LSHR_SHEEP
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 25-MAY-2022, entry version 102.
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 eggNOG; KOG2087; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
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; 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
