GNRHR_CANLF
ID GNRHR_CANLF Reviewed; 327 AA.
AC Q9MZI6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Gonadotropin-releasing hormone receptor;
DE Short=GnRH receptor;
DE Short=GnRH-R;
GN Name=GNRHR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10809231; DOI=10.1210/mend.14.5.0464;
RA Cui J., Smith R.G., Mount G.R., Lo J.L., Yu J., Walsh T.F., Singh S.B.,
RA DeVita R.J., Goulet M.T., Schaeffer J.M., Cheng K.;
RT "Identification of Phe313 of the gonadotropin-releasing hormone (GnRH)
RT receptor as a site critical for the binding of nonpeptide GnRH
RT antagonists.";
RL Mol. Endocrinol. 14:671-681(2000).
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}.
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; AF206513; AAF87097.1; -; mRNA.
DR RefSeq; NP_001003121.1; NM_001003121.1.
DR AlphaFoldDB; Q9MZI6; -.
DR SMR; Q9MZI6; -.
DR STRING; 9612.ENSCAFP00000004111; -.
DR PaxDb; Q9MZI6; -.
DR GeneID; 403718; -.
DR KEGG; cfa:403718; -.
DR CTD; 2798; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9MZI6; -.
DR OrthoDB; 858238at2759; -.
DR Proteomes; UP000002254; Unplaced.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0016500; F:protein-hormone receptor activity; IEA:InterPro.
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_0000069484"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..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 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 327 AA; 37656 MW; 778A82A9D25D3371 CRC64;
MASASPEQNQ NHCSAVNNSN MLMQGNLPTL TLSGKIRVTV TFFLFLLSTI FNASFLLKLQ
KWTQKKEKGK KLSRMKVLLK HLTLANLLET LIVMPLDGMW NITVQWYAGE FLCKVLSYLK
LFSMYAPAFM MVVISLDRSL AITRPLAMKN NGKLGQSMIG LAWLLSGIFA GPQLYIFRMI
HLADSSGQTE GFPQCVTHCS FPQWWHQAFY NFFTFSCLFI IPLFITLICN AKIIFTLTRV
LHQDPHELQL NQSKNNIPRA RLRTLKMTVA FATSFTVCWT PYYVLGIWYW FDPEMLNRVS
DPVNHFFFLF ALLNPCFDPL IYGYFSL
