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P83859 (OX26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orexigenic neuropeptide QRFP
Alternative name(s):
P518

Cleaved into the following chain:

  1. QRF-amide
    Alternative name(s):
    Neuropeptide RF-amide
    Pyroglutamylated arginine-phenylalanine-amide peptide
Gene names
Name:QRFP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Stimulates feeding behavior, metabolic rate and locomotor activity and increases blood pressure. May have orexigenic activity. May promote aldosterone secretion by the adrenal gland By similarity. Ref.2 Ref.3

Subunit structure

Ligand for the G-protein coupled receptor QRFPR/GPR103 By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed widely in the brain with highest expression levels in the cerebellum, medulla, pituitary, retina, vestibular nucleus, and white matter. Also expressed in the bladder, colon, coronary artery, parathyroid gland, prostate, testis, and thyroid. Ref.1

Sequence similarities

Belongs to the RFamide neuropeptide family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 9072
PRO_0000010086
Peptide91 – 13343QRF-amide
PRO_0000010087

Amino acid modifications

Modified residue911Pyrrolidone carboxylic acid Probable
Modified residue1331Phenylalanine amide By similarity UniProtKB P83683

Natural variations

Natural variant681L → H.
Corresponds to variant rs12340616 [ dbSNP | Ensembl ].
VAR_049184

Sequences

Sequence LengthMass (Da)Tools
P83859 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: 4FC036F7ADF4551F

FASTA13614,941
        10         20         30         40         50         60 
MVRPYPLIYF LFLPLGACFP LLDRREPTDA MGGLGAGERW ADLAMGPRPH SVWGSSRWLR 

        70         80         90        100        110        120 
ASQPQALLVI ARGLQTSGRE HAGCRFRFGR QDEGSEATGF LPAAGEKTSG PLGNLAEELN 

       130 
GYSRKKGGFS FRFGRR 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel RF-amide peptide ligand for orphan G-protein-coupled receptor SP9155."
Jiang Y., Luo L., Gustafson E.L., Yadav D., Laverty M., Murgolo N., Vassileva G., Zeng M., Laz T.M., Behan J., Qiu P., Wang L., Wang S., Bayne M., Greene J., Monsma F.J. Jr., Zhang F.L.
J. Biol. Chem. 278:27652-27657(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"A new peptidic ligand and its receptor regulating adrenal function in rats."
Fukusumi S., Yoshida H., Fujii R., Maruyama M., Komatsu H., Habata Y., Shintani Y., Hinuma S., Fujino M.
J. Biol. Chem. 278:46387-46395(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Brain.
[3]"Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity."
Chartrel N., Dujardin C., Anouar Y., Leprince J., Decker A., Clerens S., Do-Rego J.-C., Vandesande F., Llorens-Cortes C., Costentin J., Beauvillain J.-C., Vaudry H.
Proc. Natl. Acad. Sci. U.S.A. 100:15247-15252(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Tissue: Hypothalamus.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB109625 mRNA. Translation: BAC98934.1.
AY438326 Genomic DNA. Translation: AAR24354.1.
AL161733 Genomic DNA. Translation: CAM45757.1.
BC101127 mRNA. Translation: AAI01128.1.
RefSeqNP_937823.1. NM_198180.1.
UniGeneHs.660704.

3D structure databases

ProteinModelPortalP83859.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000345487.

Polymorphism databases

DMDM50400831.

Proteomic databases

PaxDbP83859.
PRIDEP83859.

Protocols and materials databases

DNASU347148.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343079; ENSP00000345487; ENSG00000188710.
GeneID347148.
KEGGhsa:347148.
UCSCuc011mcb.2. human.

Organism-specific databases

CTD347148.
GeneCardsGC09M133768.
HGNCHGNC:29982. QRFP.
HPAHPA043377.
MIM609795. gene.
neXtProtNX_P83859.
PharmGKBPA162400554.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47837.
HOGENOMHOG000231990.
HOVERGENHBG053386.
InParanoidP83859.
OMAFPLLDRR.
OrthoDBEOG7J182M.
PhylomeDBP83859.
TreeFamTF336317.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP83859.
CleanExHS_QRFP.
GenevestigatorP83859.

Family and domain databases

InterProIPR024565. P518.
[Graphical view]
PfamPF11109. RFamide_26RFa. 1 hit.
[Graphical view]
ProDomPD786889. PD786889. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

GeneWikiQRFP.
GenomeRNAi347148.
NextBio99051.
PROP83859.
SOURCESearch...

Entry information

Entry nameOX26_HUMAN
AccessionPrimary (citable) accession number: P83859
Secondary accession number(s): A3KFJ6, Q495K6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 10, 2004
Last modified: February 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM