QRFPR_BRAFL
ID QRFPR_BRAFL Reviewed; 380 AA.
AC C3ZQF9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=QRFP-like peptide receptor {ECO:0000303|PubMed:25449662};
GN Name=QRFPR {ECO:0000303|PubMed:25449662};
GN ORFNames=BRAFLDRAFT_74637 {ECO:0000312|EMBL:EEN45215.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000312|Proteomes:UP000001554};
RN [1] {ECO:0000312|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000312|Proteomes:UP000001554};
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25449662; DOI=10.1016/j.ygcen.2014.10.010;
RA Xu B., Bergqvist C.A., Sundstroem G., Lundell I., Vaudry H., Leprince J.,
RA Larhammar D.;
RT "Characterization of peptide QRFP (26RFa) and its receptor from amphioxus,
RT Branchiostoma floridae.";
RL Gen. Comp. Endocrinol. 210:107-113(2015).
CC -!- FUNCTION: Receptor for QRFP-like peptide. The activity of this receptor
CC is mediated by G proteins which activate a phosphatidyl-inositol-
CC calcium second messenger system. {ECO:0000269|PubMed:25449662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25449662};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688}.
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DR EMBL; GG666661; EEN45215.1; -; Genomic_DNA.
DR RefSeq; XP_002589204.1; XM_002589158.1.
DR AlphaFoldDB; C3ZQF9; -.
DR SMR; C3ZQF9; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; C3ZQF9; -.
DR OrthoDB; 1485786at2759; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:1901653; P:cellular response to peptide; IDA:UniProtKB.
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; IPR000611; NPY_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..380
FT /note="QRFP-like peptide receptor"
FT /id="PRO_0000442014"
FT TOPO_DOM 1..51
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..122
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..305
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 120..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 380 AA; 43187 MW; 1B9EADF040E9BE72 CRC64;
MMLGNMTFTQ TILHELLRQH NMTKNEFIER FGLPPLVYVP ELSPGAKTVT LVFYVIIFLA
ALLGNTLVVV VVWKNKVMRT TMNIFICSLA ASDLLITIVC IPVTLMQNML QNWIMGDFMC
KLVPFIQTIA VASSILTLTG IAIERYYAII HPLKVKYLLS KTRAGIILAL VWVVSVGVAT
PMLFVHKAEE IHDFLYEQRF VTCQEKWWGQ TQQTSYTIFN LVVLFIIPLL TMTSLYIRIA
HRLWVQQPVG VTGNFAHGNS VRRKRQAVKM LVVVVLLFAV CWLPYHTVTV MNELTGLRLE
EKSAKLLIAI VQLIAFSNSF NNPVVYAILN ENFKKNFMTM LRCRVNRVSP QQVTPNTLQT
PLEQSTRSCR LPAGAPNQQI
