPMDVE TTLSQVYILT ILILNVVAFI
IICACYIKIY FAVQNPELMA TNKDTKIAKK MAILIFTDFT CMAPISFFAI SAAFKVPLIT
VTNSKVLLVL FYPINSCANP FLYAIFTKTF QRDFFLLLSK FGCCKHRAEL YRRKDFSAYT
SNCKNGFTGL NKPSQSTLKL STLHCQGTAL LDKTCYTEC
//
