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Database: UniProt
Entry: A0A140T893_BOVIN
LinkDB: A0A140T893_BOVIN
Original site: A0A140T893_BOVIN 
ID   A0A140T893_BOVIN        Unreviewed;       701 AA.
AC   A0A140T893;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:ENSBTAP00000022047.5,
GN   ECO:0000313|VGNC:VGNC:111941};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000022047.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000022047.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022047.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000022047.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022047.5};
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A140T893; -.
DR   SMR; A0A140T893; -.
DR   Ensembl; ENSBTAT00000022047.6; ENSBTAP00000022047.5; ENSBTAG00000016573.6.
DR   VEuPathDB; HostDB:ENSBTAG00000016573; -.
DR   VGNC; VGNC:111941; LHCGR.
DR   GeneTree; ENSGT00940000157364; -.
DR   InParanoid; A0A140T893; -.
DR   OMA; TACIERD; -.
DR   Reactome; R-BTA-375281; Hormone ligand-binding receptors.
DR   Reactome; R-BTA-418555; G alpha (s) signalling events.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000016573; Expressed in diaphragm and 32 other cell types or tissues.
DR   ExpressionAtlas; A0A140T893; baseline.
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:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004964; F:luteinizing hormone receptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0042700; P:luteinizing hormone signaling pathway; IBA:GO_Central.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   GO; GO:0001541; P:ovarian follicle development; IBA:GO_Central.
DR   GO; GO:0022602; P:ovulation cycle process; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|RuleBase:RU361222};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641};
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..26
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   CHAIN           27..701
FT                   /note="Lutropin-choriogonadotropic hormone receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT                   /id="PRO_5007230467"
FT   TRANSMEM        366..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        399..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        443..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        485..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        528..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        574..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   DOMAIN          378..625
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
SQ   SEQUENCE   701 AA;  78456 MW;  D70AE862EB265CCF CRC64;
     MGRPSLALRL LLALLLLPPP APLLWALRPA PCPEPCSCPP DGALRCPGPQ AGLSRLSLTY
     LPIKVIPSQA FRGLNEVIKI EISQSDSLEK IEANAFDNLL NLSEILIQNT KNLVHIEAGA
     FTNLPRLKYL SICNTGIHKL PDVTKIFSSE FNFILEICDN LHITTIPRNA FQGMNNESIT
     LKLYGNGFEE IQSHAFNGTT LISLELKENA RLEKMHNDAF RGATGPSILD ISSTQLQALP
     TYGLESIQTL IATSSYSLKK LPSREKFTNL LDATLTYPSH CCAFRNLPTN EQNFSFSIFK
     NFSKQCESTA RRPNNETLYS AIFAESELSG WDYDYGFCLP KTLQCAPEPD AFNPCEDIMG
     YNFLRVLIWL INILAITGNV TVLFVLLTSR YKLTVPRFLM CNLSFADFCM GLYLLLIASV
     DAQTKGQYYN HAIDWQTGSG CSAAGFFTVF ASELSVYTLT VITLERWHTI TYAIQLDQKL
     RLKHAIPVML GGWLFSTLIA VLPLVGVSNY MKVSICLPMD VESTLSQVYI LTILILNVMA
     FIIICACYIK IYFAVQNPEL MATNKDTKIA KKMAVLIFTD FTCMAPISFF AISAAFKVPL
     ITVTNSKVLL VLFYPVNSCA NPFLYAIFTK AFQRDFFLLL SKFGCCKYRA ELYRRKDFSA
     YISNCKNGFT GSNKPSRSTF KLTTLQCQYS AVLDKTCYKE C
//
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