GNRHR_OCTVU
ID GNRHR_OCTVU Reviewed; 407 AA.
AC Q2V2K5;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Gonadotropin-releasing hormone receptor {ECO:0000250|UniProtKB:P30969};
DE Short=GnRH receptor {ECO:0000250|UniProtKB:P30969, ECO:0000312|EMBL:BAE66648.1};
DE Short=GnRH-R {ECO:0000250|UniProtKB:P30969};
DE Short=oct-GnRHR {ECO:0000303|PubMed:16367741};
GN Name=GNRHR {ECO:0000250|UniProtKB:P30969};
OS Octopus vulgaris (Common octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=6645;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE66647.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:BAE66647.1};
RX PubMed=16367741; DOI=10.1042/bj20051615;
RA Kanda A., Takahashi T., Satake H., Minakata H.;
RT "Molecular and functional characterization of a novel gonadotropin-
RT releasing-hormone receptor isolated from the common octopus (Octopus
RT vulgaris).";
RL Biochem. J. 395:125-135(2006).
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. Ligand interaction triggers steroidogenesis in spermatozoa and
CC follicles. Appears to be involved in contraction of the radula
CC retractor muscle. {ECO:0000250|UniProtKB:P30969,
CC ECO:0000269|PubMed:16367741}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed in peripheral nervous tissue,
CC gonadal tissue and brain. In the brain, expression is high in the
CC palliovisceral lobe and superior buccal lobe but low in the subvertical
CC lobe, superior and inferior frontal lobe, posterior brachial lobe and
CC pedal lobe. Expressed in stomach, rectum, aorta, heart, salivary gland,
CC branchia, pancreas, radula retractor muscle, branchial vessel but not
CC in white body, esophagus, liver and kidney.
CC {ECO:0000269|PubMed:16367741}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB185200; BAE66647.1; -; mRNA.
DR EMBL; AB185201; BAE66648.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2V2K5; -.
DR SMR; Q2V2K5; -.
DR Proteomes; UP000515154; Genome assembly.
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 InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..407
FT /note="Gonadotropin-releasing hormone receptor"
FT /id="PRO_0000389522"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 377..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 407 AA; 46003 MW; C4EA6C342C0D75FA CRC64;
MDYLNDSMFN NMTYNITSTP LPDAPRFDNV YVSKLCVLGT VFVISFFGNT LVIIQIFRIR
GSRSTIQSLI LNLAIADLMV SFFNILMDII WSATVEWLAG NTMCKIMKYL TVFGLHLSTY
ITVSIALDRC FAILSPMSRS KAPLRVRIMI TMAWVLSAIF SIPQAVIFQE QRKMFRQGMF
HQCRDSYNAL WQKQLYSASS LILLFVIPLI IMVTSYLLIL KTIVKTSRQF HDTPISPTSM
SCYSVNHGQI RTHLFERARK RSSRMSAVIV AAFILCWTPY YIIFLGFAFF QWDNSRTVIY
FFTLGTSNCM LNPLIYGAFT IYKVHRGRSG SANSPSGTRL MIMVNKRGRS TTTTTNRMSG
SGRRQLTTGQ TITQCASLTN PHQPVRPSPG INSTTSPNGK MPTKPPG
