GPR54_ORENI
ID GPR54_ORENI Reviewed; 377 AA.
AC Q6BD04;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=G-protein coupled receptor 54;
GN Name=gpr54;
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
RC TISSUE=Embryonic brain;
RX PubMed=15155576; DOI=10.1210/en.2004-0395;
RA Parhar I.S., Ogawa S., Sakuma Y.;
RT "Laser-captured single digoxigenin-labeled neurons of gonadotropin-
RT releasing hormone types reveal a novel G protein-coupled receptor (Gpr54)
RT during maturation in cichlid fish.";
RL Endocrinology 145:3613-3618(2004).
CC -!- FUNCTION: Receptor speculated to be essential for sexual development.
CC May regulate gonadotropin-releasing hormone (GnRH) secretion. The
CC receptor expression could be a 'stop signal' for GnRH1, GnRH2, and
CC GnRH3 neuronal migration, leading to suppression of cell growth and
CC modulation of GnRH secretion, which is important for normal sexual
CC development.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in a significantly high percentage (45-
CC 60%) of mature GnRH1, GnRH2, and GnRH3 neurons and in immature GnRH3
CC neurons, which had migrated to the vicinity of their final locations in
CC the brain. Only 5% of immature GnRH1 and GnRH2 neurons have receptor
CC transcripts. {ECO:0000269|PubMed:15155576}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB162143; BAD34454.1; -; mRNA.
DR RefSeq; NP_001266708.1; NM_001279779.1.
DR AlphaFoldDB; Q6BD04; -.
DR SMR; Q6BD04; -.
DR STRING; 8128.ENSONIP00000011710; -.
DR GeneID; 100534519; -.
DR KEGG; onl:100534519; -.
DR CTD; 561898; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q6BD04; -.
DR OrthoDB; 1294084at2759; -.
DR Proteomes; UP000005207; 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 InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008103; KiSS_1_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01728; KISS1RECEPTR.
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..377
FT /note="G-protein coupled receptor 54"
FT /id="PRO_0000069698"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..328
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 377 AA; 43204 MW; CFCD448F3872F1BF CRC64;
MYSSEELWNS TEQVWINGSG TNFSLGRHED DEEEEGDKHP FFTDAWLVPL FFSLIMLVGL
VGNSLVIYVI SKHRQMRTAT NFYIANLAAT DIIFLVCCVP FTATLYPLPG WIFGNFMCKF
VAFLQQVTVQ ATCITLTAMS GDRCYVTVYP LKSLRHRTPK VAMIVSICIW IGSFVLSTPI
LMYQRIEEGY WYGPRQYCME RFPSKTHERA FILYQFIAAY LLPVLTISFC YTLMVKRVGQ
PTVEPVDNNY QVNLLSERTI SIRSKVSKMV VVIVLLFAIC WGPIQIFVLF QSFYPNYQPN
YATYKIKTWA NCMSYANSSV NPIVYGFMGA SFQKSFRKTF PFLFKHKVRD SSMASRTANA
EIKFVAAEEG NNNNAVN
