PAHO_BOVIN
ID PAHO_BOVIN Reviewed; 131 AA.
AC P01302;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Pancreatic prohormone;
DE AltName: Full=Pancreatic polypeptide;
DE Short=PP;
DE Contains:
DE RecName: Full=Pancreatic hormone;
DE Contains:
DE RecName: Full=C-terminal peptide 1;
DE Contains:
DE RecName: Full=C-terminal peptide 2;
DE Flags: Precursor;
GN Name=PPY;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7831336; DOI=10.1073/pnas.92.2.594;
RA Herzog H., Hort Y., Schneider R., Shine J.;
RT "Seminalplasmin: recent evolution of another member of the neuropeptide Y
RT gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:594-598(1995).
RN [2]
RP PROTEIN SEQUENCE OF 30-65, AND AMIDATION AT TYR-65.
RA Chance R.E., Moon N.E., Johnson M.G.;
RL (In) Jaffe B.M., Behrman H.R. (eds.);
RL Methods of hormone radioimmunoassay (2nd ed.), pp.657-672, Academic Press,
RL New York and London (1979).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=1734969; DOI=10.1021/bi00119a038;
RA Li X., Sutcliffe M.J., Schwartz T.W., Dodson C.M.;
RT "Sequence-specific 1H NMR assignments and solution structure of bovine
RT pancreatic polypeptide.";
RL Biochemistry 31:1245-1253(1992).
CC -!- FUNCTION: Pancreatic hormone is synthesized in pancreatic islets of
CC Langerhans and acts as a regulator of pancreatic and gastrointestinal
CC functions.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR EMBL; L33970; AAA98526.1; -; Genomic_DNA.
DR PIR; A01570; PCBO.
DR PDB; 1BBA; NMR; -; A=30-65.
DR PDB; 1LJV; NMR; -; A=30-65.
DR PDB; 1V1D; NMR; -; A=30-60.
DR PDBsum; 1BBA; -.
DR PDBsum; 1LJV; -.
DR PDBsum; 1V1D; -.
DR AlphaFoldDB; P01302; -.
DR BMRB; P01302; -.
DR SMR; P01302; -.
DR InParanoid; P01302; -.
DR EvolutionaryTrace; P01302; -.
DR Proteomes; UP000009136; 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; IBA:GO_Central.
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 InterPro; IPR015480; Pancreatic_hormone.
DR InterPro; IPR001955; Pancreatic_hormone-like.
DR InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR PANTHER; PTHR10533; PTHR10533; 1.
DR PANTHER; PTHR10533:SF2; PTHR10533:SF2; 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 Direct protein sequencing; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|Ref.2"
FT PEPTIDE 30..65
FT /note="Pancreatic hormone"
FT /id="PRO_0000025355"
FT PEPTIDE 69..89
FT /note="C-terminal peptide 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025356"
FT PEPTIDE 93..131
FT /note="C-terminal peptide 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025357"
FT MOD_RES 65
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1LJV"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:1BBA"
SQ SEQUENCE 131 AA; 14376 MW; DCDFE1011C67DF9B CRC64;
MAAAHRCLFL LLLSTCVALL LQPPLGALGA PLEPEYPGDN ATPEQMAQYA AELRRYINML
TRPRYGKRDK EGTLDFLECG SPHSAVPRYG KRDKEGTLDF LECGSPHSAV PRWVFSLSCV
PRCLGQENGG V