NPY_PIG
ID NPY_PIG Reviewed; 76 AA.
AC P01304; Q9N0M5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 25-MAY-2022, entry version 130.
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; Fragment;
GN Name=NPY;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RA Matteri R.L.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 10-45, AND AMIDATION AT TYR-45.
RX PubMed=6957876; DOI=10.1073/pnas.79.18.5485;
RA Tatemoto K.;
RT "Neuropeptide Y: complete amino acid sequence of the brain peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5485-5489(1982).
RN [3]
RP STRUCTURE BY NMR OF 10-45.
RX PubMed=2372534; DOI=10.1021/bi00471a002;
RA Saudek V., Pelton J.T.;
RT "Sequence-specific 1H NMR assignment and secondary structure of
RT neuropeptide Y in aqueous solution.";
RL Biochemistry 29:4509-4515(1990).
RN [4]
RP STRUCTURE BY NMR OF 10-45.
RX PubMed=1576993; DOI=10.1111/j.1432-1033.1992.tb16878.x;
RA Cowley D.J., Hoflack J.M., Pelton J.T., Saudek V.;
RT "Structure of neuropeptide Y dimer in solution.";
RL Eur. J. Biochem. 205:1099-1106(1992).
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: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-11 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; AF264083; AAF72538.1; -; mRNA.
DR PIR; A01573; NYPGY.
DR PDB; 1F8P; NMR; -; A=10-45.
DR PDB; 1FVN; NMR; -; A=10-45.
DR PDB; 1ICY; NMR; -; A=10-45.
DR PDB; 1TZ4; NMR; -; A=10-27, A=33-45.
DR PDB; 1TZ5; NMR; -; A=28-32.
DR PDBsum; 1F8P; -.
DR PDBsum; 1FVN; -.
DR PDBsum; 1ICY; -.
DR PDBsum; 1TZ4; -.
DR PDBsum; 1TZ5; -.
DR AlphaFoldDB; P01304; -.
DR BMRB; P01304; -.
DR SMR; P01304; -.
DR STRING; 9823.ENSSSCP00000017708; -.
DR PaxDb; P01304; -.
DR PeptideAtlas; P01304; -.
DR eggNOG; ENOG502S2BU; Eukaryota.
DR HOGENOM; CLU_162379_1_0_1; -.
DR InParanoid; P01304; -.
DR EvolutionaryTrace; P01304; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P01304; SS.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008343; P:adult feeding behavior; ISS:HGNC-UCL.
DR GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR GO; GO:0090275; P:negative regulation of somatostatin secretion; IMP:AgBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC-UCL.
DR GO; GO:0090274; P:positive regulation of somatostatin secretion; IMP:AgBase.
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 3D-structure; Amidation; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Direct protein sequencing; Neuropeptide;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL <1..9
FT /evidence="ECO:0000269|PubMed:6957876"
FT PEPTIDE 10..45
FT /note="Neuropeptide Y"
FT /evidence="ECO:0000269|PubMed:6957876"
FT /id="PRO_0000025327"
FT PEPTIDE 49..>76
FT /note="C-flanking peptide of NPY"
FT /id="PRO_0000025328"
FT SITE 11..12
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P01303"
FT MOD_RES 45
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:6957876"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01303"
FT NON_TER 1
FT NON_TER 76
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:1F8P"
FT HELIX 26..44
FT /evidence="ECO:0007829|PDB:1F8P"
SQ SEQUENCE 76 AA; 8596 MW; 84E40EC2A4F94B2C CRC64;
VCLCALAEAY PSKPDNPGED APAEDLARYY SALRHYINLI TRQRYGKRSS PETLISDLLM
REGTENVPRT RLEDPS
