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Pro-neuropeptide Y [Cleaved into: Neuropeptide Y (Neuropeptide tyrosine) (NPY); C-flanking peptide of NPY (CPON)] (Fragment)

 NPY_PIG                 Reviewed;          76 AA.
P01304; Q9N0M5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
07-JUN-2017, entry version 117.
RecName: Full=Pro-neuropeptide Y;
Contains:
RecName: Full=Neuropeptide Y;
AltName: Full=Neuropeptide tyrosine;
Short=NPY;
Contains:
RecName: Full=C-flanking peptide of NPY;
Short=CPON;
Flags: Precursor; Fragment;
Name=NPY;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hypothalamus;
Matteri R.L.;
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 10-45, AND AMIDATION AT TYR-45.
PubMed=6957876; DOI=10.1073/pnas.79.18.5485;
Tatemoto K.;
"Neuropeptide Y: complete amino acid sequence of the brain peptide.";
Proc. Natl. Acad. Sci. U.S.A. 79:5485-5489(1982).
[3]
STRUCTURE BY NMR OF 10-45.
PubMed=2372534; DOI=10.1021/bi00471a002;
Saudek V., Pelton J.T.;
"Sequence-specific 1H NMR assignment and secondary structure of
neuropeptide Y in aqueous solution.";
Biochemistry 29:4509-4515(1990).
[4]
STRUCTURE BY NMR OF 10-45.
PubMed=1576993; DOI=10.1111/j.1432-1033.1992.tb16878.x;
Cowley D.J., Hoflack J.M., Pelton J.T., Saudek V.;
"Structure of neuropeptide Y dimer in solution.";
Eur. J. Biochem. 205:1099-1106(1992).
-!- FUNCTION: NPY is implicated in the control of feeding and in
secretion of gonadotrophin-release hormone.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: One of the most abundant peptides in the
nervous system. Also found in some chromaffin cells of the adrenal
medulla.
-!- PTM: The neuropeptide Y form is cleaved at Pro-11 by the prolyl
endopeptidase FAP (seprase) activity (in vitro).
{ECO:0000250|UniProtKB:P01303}.
-!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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EMBL; AF264083; AAF72538.1; -; mRNA.
PIR; A01573; NYPGY.
UniGene; Ssc.15981; -.
PDB; 1F8P; NMR; -; A=10-45.
PDB; 1FVN; NMR; -; A=10-45.
PDB; 1ICY; NMR; -; A=10-45.
PDB; 1TZ4; NMR; -; A=10-27, A=33-45.
PDB; 1TZ5; NMR; -; A=28-32.
PDBsum; 1F8P; -.
PDBsum; 1FVN; -.
PDBsum; 1ICY; -.
PDBsum; 1TZ4; -.
PDBsum; 1TZ5; -.
ProteinModelPortal; P01304; -.
SMR; P01304; -.
STRING; 9823.ENSSSCP00000017708; -.
PaxDb; P01304; -.
PeptideAtlas; P01304; -.
PRIDE; P01304; -.
eggNOG; ENOG410J0KC; Eukaryota.
eggNOG; ENOG41128I2; LUCA.
InParanoid; P01304; -.
OrthoDB; EOG091G0ZRE; -.
EvolutionaryTrace; P01304; -.
Proteomes; UP000008227; Unplaced.
Genevisible; P01304; SS.
GO; GO:0005615; C:extracellular space; ISS:HGNC.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
GO; GO:0008343; P:adult feeding behavior; ISS:HGNC.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
GO; GO:0090275; P:negative regulation of somatostatin secretion; IMP:AgBase.
GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC.
GO; GO:0090274; P:positive regulation of somatostatin secretion; IMP:AgBase.
GO; GO:0032098; P:regulation of appetite; IBA:GO_Central.
CDD; cd00126; PAH; 1.
InterPro; IPR001955; Pancreatic_hormone-like.
InterPro; IPR020392; Pancreatic_hormone-like_CS.
PANTHER; PTHR10533; PTHR10533; 1.
Pfam; PF00159; Hormone_3; 1.
PRINTS; PR00278; PANCHORMONE.
ProDom; PD001267; Pancreatic_hormone-like; 1.
SMART; SM00309; PAH; 1.
PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
PROSITE; PS50276; PANCREATIC_HORMONE_2; 1.
1: Evidence at protein level;
3D-structure; Amidation; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Neuropeptide;
Phosphoprotein; Reference proteome; Secreted; Signal.
SIGNAL <1 9 {ECO:0000269|PubMed:6957876}.
PEPTIDE 10 45 Neuropeptide Y.
{ECO:0000269|PubMed:6957876}.
/FTId=PRO_0000025327.
PEPTIDE 49 >76 C-flanking peptide of NPY.
/FTId=PRO_0000025328.
SITE 11 12 Cleavage; by FAP.
{ECO:0000250|UniProtKB:P01303}.
MOD_RES 45 45 Tyrosine amide.
{ECO:0000269|PubMed:6957876}.
MOD_RES 64 64 Phosphothreonine.
{ECO:0000250|UniProtKB:P01303}.
NON_TER 1 1
NON_TER 76 76
TURN 22 25 {ECO:0000244|PDB:1F8P}.
HELIX 26 44 {ECO:0000244|PDB:1F8P}.
SEQUENCE 76 AA; 8596 MW; 84E40EC2A4F94B2C CRC64;
VCLCALAEAY PSKPDNPGED APAEDLARYY SALRHYINLI TRQRYGKRSS PETLISDLLM
REGTENVPRT RLEDPS


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