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Database: UniProt
Entry: Q28585
LinkDB: Q28585
Original site: Q28585 
ID   LSHR_SHEEP              Reviewed;         538 AA.
AC   Q28585;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 105.
DE   RecName: Full=Lutropin-choriogonadotropic hormone receptor;
DE            Short=LH/CG-R;
DE   AltName: Full=Luteinizing hormone receptor;
DE            Short=LSH-R;
DE   Flags: Fragment;
GN   Name=LHCGR; Synonyms=LHR;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Dorset-Leicester-Suffolk; TISSUE=Testis;
RA   Yarney T.A.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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; L36329; AAA88538.1; -; mRNA.
DR   AlphaFoldDB; Q28585; -.
DR   SMR; Q28585; -.
DR   STRING; 9940.ENSOARP00000004768; -.
DR   GlyCosmos; Q28585; 6 sites, No reported glycans.
DR   PaxDb; 9940-ENSOARP00000004768; -.
DR   eggNOG; KOG2087; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
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; 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; Membrane; Receptor; Reference proteome; Repeat;
KW   Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..>538
FT                   /note="Lutropin-choriogonadotropic hormone receptor"
FT                   /id="PRO_0000069706"
FT   TOPO_DOM        <1..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..305
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..315
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..359
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..382
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..425
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        426..445
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..469
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        470..490
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..514
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..525
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        526..>538
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          <1..5
FT                   /note="LRR 1"
FT   REPEAT          6..30
FT                   /note="LRR 2"
FT   REPEAT          42..67
FT                   /note="LRR 3"
FT   REPEAT          92..116
FT                   /note="LRR 4"
FT   REPEAT          118..140
FT                   /note="LRR 5"
FT   REPEAT          141..164
FT                   /note="LRR 6"
FT   MOD_RES         251
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P22888"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        359..434
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         538
SQ   SEQUENCE   538 AA;  60232 MW;  04326641BC7B14C2 CRC64;
     SQSDSLEKIE ANALHNLLNL SEIPIQNTKN LVYIEPGAFT NLPRLKYLSI CNTGIRKLPD
     VTKIFSSEFN FILEICDNLH ITTVPGNAFQ GMNNESITLK LYGNGFEEIQ SHAFNGTTLI
     SLELKENAHL KKMHDDAFRG ARGPSILDIS STKLQALPSY GLESIQTLIA TSSYSLKKLP
     SREKFTNLLD ATLTYPSHCC AFRNLPTKEQ NFSFSIFKNF SKQCESTARR PNNETLYSAI
     FAESELSDWD YDYGFCSPKT LQCAPEPDAF NPCEDIMGYD FLRVLIWLIN ILAIMGNVTV
     LFVLLTSHYK LTVPRFLMCN LSFADFCMGL YLLLIASVDA QTKGQCYNHA IDWQTGNGCS
     VAGFFTVFAS ELSVYTLTVI TLERWHTITY AIQLDQKLRL RHAIPIMLGG WLFSTLIAML
     PLVGVSSYMK VSICLPMDVE TTLSQVYILT ILILNVVAFI IICACYIKIY FAVQNPELMA
     TNKDTKIAKK MAVLIFTDFT CMAPISFFAI SAALKVPLIT VTNSKVLLVL FYPVNSCA
//
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