OX26_MOUSE
ID OX26_MOUSE Reviewed; 124 AA.
AC Q8CE23; A2AV24;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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:BAC98937.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAC26323.1};
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:0000312|EMBL:BAC98937.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000269|PubMed:12960173};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16648250; DOI=10.1073/pnas.0602371103;
RA Takayasu S., Sakurai T., Iwasaki S., Teranishi H., Yamanaka A.,
RA Williams S.C., Iguchi H., Kawasawa Y.I., Ikeda Y., Sakakibara I., Ohno K.,
RA Ioka R.X., Murakami S., Dohmae N., Xie J., Suda T., Motoike T., Ohuchi T.,
RA Yanagisawa M., Sakai J.;
RT "A neuropeptide ligand of the G protein-coupled receptor GPR103 regulates
RT feeding, behavioral arousal, and blood pressure in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7438-7443(2006).
CC -!- FUNCTION: Stimulates feeding and grooming behavior, metabolic rate and
CC locomotor activity and increases blood pressure. May have orexigenic
CC activity. May promote aldosterone secretion by the adrenal gland.
CC {ECO:0000269|PubMed:16648250}.
CC -!- SUBUNIT: Ligand for the G-protein coupled receptor QRFPR/GPR103.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the brain with highest levels in the
CC periventricular hypothalamic nucleus and lateral hypothalamic areas.
CC Expressed at moderate levels in the adrenal gland, eye, heart,
CC intestine, liver, lung, kidney, mesenteric lymph node, ovary, placenta,
CC Peyer patches, skin, spleen, stomach, testis, thymus and uterus.
CC {ECO:0000269|PubMed:12714592, ECO:0000269|PubMed:16648250}.
CC -!- SIMILARITY: Belongs to the RFamide neuropeptide family. {ECO:0000305}.
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DR EMBL; AB109628; BAC98937.1; -; mRNA.
DR EMBL; AK029144; BAC26323.1; -; mRNA.
DR EMBL; AL929275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15902.1; -.
DR RefSeq; NP_906269.1; NM_183424.4.
DR AlphaFoldDB; Q8CE23; -.
DR STRING; 10090.ENSMUSP00000055746; -.
DR PaxDb; Q8CE23; -.
DR PRIDE; Q8CE23; -.
DR Antibodypedia; 48446; 27 antibodies from 7 providers.
DR DNASU; 227717; -.
DR Ensembl; ENSMUST00000057407; ENSMUSP00000055746; ENSMUSG00000043102.
DR GeneID; 227717; -.
DR KEGG; mmu:227717; -.
DR UCSC; uc008jed.1; mouse.
DR CTD; 347148; -.
DR MGI; MGI:3630329; Qrfp.
DR VEuPathDB; HostDB:ENSMUSG00000043102; -.
DR eggNOG; ENOG502S84J; Eukaryota.
DR GeneTree; ENSGT00390000015756; -.
DR HOGENOM; CLU_155319_0_0_1; -.
DR InParanoid; Q8CE23; -.
DR OMA; PLGTCFP; -.
DR OrthoDB; 1571514at2759; -.
DR PhylomeDB; Q8CE23; -.
DR TreeFam; TF336317; -.
DR Reactome; R-MMU-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 227717; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8CE23; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CE23; protein.
DR Bgee; ENSMUSG00000043102; Expressed in forelimb bud and 12 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0031854; F:orexigenic neuropeptide QRFP receptor binding; IDA:UniProtKB.
DR GO; GO:0007625; P:grooming behavior; IDA:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:UniProtKB.
DR GO; GO:0060259; P:regulation of feeding behavior; IDA: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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..79
FT /evidence="ECO:0000250"
FT /id="PRO_0000010088"
FT PEPTIDE 80..122
FT /note="QRF-amide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000010089"
FT REGION 63..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 124 AA; 13485 MW; 2BA6A90F3575EF20 CRC64;
MRGFRPLLSL LLPLSACFPL LDRRGPTDIG DIGARMNWAQ LAEGHPPNSV QNPQPQALLV
VAREQQASHR EHTGFRLGRQ DGSSEAAGFL PADSEKASGP LGTLAEELSS YSRRKGGFSF
RFGR
