PYY_RABIT
ID PYY_RABIT Reviewed; 36 AA.
AC Q9TR93; Q9TR92;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Peptide YY {ECO:0000303|PubMed:7984499};
DE Short=PYY {ECO:0000303|PubMed:7984499};
DE AltName: Full=PYY-I {ECO:0000303|PubMed:7984499};
DE AltName: Full=Peptide tyrosine tyrosine;
DE Contains:
DE RecName: Full=Peptide YY(3-36) {ECO:0000303|PubMed:7984499};
DE AltName: Full=PYY-II {ECO:0000303|PubMed:7984499};
GN Name=PYY;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND AMIDATION AT TYR-36.
RC TISSUE=Intestinal mucosa;
RX PubMed=7984499; DOI=10.1016/0196-9781(94)90035-3;
RA Grandt D., Schimiczek M., Struk K., Shively J., Eysselein V.E., Goebell H.,
RA Reeve J.R. Jr.;
RT "Characterization of two forms of peptide YY, PYY(1-36) and PYY(3-36), in
RT the rabbit.";
RL Peptides 15:815-820(1994).
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}.
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 AlphaFoldDB; Q9TR93; -.
DR BMRB; Q9TR93; -.
DR SMR; Q9TR93; -.
DR STRING; 9986.ENSOCUP00000011243; -.
DR eggNOG; ENOG502S267; Eukaryota.
DR InParanoid; Q9TR93; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; Direct protein sequencing; Hormone; Phosphoprotein;
KW Reference proteome; Secreted.
FT PEPTIDE 1..36
FT /note="Peptide YY"
FT /id="PRO_0000025389"
FT PEPTIDE 3..36
FT /note="Peptide YY(3-36)"
FT /id="PRO_0000025390"
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:0000250|UniProtKB:P68005"
FT MOD_RES 36
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:7984499"
SQ SEQUENCE 36 AA; 4285 MW; 02D499C8086DCC8D CRC64;
YPSKPEAPGE DASPEELNRY YASLRHYLNL VTRQRY