LSHR_PIG
ID LSHR_PIG Reviewed; 696 AA.
AC P16582;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D).
RX PubMed=2502844; DOI=10.1126/science.2502844;
RA Loosfelt H., Misrahi M., Atger M., Salesse R., Thi M.T.V.H.-L., Jolivet A.,
RA Guiochon-Mantel A., Sar S., Jallal B., Garnier J., Milgrom E.;
RT "Cloning and sequencing of porcine LH-hCG receptor cDNA: variants lacking
RT transmembrane domain.";
RL Science 245:525-528(1989).
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=4;
CC Name=A;
CC IsoId=P16582-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P16582-2; Sequence=VSP_001963, VSP_001964;
CC Name=C;
CC IsoId=P16582-3; Sequence=VSP_001965, VSP_001966;
CC Name=D;
CC IsoId=P16582-4; Sequence=VSP_001967;
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; M29525; AAA31062.1; -; mRNA.
DR EMBL; M29526; AAA31063.1; -; mRNA.
DR EMBL; M29527; AAA31064.1; -; mRNA.
DR EMBL; M29528; AAA31065.1; -; mRNA.
DR PIR; A41344; A41344.
DR PIR; B41344; B41344.
DR PIR; C41344; C41344.
DR PIR; D41344; D41344.
DR RefSeq; NP_999614.1; NM_214449.1. [P16582-1]
DR AlphaFoldDB; P16582; -.
DR SMR; P16582; -.
DR STRING; 9823.ENSSSCP00000008988; -.
DR PRIDE; P16582; -.
DR Ensembl; ENSSSCT00000009222; ENSSSCP00000008988; ENSSSCG00000008421. [P16582-1]
DR Ensembl; ENSSSCT00025064230; ENSSSCP00025027355; ENSSSCG00025047035. [P16582-1]
DR Ensembl; ENSSSCT00045051839; ENSSSCP00045036075; ENSSSCG00045030248. [P16582-1]
DR Ensembl; ENSSSCT00055038309; ENSSSCP00055030435; ENSSSCG00055019461. [P16582-1]
DR Ensembl; ENSSSCT00060033796; ENSSSCP00060014472; ENSSSCG00060024924. [P16582-1]
DR Ensembl; ENSSSCT00065044915; ENSSSCP00065019221; ENSSSCG00065033063. [P16582-1]
DR GeneID; 407247; -.
DR KEGG; ssc:407247; -.
DR CTD; 3973; -.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000157364; -.
DR InParanoid; P16582; -.
DR OMA; HCCAFIN; -.
DR Reactome; R-SSC-375281; Hormone ligand-binding receptors.
DR Reactome; R-SSC-418555; G alpha (s) signalling events.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000008421; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; P16582; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0007190; P:activation of adenylate cyclase 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; ISS:UniProtKB.
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; 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 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 Gene3D; 3.80.10.10; -; 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 Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF13306; LRR_5; 2.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01144; LSHRECEPTOR.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..696
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /id="PRO_0000012782"
FT TOPO_DOM 28..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..386
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..418
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..462
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..505
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..525
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..547
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..594
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 122..147
FT /note="LRR 1"
FT REPEAT 149..171
FT /note="LRR 2"
FT REPEAT 172..196
FT /note="LRR 3"
FT REPEAT 198..220
FT /note="LRR 4"
FT REPEAT 221..244
FT /note="LRR 5"
FT REPEAT 250..271
FT /note="LRR 6"
FT MOD_RES 331
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22888"
FT LIPID 643
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 644
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 439..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 317..628
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:2502844"
FT /id="VSP_001967"
FT VAR_SEQ 317..331
FT /note="YSAIFAESELSDWDY -> SKSRADGYQQRHKDC (in isoform C)"
FT /evidence="ECO:0000303|PubMed:2502844"
FT /id="VSP_001965"
FT VAR_SEQ 317..329
FT /note="YSAIFAESELSDW -> LLHGALPATHCLS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2502844"
FT /id="VSP_001963"
FT VAR_SEQ 330..696
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2502844"
FT /id="VSP_001964"
FT VAR_SEQ 332..696
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:2502844"
FT /id="VSP_001966"
SQ SEQUENCE 696 AA; 78092 MW; 593DEF1C25F982FE CRC64;
MRRRSLALRL LLALLLLPPP LPQTLLGAPC PEPCSCRPDG ALRCPGPRAG LSRLSLTYLP
IKVIPSQAFR GLNEVVKIEI SQSDSLEKIE ANAFDNLLNL SEILIQNTKN LVYIEPGAFT
NLPRLKYLSI CNTGIRKLPD VTKIFSSEFN FILEICDNLH ITTVPANAFQ GMNNESITLK
LYGNGFEEIQ SHAFNGTTLI SLELKENAHL KKMHNDAFRG ARGPSILDIS STKLQALPSY
GLESIQTLIA TSSYSLKKLP SREKFTNLLD ATLTYPSHCC AFRNLPTKEQ NFSFSIFKNF
SKQCESTARR PNNETLYSAI FAESELSDWD YDYGFCSPKT LQCAPEPDAF NPCEDIMGYD
FLRVLIWLIN ILAIMGNVTV LFVLLTSHYK LTVPRFLMCN LSFADFCMGL YLLLIASVDA
QTKGQYYNHA IDWQTGNGCS VAGFFTVFAS ELSVYTLTVI TLERWHTITY AIQLDQKLRL
RHAIPIMLGG WLFSTLIAML PLVGVSSYMK VSICLPMDVE TTLSQVYILT ILILNVVAFI
IICACYIKIY FAVQNPELMA TNKDTKIAKK MAVLIFTDFT CMAPISFFAI SAALKVPLIT
VTNSKVLLVL FYPVNSCANP FLYAIFTKAF RRDFFLLLSK SGCCKHQAEL YRRKDFSAYC
KNGFTGSNKP SRSTLKLTTL QCQYSTVMDK TCYKDC