LSHR_CALJA
ID LSHR_CALJA Reviewed; 676 AA.
AC O02721;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9165039; DOI=10.1210/endo.138.6.5196;
RA Zhang F.-P., Rannikko A.S., Manna P.R., Fraser H.M., Huhtaniemi I.T.;
RT "Cloning and functional expression of the luteinizing hormone receptor
RT complementary deoxyribonucleic acid from the marmoset monkey testis:
RT absence of sequences encoding exon 10 in other species.";
RL Endocrinology 138:2481-2490(1997).
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; U80673; AAB53698.1; -; mRNA.
DR RefSeq; NP_001288772.1; NM_001301843.1.
DR AlphaFoldDB; O02721; -.
DR SMR; O02721; -.
DR STRING; 9483.ENSCJAP00000019804; -.
DR Ensembl; ENSCJAT00000055166; ENSCJAP00000045777; ENSCJAG00000010733.
DR GeneID; 100385029; -.
DR KEGG; cjc:100385029; -.
DR CTD; 3973; -.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000157364; -.
DR HOGENOM; CLU_006130_1_1_1; -.
DR InParanoid; O02721; -.
DR OrthoDB; 257031at2759; -.
DR Proteomes; UP000008225; Chromosome 14.
DR Bgee; ENSCJAG00000010733; Expressed in ovary.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004964; F:luteinizing hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0042700; P:luteinizing hormone signaling pathway; ISS:UniProtKB.
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 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..676
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /id="PRO_0000012779"
FT TOPO_DOM 30..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..362
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..439
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..482
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..526
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..571
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..604
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 126..151
FT /note="LRR 1"
FT REPEAT 153..175
FT /note="LRR 2"
FT REPEAT 176..200
FT /note="LRR 3"
FT REPEAT 201..224
FT /note="LRR 4"
FT REPEAT 225..248
FT /note="LRR 5"
FT MOD_RES 308
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22888"
FT LIPID 620
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 621
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 DISULFID 416..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 676 AA; 75678 MW; FB018227641654E1 CRC64;
MKQPLLALQL LKLLLLLLLP LPPLPRALRE ARCCPEPCNC TPDGALRCPG PGAGLTRLSL
AYLPVKVIPS QAFRGLNEVI KIEISQSDSL ERIEANAFDN LLNLSEILIQ NTKNLIHIEP
GAFTNLPRLK YLSICNTGIR KFPDVTKIFS SETNFILEIC DNLHITTIPG NAFQGMNNES
ITLKLYGNGF EEVQSHAFNG TTVISLVLKE NVHLERIHNG AFRGATGPSI LDISSTKLQA
LPSHGLESIQ TLIATSSYSL KKLPSREKFA NLLDATLTYP SHCCAFRNVP TKDYPAIFAE
SGQSGWDYDY GFHLPKTPRC APEPDAFNPC EDIMGYDFLR VLIWLINILA IMGNMTVLFV
LLTSRYKLTV PRFLMCNLSF ADFCMGLYLL LIASVDSQTK GQYYNHAIDW QTGSGCNTAG
FFTVFASELS VYTLTVITLE RWHTITYAIH LDQKLRLRHA ILIMLGGWLF SSLIAMLPLV
GVSNYMKVSI CFPMDVETTL SQIYILTILI LNVVAFIIIC ACYIKIYFAV RNPELMATNK
DTKIAKKMAI LIFTDFTCMA PISFFAISAA FKMPLITVTN SKVLLVLFYP INSCANPFLY
AIFTKTFRRD FFLLLGKFGC CKHRAELYRR KDFSAYTSNY KNGFTGSSKP SQSTLKLPAL
HCQGTALLDK TCYKEY
