NPY_MOUSE
ID NPY_MOUSE Reviewed; 97 AA.
AC P57774; Q925V2; Q9ET27;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pro-neuropeptide Y;
DE Contains:
DE RecName: Full=Neuropeptide Y;
DE AltName: Full=Neuropeptide tyrosine;
DE Short=NPY;
DE Contains:
DE RecName: Full=C-flanking peptide of NPY;
DE Short=CPON;
DE Flags: Precursor;
GN Name=Npy;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Hennessey K., Chua S. Jr.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-89.
RC STRAIN=NZO, and SM/J; TISSUE=Brain;
RX PubMed=11210195; DOI=10.1007/s003350010254;
RA Taylor B.A., Wnek C., Schroeder D., Phillips S.J.;
RT "Multiple obesity QTLs identified in an intercross between the NZO (New
RT Zealand obese) and the SM (small) mouse strains.";
RL Mamm. Genome 12:95-103(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: NPY is implicated in the control of feeding and in secretion
CC of gonadotrophin-release hormone. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle,
CC neuronal dense core vesicle {ECO:0000250|UniProtKB:P07808}.
CC -!- TISSUE SPECIFICITY: One of the most abundant peptides in the nervous
CC system. Also found in some chromaffin cells of the adrenal medulla.
CC -!- PTM: The neuropeptide Y form is cleaved at Pro-30 by the prolyl
CC endopeptidase FAP (seprase) activity (in vitro).
CC {ECO:0000250|UniProtKB:P01303}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF273768; AAG00945.1; -; mRNA.
DR EMBL; AK002982; BAB22495.1; -; mRNA.
DR EMBL; BC043012; AAH43012.1; -; mRNA.
DR EMBL; AF286198; AAG01330.1; -; mRNA.
DR EMBL; AF286199; AAG01331.1; -; mRNA.
DR CCDS; CCDS39488.1; -.
DR RefSeq; NP_075945.1; NM_023456.3.
DR AlphaFoldDB; P57774; -.
DR BMRB; P57774; -.
DR BioGRID; 224929; 2.
DR STRING; 10090.ENSMUSP00000031843; -.
DR iPTMnet; P57774; -.
DR PhosphoSitePlus; P57774; -.
DR CPTAC; non-CPTAC-3487; -.
DR PaxDb; P57774; -.
DR PeptideAtlas; P57774; -.
DR PRIDE; P57774; -.
DR ProteomicsDB; 253007; -.
DR ABCD; P57774; 1 sequenced antibody.
DR Antibodypedia; 12195; 602 antibodies from 40 providers.
DR DNASU; 109648; -.
DR Ensembl; ENSMUST00000031843; ENSMUSP00000031843; ENSMUSG00000029819.
DR GeneID; 109648; -.
DR KEGG; mmu:109648; -.
DR UCSC; uc009bwt.1; mouse.
DR CTD; 4852; -.
DR MGI; MGI:97374; Npy.
DR VEuPathDB; HostDB:ENSMUSG00000029819; -.
DR eggNOG; ENOG502S2BU; Eukaryota.
DR GeneTree; ENSGT00940000156475; -.
DR HOGENOM; CLU_162379_1_0_1; -.
DR InParanoid; P57774; -.
DR OMA; QGTMRLW; -.
DR OrthoDB; 1542445at2759; -.
DR PhylomeDB; P57774; -.
DR TreeFam; TF332778; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 109648; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Npy; mouse.
DR PRO; PR:P57774; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P57774; protein.
DR Bgee; ENSMUSG00000029819; Expressed in median eminence of neurohypophysis and 179 other tissues.
DR Genevisible; P57774; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR GO; GO:0031841; F:neuropeptide Y receptor binding; ISO:MGI.
DR GO; GO:0008343; P:adult feeding behavior; ISS:HGNC-UCL.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0019732; P:antifungal humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0042117; P:monocyte activation; ISO:MGI.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISO:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISO:MGI.
DR GO; GO:1904000; P:positive regulation of eating behavior; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1904407; P:positive regulation of nitric oxide metabolic process; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IDA:MGI.
DR GO; GO:0032903; P:regulation of nerve growth factor production; ISO:MGI.
DR GO; GO:0001878; P:response to yeast; ISO:MGI.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0048572; P:short-day photoperiodism; IEA:Ensembl.
DR CDD; cd00126; PAH; 1.
DR InterPro; IPR001955; Pancreatic_hormone-like.
DR InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR PANTHER; PTHR10533; PTHR10533; 1.
DR Pfam; PF00159; Hormone_3; 1.
DR PRINTS; PR00278; PANCHORMONE.
DR SMART; SM00309; PAH; 1.
DR PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
DR PROSITE; PS50276; PANCREATIC_HORMONE_2; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Neuropeptide; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT PEPTIDE 29..64
FT /note="Neuropeptide Y"
FT /id="PRO_0000025325"
FT PEPTIDE 68..97
FT /note="C-flanking peptide of NPY"
FT /id="PRO_0000025326"
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 30..31
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P01303"
FT MOD_RES 64
FT /note="Tyrosine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01303"
FT CONFLICT 42
FT /note="A -> R (in Ref. 4; AAG01330/AAG01331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 10874 MW; 7E0CE28FA330844E CRC64;
MLGNKRMGLC GLTLALSLLV CLGILAEGYP SKPDNPGEDA PAEDMARYYS ALRHYINLIT
RQRYGKRSSP ETLISDLLMK ESTENAPRTR LEDPSMW
