GNRHR_SHEEP
ID GNRHR_SHEEP Reviewed; 328 AA.
AC P32237;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Gonadotropin-releasing hormone receptor;
DE Short=GnRH receptor;
DE Short=GnRH-R;
GN Name=GNRHR;
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 TISSUE=Pituitary;
RX PubMed=7694577; DOI=10.1006/bbrc.1993.2312;
RA Illing N., Jacobs G.F.M., Becker I.I., Flanagan C.A., Davidson J.S.,
RA Eales A., Zhou W., Sealfon S.C., Millar R.P.;
RT "Comparative sequence analysis and functional characterization of the
RT cloned sheep gonadotropin-releasing hormone receptor reveal differences in
RT primary structure and ligand specificity among mammalian receptors.";
RL Biochem. Biophys. Res. Commun. 196:745-751(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Scottish blackface; TISSUE=Pituitary;
RX PubMed=8224516; DOI=10.1016/0303-7207(93)90177-l;
RA Brooks J., Taylor P.L., Sauders P.T.K., Eidne K.A., Struthers W.J.,
RA McNeilly A.S.;
RT "Cloning and sequencing of the sheep pituitary gonadotropin-releasing
RT hormone receptor and changes in expression of its mRNA during the estrous
RT cycle.";
RL Mol. Cell. Endocrinol. 94:R23-R27(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8666259; DOI=10.1016/0378-1119(96)00042-x;
RA Campion C.E., Turzillo A.M., Clay C.M.;
RT "The gene encoding the ovine gonadotropin-releasing hormone (GnRH)
RT receptor: cloning and initial characterization.";
RL Gene 170:277-280(1996).
CC -!- FUNCTION: Receptor for gonadotropin releasing hormone (GnRH) that
CC mediates the action of GnRH to stimulate the secretion of the
CC gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating
CC hormone (FSH). This receptor mediates its action by association with G-
CC proteins that activate a phosphatidylinositol-calcium second messenger
CC system.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L22215; AAC37336.1; -; mRNA.
DR EMBL; X72088; CAA50978.1; -; mRNA.
DR EMBL; L42937; AAB38515.1; -; Genomic_DNA.
DR EMBL; AH004943; AAB41939.1; -; Genomic_DNA.
DR PIR; JN0882; JN0882.
DR RefSeq; NP_001009397.1; NM_001009397.1.
DR AlphaFoldDB; P32237; -.
DR SMR; P32237; -.
DR STRING; 9940.ENSOARP00000008075; -.
DR Ensembl; ENSOART00000008195; ENSOARP00000008075; ENSOARG00000007526.
DR Ensembl; ENSOART00020000471; ENSOARP00020000363; ENSOARG00020000382.
DR GeneID; 443413; -.
DR KEGG; oas:443413; -.
DR CTD; 2798; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_15_2_1; -.
DR OMA; SEPVNHF; -.
DR OrthoDB; 858238at2759; -.
DR Proteomes; UP000002356; Chromosome 6.
DR Bgee; ENSOARG00000007526; Expressed in pituitary gland and 14 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004968; F:gonadotropin-releasing hormone receptor activity; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001658; GphnRH_fam_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00529; GNADOTRPHINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..328
FT /note="Gonadotropin-releasing hormone receptor"
FT /id="PRO_0000069492"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 8
FT /note="D -> N (in Ref. 2; CAA50978)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="S -> R (in Ref. 2; CAA50978)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="T -> A (in Ref. 2; CAA50978)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> G (in Ref. 2; CAA50978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37685 MW; 0618374F33ECC6FE CRC64;
MANGDSPDQN ENHCSAINSS ILLTPGSLPT LTLSGKIRVT VTFFLFLLST IFNTSFLLKL
QNWTQRKEKR KKLSKMKVLL KHLTLANLLE TLIVMPLDGM WNITVQWYAG ELLCKVLSYL
KLFSMYAPAF MMVVISLDRS LAITRPLAVK SNSKLGQFMI GLAWLLSSIF AGPQLYIFGM
IHLADDSGQT EGFSQCVTHC SFPQWWHQAF YNFFTFSCLF IIPLLIMLIC NAKIIFTLTR
VLHQDPHKLQ LNQSKNNIPQ ARLRTLKMTV AFATSFTVCW TPYYVLGIWY WFDPDMVNRV
SDPVNHFFFL FAFLNPCFDP LIYGYFSL