| Title : Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface - Misumi_1992_Biochim.Biophys.Acta_1131_333 |
| Author(s) : Misumi Y , Hayashi Y , Arakawa F , Ikehara Y |
| Ref : Biochimica & Biophysica Acta , 1131 :333 , 1992 |
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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). |
| PubMedSearch : Misumi_1992_Biochim.Biophys.Acta_1131_333 |
| PubMedID: 1352704 |
| Gene_locus related to this paper: human-DPP4 |
| Gene_locus | human-DPP4 |
Misumi Y, Hayashi Y, Arakawa F, Ikehara Y (1992)
Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface
Biochimica & Biophysica Acta
1131 :333
Misumi Y, Hayashi Y, Arakawa F, Ikehara Y (1992)
Biochimica & Biophysica Acta
1131 :333