OX26_HUMAN
ID OX26_HUMAN Reviewed; 136 AA.
AC P83859; A3KFJ6; Q495K6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Orexigenic neuropeptide QRFP;
DE AltName: Full=P518;
DE Contains:
DE RecName: Full=QRF-amide;
DE AltName: Full=Neuropeptide RF-amide;
DE AltName: Full=Pyroglutamylated arginine-phenylalanine-amide peptide;
DE Flags: Precursor;
GN Name=QRFP {ECO:0000312|EMBL:BAC98934.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAR24354.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12714592; DOI=10.1074/jbc.m302945200;
RA Jiang Y., Luo L., Gustafson E.L., Yadav D., Laverty M., Murgolo N.,
RA Vassileva G., Zeng M., Laz T.M., Behan J., Qiu P., Wang L., Wang S.,
RA Bayne M., Greene J., Monsma F.J. Jr., Zhang F.L.;
RT "Identification and characterization of a novel RF-amide peptide ligand for
RT orphan G-protein-coupled receptor SP9155.";
RL J. Biol. Chem. 278:27652-27657(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain {ECO:0000269|PubMed:12714592};
RX PubMed=12960173; DOI=10.1074/jbc.m305270200;
RA Fukusumi S., Yoshida H., Fujii R., Maruyama M., Komatsu H., Habata Y.,
RA Shintani Y., Hinuma S., Fujino M.;
RT "A new peptidic ligand and its receptor regulating adrenal function in
RT rats.";
RL J. Biol. Chem. 278:46387-46395(2003).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Hypothalamus {ECO:0000312|EMBL:AAR24354.1};
RX PubMed=14657341; DOI=10.1073/pnas.2434676100;
RA Chartrel N., Dujardin C., Anouar Y., Leprince J., Decker A., Clerens S.,
RA Do-Rego J.-C., Vandesande F., Llorens-Cortes C., Costentin J.,
RA Beauvillain J.-C., Vaudry H.;
RT "Identification of 26RFa, a hypothalamic neuropeptide of the RFamide
RT peptide family with orexigenic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15247-15252(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Stimulates feeding behavior, metabolic rate and locomotor
CC activity and increases blood pressure. May have orexigenic activity.
CC May promote aldosterone secretion by the adrenal gland (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12960173,
CC ECO:0000269|PubMed:14657341}.
CC -!- SUBUNIT: Ligand for the G-protein coupled receptor QRFPR/GPR103.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed widely in the brain with highest
CC expression levels in the cerebellum, medulla, pituitary, retina,
CC vestibular nucleus, and white matter. Also expressed in the bladder,
CC colon, coronary artery, parathyroid gland, prostate, testis, and
CC thyroid. {ECO:0000269|PubMed:12714592}.
CC -!- SIMILARITY: Belongs to the RFamide neuropeptide family. {ECO:0000305}.
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DR EMBL; AB109625; BAC98934.1; -; mRNA.
DR EMBL; AY438326; AAR24354.1; -; Genomic_DNA.
DR EMBL; AL161733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101127; AAI01128.1; -; mRNA.
DR CCDS; CCDS6936.1; -.
DR RefSeq; NP_937823.1; NM_198180.2.
DR AlphaFoldDB; P83859; -.
DR STRING; 9606.ENSP00000485512; -.
DR BioMuta; QRFP; -.
DR DMDM; 50400831; -.
DR PaxDb; P83859; -.
DR PeptideAtlas; P83859; -.
DR PRIDE; P83859; -.
DR Antibodypedia; 48446; 27 antibodies from 7 providers.
DR DNASU; 347148; -.
DR Ensembl; ENST00000343079.1; ENSP00000345487.1; ENSG00000188710.3.
DR Ensembl; ENST00000623824.2; ENSP00000485512.1; ENSG00000188710.3.
DR GeneID; 347148; -.
DR KEGG; hsa:347148; -.
DR MANE-Select; ENST00000623824.2; ENSP00000485512.1; NM_198180.3; NP_937823.1.
DR UCSC; uc011mcb.2; human.
DR CTD; 347148; -.
DR DisGeNET; 347148; -.
DR GeneCards; QRFP; -.
DR HGNC; HGNC:29982; QRFP.
DR HPA; ENSG00000188710; Low tissue specificity.
DR MIM; 609795; gene.
DR neXtProt; NX_P83859; -.
DR OpenTargets; ENSG00000188710; -.
DR PharmGKB; PA162400554; -.
DR VEuPathDB; HostDB:ENSG00000188710; -.
DR eggNOG; ENOG502S84J; Eukaryota.
DR GeneTree; ENSGT00390000015756; -.
DR HOGENOM; CLU_155319_0_0_1; -.
DR InParanoid; P83859; -.
DR OMA; PLGTCFP; -.
DR OrthoDB; 1571514at2759; -.
DR PhylomeDB; P83859; -.
DR TreeFam; TF336317; -.
DR PathwayCommons; P83859; -.
DR Reactome; R-HSA-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 347148; 20 hits in 1058 CRISPR screens.
DR GeneWiki; QRFP; -.
DR GenomeRNAi; 347148; -.
DR Pharos; P83859; Tbio.
DR PRO; PR:P83859; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P83859; protein.
DR Bgee; ENSG00000188710; Expressed in lower esophagus mucosa and 86 other tissues.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:UniProtKB.
DR GO; GO:0031854; F:orexigenic neuropeptide QRFP receptor binding; ISS:UniProtKB.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
DR InterPro; IPR024565; P518.
DR PANTHER; PTHR36476; PTHR36476; 1.
DR Pfam; PF11109; RFamide_26RFa; 1.
PE 2: Evidence at transcript level;
KW Amidation; Neuropeptide; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..90
FT /evidence="ECO:0000255, ECO:0000305"
FT /id="PRO_0000010086"
FT PEPTIDE 91..133
FT /note="QRF-amide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000010087"
FT MOD_RES 91
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P83860, ECO:0000305"
FT MOD_RES 133
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT VARIANT 68
FT /note="L -> H (in dbSNP:rs12340616)"
FT /id="VAR_049184"
SQ SEQUENCE 136 AA; 14941 MW; 4FC036F7ADF4551F CRC64;
MVRPYPLIYF LFLPLGACFP LLDRREPTDA MGGLGAGERW ADLAMGPRPH SVWGSSRWLR
ASQPQALLVI ARGLQTSGRE HAGCRFRFGR QDEGSEATGF LPAAGEKTSG PLGNLAEELN
GYSRKKGGFS FRFGRR
