ID LSHR_BOVIN Reviewed; 701 AA.
AC Q28005; P79133; Q8SPS8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 08-NOV-2023, entry version 157.
DE RecName: Full=Lutropin-choriogonadotropic hormone receptor;
DE Short=LH/CG-R;
DE AltName: Full=Luteinizing hormone receptor;
DE Short=LSH-R;
DE Flags: Precursor;
GN Name=LHCGR;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Holstein; TISSUE=Ovary, and Testis;
RA Lussier J.G., Houde A., Ethier J.-F., Silversides D.W.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Holstein; TISSUE=Corpus luteum;
RA Kawate N., Tamada H., Inaba T., Sawada T.;
RT "Expression of a cloned full-length cDNA encoding bovine luteinizing
RT hormone receptor in COS-7 cells.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-701 (ISOFORM LONG).
RX PubMed=9532424; DOI=10.1016/s0739-7240(97)00085-4;
RA Mamluk R., Wolfenson D., Meidan R.;
RT "LH receptor mRNA and cytochrome P450 side-chain cleavage expression in
RT bovine theca and granulosa cells luteinized by LH or forskolin.";
RL Domest. Anim. Endocrinol. 15:103-114(1998).
CC -!- FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The
CC activity of this receptor is mediated by G proteins which activate
CC adenylate cyclase. {ECO:0000250|UniProtKB:P22888}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22888};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P22888}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q28005-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q28005-2; Sequence=VSP_001961;
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P22888}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U20504; AAC24012.1; -; mRNA.
DR EMBL; AF491303; AAM09535.1; -; mRNA.
DR EMBL; U87230; AAC33486.1; -; mRNA.
DR RefSeq; NP_776806.1; NM_174381.1. [Q28005-1]
DR AlphaFoldDB; Q28005; -.
DR SMR; Q28005; -.
DR STRING; 9913.ENSBTAP00000022047; -.
DR GlyCosmos; Q28005; 6 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000022047; -.
DR GeneID; 281900; -.
DR KEGG; bta:281900; -.
DR CTD; 3973; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; Q28005; -.
DR OrthoDB; 1202285at2759; -.
DR TreeFam; TF316814; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004964; F:luteinizing hormone receptor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042700; P:luteinizing hormone signaling pathway; ISS:UniProtKB.
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 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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Leucine-rich repeat; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Repeat; Signal;
KW Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..701
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /id="PRO_0000012778"
FT TOPO_DOM 27..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..387
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..464
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..507
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..551
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..596
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..629
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 124..149
FT /note="LRR 1"
FT REPEAT 151..173
FT /note="LRR 2"
FT REPEAT 174..198
FT /note="LRR 3"
FT REPEAT 200..222
FT /note="LRR 4"
FT REPEAT 223..246
FT /note="LRR 5"
FT REPEAT 250..271
FT /note="LRR 6"
FT MOD_RES 333
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22888"
FT LIPID 645
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 646
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 441..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 229..291
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001961"
FT CONFLICT 235
FT /note="K -> Q (in Ref. 2; AAM09535)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="N -> D (in Ref. 3; AAC33486)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="I -> T (in Ref. 3; AAC33486)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="F -> S (in Ref. 3; AAC33486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 78456 MW; 8CDCE92F59EDBBD7 CRC64;
MGRPSLALRL LLALLLLPPP APLLWALRPA PCPEPCSCPP DGALRCPGPQ AGLSRLSLTY
LPIKVIPSQA FRGLNEVIKI EISQSDSLEK IEANAFDNLL NLSEILIQNT KNLVHIEAGA
FTNLPRLKYL SICNTGIHKL PDVTKIFSSE FNFILEICDN LHITTIPRNA FQGMNNESIT
LKLYGNGFEE IQSHAFNGTT LISLELKENA RLEKMHNDAF RGATGPSILD ISSTKLQALP
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
//
