GNRHR_PIG
ID GNRHR_PIG Reviewed; 328 AA.
AC P49922; Q9N142;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Gonadotropin-releasing hormone receptor;
DE Short=GnRH receptor;
DE Short=GnRH-R;
DE AltName: Full=Luteinizing hormone-releasing hormone receptor;
DE Short=LHRH;
GN Name=GNRHR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=7928774; DOI=10.2527/1994.7271911x;
RA Weesner G.D., Matteri R.L.;
RT "Rapid communication: nucleotide sequence of luteinizing hormone-releasing
RT hormone (LHRH) receptor cDNA in the pig pituitary.";
RL J. Anim. Sci. 72:1911-1911(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11269358; DOI=10.1139/gen-44-1-7;
RA Jiang Z., Gibson J.P., Archibald A.L., Haley C.S.;
RT "The porcine gonadotropin-releasing hormone receptor gene (GNRHR): genomic
RT organization, polymorphisms, and association with the number of corpora
RT lutea.";
RL Genome 44:7-12(2001).
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 -!- TISSUE SPECIFICITY: Pituitary gland.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L29342; AAA31067.1; -; mRNA.
DR EMBL; AF227686; AAF33402.1; -; Genomic_DNA.
DR EMBL; AF227685; AAF33402.1; JOINED; Genomic_DNA.
DR RefSeq; NP_999438.1; NM_214273.1.
DR AlphaFoldDB; P49922; -.
DR SMR; P49922; -.
DR STRING; 9823.ENSSSCP00000009521; -.
DR PaxDb; P49922; -.
DR PRIDE; P49922; -.
DR Ensembl; ENSSSCT00070017085; ENSSSCP00070014138; ENSSSCG00070008818.
DR GeneID; 397515; -.
DR KEGG; ssc:397515; -.
DR CTD; 2798; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_15_2_1; -.
DR InParanoid; P49922; -.
DR OrthoDB; 858238at2759; -.
DR TreeFam; TF106499; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 8.
DR Genevisible; P49922; SS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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_0000069490"
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 35..36
FT /note="GK -> PN (in Ref. 1; AAA31067)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="N -> D (in Ref. 1; AAA31067)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Y -> L (in Ref. 1; AAA31067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37747 MW; 60B04FD5E9634F25 CRC64;
MANSASPEQN QNHCSAINSS ILLTQGNLPT LTLSGKIRVT VTFFLFLLST AFNASFLLKL
QKWTQRKEKG KKLSRMKVLL KHLTLANLLE TLIVMPLDGM WNITVQWYAG EFLCKVLSYL
KLFSMYAPAF MMVVISLDRS LAITRPLAVK SNSRLGRFMI GLAWLLSSIF AGPQLYIFRM
IHLADSSGQT EGFSQCVTHG SFPQWWHQAF YNFFTFSCLF IIPLLIMLIC NAKIMFTLTR
VLQQDPHNLQ LNQSKNNIPR ARLRTLKMTV AFAASFIVCW TPYYVLGIWY WFDPEMVNRV
SDPVNHFFFL FAFLNPCFDP LIYGYFSL
