ID LSHR_MOUSE Reviewed; 700 AA.
AC P30730;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 24-JAN-2024, entry version 184.
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; Synonyms=Lhr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1311310; DOI=10.1016/s0021-9258(18)42858-x;
RA Gudermann T., Birnbaumer M., Birnbaumer L.;
RT "Evidence for dual coupling of the murine luteinizing hormone receptor to
RT adenylyl cyclase and phosphoinositide breakdown and Ca2+ mobilization.
RT Studies with the cloned murine luteinizing hormone receptor expressed in L
RT cells.";
RL J. Biol. Chem. 267:4479-4488(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX PubMed=1459341; DOI=10.1016/0303-7207(92)90009-u;
RA Huhtaniemi I.T., Eskola V., Pakarinen P., Matikainen T., Sprengel R.;
RT "The murine luteinizing hormone and follicle-stimulating hormone receptor
RT genes: transcription initiation sites, putative promoter sequences and
RT promoter activity.";
RL Mol. Cell. Endocrinol. 88:55-66(1992).
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 -!- 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}.
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DR EMBL; M81310; AAA39432.1; -; mRNA.
DR EMBL; M87571; AAA39433.1; -; Genomic_DNA.
DR EMBL; S49753; AAB24402.1; -; Genomic_DNA.
DR CCDS; CCDS29025.1; -.
DR PIR; A42395; A42395.
DR PIR; I77464; I77464.
DR RefSeq; NP_038610.1; NM_013582.2.
DR AlphaFoldDB; P30730; -.
DR SMR; P30730; -.
DR BioGRID; 201153; 2.
DR IntAct; P30730; 2.
DR MINT; P30730; -.
DR STRING; 10090.ENSMUSP00000024916; -.
DR BindingDB; P30730; -.
DR ChEMBL; CHEMBL4523213; -.
DR GlyCosmos; P30730; 6 sites, No reported glycans.
DR GlyGen; P30730; 6 sites.
DR PhosphoSitePlus; P30730; -.
DR SwissPalm; P30730; -.
DR MaxQB; P30730; -.
DR PaxDb; 10090-ENSMUSP00000024916; -.
DR ProteomicsDB; 293404; -.
DR DNASU; 16867; -.
DR Ensembl; ENSMUST00000024916.7; ENSMUSP00000024916.6; ENSMUSG00000024107.8.
DR GeneID; 16867; -.
DR KEGG; mmu:16867; -.
DR UCSC; uc008dvw.1; mouse.
DR AGR; MGI:96783; -.
DR CTD; 3973; -.
DR MGI; MGI:96783; Lhcgr.
DR VEuPathDB; HostDB:ENSMUSG00000024107; -.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000157364; -.
DR HOGENOM; CLU_006130_1_1_1; -.
DR InParanoid; P30730; -.
DR OMA; FFRSFTH; -.
DR OrthoDB; 1202285at2759; -.
DR PhylomeDB; P30730; -.
DR TreeFam; TF316814; -.
DR Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 16867; 4 hits in 79 CRISPR screens.
DR PRO; PR:P30730; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P30730; Protein.
DR Bgee; ENSMUSG00000024107; Expressed in gonadal ridge and 46 other cell types or tissues.
DR ExpressionAtlas; P30730; baseline and differential.
DR Genevisible; P30730; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0038106; F:choriogonadotropin hormone binding; IDA:BHF-UCL.
DR GO; GO:0035472; F:choriogonadotropin hormone receptor activity; IDA:BHF-UCL.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004964; F:luteinizing hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:BHF-UCL.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:MGI.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:BHF-UCL.
DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0046544; P:development of secondary male sexual characteristics; IMP:MGI.
DR GO; GO:0008585; P:female gonad development; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
DR GO; GO:0042700; P:luteinizing hormone signaling pathway; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0022602; P:ovulation cycle process; IMP:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISO:MGI.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; ISO:MGI.
DR GO; GO:0090030; P:regulation of steroid hormone biosynthetic process; IMP:MGI.
DR GO; GO:0034699; P:response to luteinizing hormone; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0060065; P:uterus development; IMP:MGI.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Repeat; Signal; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..700
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /id="PRO_0000012781"
FT TOPO_DOM 27..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..390
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..422
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..466
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..509
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..551
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..598
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..631
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 632..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 52..75
FT /note="LRR 1"
FT REPEAT 126..150
FT /note="LRR 2"
FT REPEAT 176..200
FT /note="LRR 3"
FT REPEAT 225..248
FT /note="LRR 4"
FT MOD_RES 335
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22888"
FT LIPID 647
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 648
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 443..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 700 AA; 78215 MW; 8A6840A011E1E014 CRC64;
MGRRVPALRQ LLVLAMLVLK QSQLHSPELS GSRCPEPCDC APDGALRCPG PRAGLARLSL
TYLPVKVIPS QAFRGLNEVV KIEISQSDSL ERIEANAFDN LLNLSEILIQ NTKNLLYIEP
GAFTNLPRLK YLSICNTGIR TLPDVSKISS SEFNFILEIC DNLYITTIPG NAFQGMNNES
ITLKLYGNGF EEVQSHAFNG TTLISLELKE NIYLEKMHSG TFQGATGPSI LDVSSTKLQA
LPSHGLESIQ TLIATSSYSL KTLPSREKFT SLLVATLTYP SHCCAFRNLP KKEQNFSFSI
FENFSKQCES TVREANNETL YSAIFEENEL SGWDYDYDFC SPKTLQCTPE PDAFNPCEDI
MGYAFLRVLI WLINILAIFG NLTVLFVLLT SRYKLTVPRF LMCNLSFADF CMGLYLLLIA
SVDSQTKGQY YNHAIDWQTG SGCSAAGFFT VFASELSVYT LTVITLERWH TITYAVQLDQ
KLRLRHAIPI MLGGWIFSTL MATLPLVGVS SYMKVSICLP MDVESTLSQV YILSILLLNA
VAFVVICACY VRIYFAVQNP ELTAPNKDTK IAKKMAILIF TDFTCMAPIS FFAISAAFKV
PLITVTNSKV LLVLFYPVNS CANPFLYAVF TKAFQRDFFL LLSRFGCCKH RAELYRRKEF
SACTFNSKNG FPRSSKPSQA ALKLSIVHCQ QPTPPRVLIQ
//
