GNRHR_RAT
ID GNRHR_RAT Reviewed; 327 AA.
AC P30969;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Gonadotropin-releasing hormone receptor;
DE Short=GnRH receptor;
DE Short=GnRH-R;
GN Name=Gnrhr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=1338727; DOI=10.1016/0303-7207(92)90116-n;
RA Eidne K.A., Sellar R.E., Couper G., Anderson L., Taylor P.L.;
RT "Molecular cloning and characterisation of the rat pituitary gonadotropin-
RT releasing hormone (GnRH) receptor.";
RL Mol. Cell. Endocrinol. 90:R5-R9(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Buffalo; TISSUE=Pituitary;
RA Kakar S.S., Grantham K., Musgrove L.C., Devor D.C., Sellers J.C.,
RA Neill J.D.;
RT "Molecular cloning and regulation of gene expression of rat gonadotropin
RT releasing hormone (GnRH) receptor.";
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=7916600; DOI=10.1006/bbrc.1993.1335;
RA Perrin M.H., Bilezikjian L.M., Hoeger C., Donaldson C.J., Rivier J.,
RA Haas Y., Vale W.W.;
RT "Molecular and functional characterization of GnRH receptors cloned from
RT rat pituitary and a mouse pituitary tumor cell line.";
RL Biochem. Biophys. Res. Commun. 191:1139-1144(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=1339279; DOI=10.1016/0006-291x(92)90266-n;
RA Kaiser U.B., Zhao D., Cardona G.R., Chin W.W.;
RT "Isolation and characterization of cDNAs encoding the rat pituitary
RT gonadotropin-releasing hormone receptor.";
RL Biochem. Biophys. Res. Commun. 189:1645-1652(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary, and Testis;
RX PubMed=8185587; DOI=10.1006/bbrc.1994.1601;
RA Moumni M., Kottler M.L., Counis R.;
RT "Nucleotide sequence analysis of mRNAs predicts that rat pituitary and
RT gonadal gonadotropin-releasing hormone receptor proteins have identical
RT primary structure.";
RL Biochem. Biophys. Res. Commun. 200:1359-1366(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7764374;
RA Kudo A., Park M.K., Kawashima S.;
RT "Isolation of rat GnRH receptor cDNA having different 5'-noncoding
RT sequence.";
RL Zool. Sci. 10:863-867(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Reinhart J., Xiao S., Arora K.K., Catt K.J.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION.
RX PubMed=22356123; DOI=10.1111/j.1365-2826.2012.02302.x;
RA Matagne V., Kim J.G., Ryu B.J., Hur M.K., Kim M.S., Kim K., Park B.S.,
RA Damante G., Smiley G., Lee B.J., Ojeda S.R.;
RT "Thyroid transcription factor 1, a homeodomain containing transcription
RT factor, contributes to regulating periodic oscillations in GnRH gene
RT expression.";
RL J. Neuroendocrinol. 24:916-929(2012).
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 -!- INDUCTION: Expression oscillates in a diurnal and melatonin-dependent
CC fashion in the preoptic area (POA) region in the hypothalamus, with
CC maximal expression attained during the dark phase of the light/dark
CC cycle. {ECO:0000269|PubMed:22356123}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41265.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S59525; AAB26420.1; -; mRNA.
DR EMBL; X68980; CAA48776.1; -; mRNA.
DR EMBL; U00935; AAC27349.1; -; mRNA.
DR EMBL; L25053; AAA41265.1; ALT_INIT; mRNA.
DR EMBL; L07646; AAA41274.1; -; mRNA.
DR EMBL; X76635; CAA54083.1; -; mRNA.
DR EMBL; S68578; AAC60671.1; -; mRNA.
DR EMBL; U92471; AAB58038.1; -; Genomic_DNA.
DR EMBL; U92469; AAB58038.1; JOINED; Genomic_DNA.
DR EMBL; U92470; AAB58038.1; JOINED; Genomic_DNA.
DR PIR; I60169; I60169.
DR RefSeq; NP_112300.2; NM_031038.3.
DR AlphaFoldDB; P30969; -.
DR SMR; P30969; -.
DR BioGRID; 249567; 3.
DR STRING; 10116.ENSRNOP00000002755; -.
DR BindingDB; P30969; -.
DR ChEMBL; CHEMBL3066; -.
DR DrugCentral; P30969; -.
DR GuidetoPHARMACOLOGY; 256; -.
DR GlyGen; P30969; 3 sites.
DR iPTMnet; P30969; -.
DR PhosphoSitePlus; P30969; -.
DR PaxDb; P30969; -.
DR GeneID; 81668; -.
DR KEGG; rno:81668; -.
DR UCSC; RGD:70513; rat.
DR CTD; 2798; -.
DR RGD; 70513; Gnrhr.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P30969; -.
DR OrthoDB; 858238at2759; -.
DR PhylomeDB; P30969; -.
DR Reactome; R-RNO-375281; Hormone ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P30969; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004968; F:gonadotropin-releasing hormone receptor activity; IBA:GO_Central.
DR GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; IDA:RGD.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
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..327
FT /note="Gonadotropin-releasing hormone receptor"
FT /id="PRO_0000069491"
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..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
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..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 184
FT /note="A -> V (in Ref. 1; CAA48776/AAB26420)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="G -> A (in Ref. 3; AAA41265, 5; CAA54083, 6;
FT AAC60671 and 7; AAB58038)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="A -> G (in Ref. 1; CAA48776/AAB26420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37748 MW; 86A2CA1A2C9F1BE4 CRC64;
MANNASLEQD QNHCSAINNS IPLTQGKLPT LTLSGKIRVT VTFFLFLLST AFNASFLVKL
QRWTQKRKKG KKLSRMKVLL KHLTLANLLE TLIVMPLDGM WNITVQWYAG EFLCKVLSYL
KLFSMYAPAF MMVVISLDRS LAVTQPLAVQ SKSKLERSMT SLAWILSIVF AGPQLYIFRM
IYLADGSGPA VFSQCVTHCS FPQWWHEAFY NFFTFSCLFI IPLLIMLICN AKIIFALTRV
LHQDPRKLQL NQSKNNIPRA RLRTLKMTVA FGTSFVICWT PYYVLGIWYW FDPEMLNRVS
EPVNHFFFLF AFLNPCFDPL IYGYFSL
