NPY_RAT
ID NPY_RAT Reviewed; 98 AA.
AC P07808;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3031687; DOI=10.1073/pnas.84.8.2532;
RA Allen J., Novotny J., Martin J., Heinrich G.;
RT "Molecular structure of mammalian neuropeptide Y: analysis by molecular
RT cloning and computer-aided comparison with crystal structure of avian
RT homologue.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2532-2536(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3031663; DOI=10.1073/pnas.84.7.2068;
RA Larhammar D., Ericsson A., Persson H.;
RT "Structure and expression of the rat neuropeptide Y gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2068-2072(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2834371; DOI=10.1016/s0021-9258(18)68784-8;
RA Higuchi H., Yang H.-Y.T., Sabol S.L.;
RT "Rat neuropeptide Y precursor gene expression. mRNA structure, tissue
RT distribution, and regulation by glucocorticoids, cyclic AMP, and phorbol
RT ester.";
RL J. Biol. Chem. 263:6288-6295(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ACI/SegHsd, BB(DR)/Wor, Brown Norway/SsNHsd, DA/Bkl, F344/NHsd, and
RC LEW/NHsd;
RA Dracheva T.V., Joe B., Hashiramoto A., Dobbins D.E., Wilder R.L.,
RA Remmers E.F.;
RT "Polymorphic differences in the neuropeptide Y gene among six autoimmune
RT disease susceptible and resistant inbred rat strains.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 30-65, AND AMIDATION AT TYR-65.
RX PubMed=3413293; DOI=10.1016/0167-0115(88)90008-0;
RA Corder R., Gaillard R.C., Boehlen P.;
RT "Isolation and sequence of rat peptide YY and neuropeptide Y.";
RL Regul. Pept. 21:253-261(1988).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=29166604; DOI=10.1016/j.celrep.2017.10.084;
RA Bharat V., Siebrecht M., Burk K., Ahmed S., Reissner C.,
RA Kohansal-Nodehi M., Steubler V., Zweckstetter M., Ting J.T., Dean C.;
RT "Capture of Dense Core Vesicles at Synapses by JNK-Dependent
RT Phosphorylation of Synaptotagmin-4.";
RL Cell Rep. 21:2118-2133(2017).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
CC -!- FUNCTION: NPY is implicated in the control of feeding and in secretion
CC of gonadotrophin-release hormone.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle,
CC neuronal dense core vesicle {ECO:0000269|PubMed:29166604,
CC ECO:0000269|PubMed:30021165}.
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-31 by the prolyl
CC endopeptidase FAP (seprase) activity (in vitro).
CC {ECO:0000250|UniProtKB:P01303}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR EMBL; M15880; AAA41722.1; -; mRNA.
DR EMBL; M15793; AAA41723.1; -; Genomic_DNA.
DR EMBL; M15792; AAA41723.1; JOINED; Genomic_DNA.
DR EMBL; M20373; AAA41724.1; -; mRNA.
DR EMBL; AF392056; AAL28016.1; -; Genomic_DNA.
DR EMBL; AF392057; AAL28017.1; -; Genomic_DNA.
DR EMBL; AF392058; AAL28018.1; -; Genomic_DNA.
DR EMBL; AF392059; AAL28019.1; -; Genomic_DNA.
DR EMBL; AF392060; AAL28020.1; -; Genomic_DNA.
DR EMBL; AF392061; AAL28021.1; -; Genomic_DNA.
DR PIR; A27651; A25916.
DR RefSeq; NP_036746.1; NM_012614.2.
DR RefSeq; XP_003749793.1; XM_003749745.4.
DR AlphaFoldDB; P07808; -.
DR BMRB; P07808; -.
DR STRING; 10116.ENSRNOP00000013146; -.
DR BindingDB; P07808; -.
DR iPTMnet; P07808; -.
DR PhosphoSitePlus; P07808; -.
DR PaxDb; P07808; -.
DR PRIDE; P07808; -.
DR ABCD; P07808; 1 sequenced antibody.
DR GeneID; 24604; -.
DR KEGG; rno:24604; -.
DR UCSC; RGD:3197; rat.
DR CTD; 4852; -.
DR RGD; 3197; Npy.
DR VEuPathDB; HostDB:ENSRNOG00000046449; -.
DR eggNOG; ENOG502S2BU; Eukaryota.
DR HOGENOM; CLU_162379_1_0_1; -.
DR InParanoid; P07808; -.
DR OMA; QGTMRLW; -.
DR OrthoDB; 1542445at2759; -.
DR PhylomeDB; P07808; -.
DR TreeFam; TF332778; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P07808; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009768; Expressed in ileum and 15 other tissues.
DR ExpressionAtlas; P07808; baseline and differential.
DR Genevisible; P07808; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:HGNC-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0008343; P:adult feeding behavior; IDA:HGNC-UCL.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0021954; P:central nervous system neuron development; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
DR GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR GO; GO:0042117; P:monocyte activation; IDA:RGD.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IMP:RGD.
DR GO; GO:0032100; P:positive regulation of appetite; IDA:HGNC-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:RGD.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IDA:RGD.
DR GO; GO:1904000; P:positive regulation of eating behavior; IDA:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:1904407; P:positive regulation of nitric oxide metabolic process; IDA:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0032903; P:regulation of nerve growth factor production; IDA:RGD.
DR GO; GO:0050909; P:sensory perception of taste; IEP:RGD.
DR GO; GO:0048572; P:short-day photoperiodism; IEP:RGD.
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 Direct protein sequencing; Neuropeptide; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:3413293"
FT PEPTIDE 30..65
FT /note="Neuropeptide Y"
FT /evidence="ECO:0000269|PubMed:3413293"
FT /id="PRO_0000025329"
FT PEPTIDE 69..98
FT /note="C-flanking peptide of NPY"
FT /id="PRO_0000025330"
FT REGION 76..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 31..32
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P01303"
FT MOD_RES 65
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:2834371,
FT ECO:0000269|PubMed:3413293"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01303"
SQ SEQUENCE 98 AA; 11033 MW; E77EACEF3A3914B7 CRC64;
MMLGNKRMGL CGLTLALSLL VCLGILAEGY PSKPDNPGED APAEDMARYY SALRHYINLI
TRQRYGKRSS PETLISDLLM RESTENAPRT RLEDPSMW