PYY_PIG
ID PYY_PIG Reviewed; 36 AA.
AC P68005; P01305;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Peptide YY {ECO:0000303|PubMed:6953409};
DE Short=PYY {ECO:0000303|PubMed:6953409};
DE AltName: Full=Peptide tyrosine tyrosine;
DE Contains:
DE RecName: Full=Peptide YY(3-36) {ECO:0000250|UniProtKB:Q9TR93};
DE AltName: Full=PYY-II {ECO:0000250|UniProtKB:Q9TR93};
GN Name=PYY;
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 PROTEIN SEQUENCE, AND AMIDATION AT TYR-36.
RC TISSUE=Intestine;
RX PubMed=6953409; DOI=10.1073/pnas.79.8.2514;
RA Tatemoto K.;
RT "Isolation and characterization of peptide YY (PYY), a candidate gut
RT hormone that inhibits pancreatic exocrine secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2514-2518(1982).
RN [2]
RP PHOSPHORYLATION AT SER-13, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11248248; DOI=10.1016/s0014-5793(01)02234-7;
RA Chen Z.-W., Eriste E., Jonsson A.P., Norberg A., Nepomuceno D.,
RA Lovenberg T.W., Bergman T., Efendic S., Joernvall H., Sillard R.;
RT "Ser(13)-phosphorylated PYY from porcine intestine with a potent biological
RT activity.";
RL FEBS Lett. 492:119-122(2001).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=10933813; DOI=10.1021/bi992576a;
RA Keire D.A., Kobayashi M., Solomon T.E., Reeve J.R. Jr.;
RT "Solution structure of monomeric peptide YY supports the functional
RT significance of the PP-fold.";
RL Biochemistry 39:9935-9942(2000).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=15178255; DOI=10.1016/j.jmb.2004.04.032;
RA Lerch M., Mayrhofer M., Zerbe O.;
RT "Structural similarities of micelle-bound peptide YY (PYY) and neuropeptide
RT Y (NPY) are related to their affinity profiles at the Y receptors.";
RL J. Mol. Biol. 339:1153-1168(2004).
CC -!- FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has
CC a vasoconstrictory action and inhibitis jejunal and colonic mobility.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The peptide YY form is cleaved at Pro-2 by the prolyl
CC endopeptidase FAP (seprase) activity (in vitro) to generate peptide
CC YY(3-36). {ECO:0000250|UniProtKB:P10082}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR PIR; A01574; YYPG.
DR PDB; 1QBF; NMR; -; A=1-36.
DR PDB; 1RU5; NMR; -; A=1-36.
DR PDB; 1RUU; NMR; -; A=1-36.
DR PDB; 2OON; NMR; -; A=1-36.
DR PDB; 2OOP; NMR; -; A=1-36.
DR PDB; 2RLK; NMR; -; A=1-36.
DR PDBsum; 1QBF; -.
DR PDBsum; 1RU5; -.
DR PDBsum; 1RUU; -.
DR PDBsum; 2OON; -.
DR PDBsum; 2OOP; -.
DR PDBsum; 2RLK; -.
DR AlphaFoldDB; P68005; -.
DR BMRB; P68005; -.
DR SMR; P68005; -.
DR STRING; 9823.ENSSSCP00000023751; -.
DR iPTMnet; P68005; -.
DR PaxDb; P68005; -.
DR PeptideAtlas; P68005; -.
DR eggNOG; ENOG502S267; Eukaryota.
DR HOGENOM; CLU_162379_1_0_1; -.
DR InParanoid; P68005; -.
DR EvolutionaryTrace; P68005; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IMP:AgBase.
DR GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR CDD; cd00126; PAH; 1.
DR DisProt; DP01838; -.
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; Direct protein sequencing; Hormone;
KW Phosphoprotein; Reference proteome; Secreted.
FT PEPTIDE 1..36
FT /note="Peptide YY"
FT /id="PRO_0000044810"
FT PEPTIDE 3..36
FT /note="Peptide YY(3-36)"
FT /evidence="ECO:0000250|UniProtKB:P10082"
FT /id="PRO_0000430665"
FT SITE 2..3
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P10082"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11248248"
FT MOD_RES 36
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:6953409"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1RUU"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1QBF"
FT TURN 16..22
FT /evidence="ECO:0007829|PDB:1QBF"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1QBF"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:1QBF"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1QBF"
SQ SEQUENCE 36 AA; 4242 MW; 02CD6B8C586DCC8D CRC64;
YPAKPEAPGE DASPEELSRY YASLRHYLNL VTRQRY
