Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface

Biochim Biophys Acta. 1992 Jul 15;1131(3):333-6. doi: 10.1016/0167-4781(92)90036-y.

Abstract

The cDNA coding for the human dipeptidyl peptidase IV (DPPIV) has been isolated and sequenced. The nucleotide sequence (3465 bp) of the cDNA contains an open reading frame encoding a polypeptide comprising 766 amino acids, one residue less than those of rat DPPIV. The predicted amino acid sequence exhibits 84.9% identity to that of the rat enzyme, and contains nine potential N-linked glycosylation sites, one site more than those in the rat enzyme. A putative catalytic triad for serine proteinases, serine, aspartic acid and histidine, are found in a completely conserved COOH-terminal region (positions 625-752).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Dipeptidyl Peptidase 4
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / chemistry
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / genetics*
  • Humans
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics*
  • Molecular Sequence Data

Substances

  • Membrane Glycoproteins
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • Dipeptidyl Peptidase 4

Associated data

  • GENBANK/M80530
  • GENBANK/M80531
  • GENBANK/M80532
  • GENBANK/M80533
  • GENBANK/M91429
  • GENBANK/M91430
  • GENBANK/X60708
  • GENBANK/X64342
  • GENBANK/X64343
  • GENBANK/X64766