Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase

Takafumi Uchida, Fumihiro Fujimori, Thomas Tradler, Gunter Fischer, Jens U. Rahfeld

Research output: Contribution to journalArticlepeer-review

77 Citations (Scopus)

Abstract

A second member of the parvulin family of peptidyl-prolyl cis/trans isomerases was identified in a human lung cDNA library. The gene encoded a protein named hPar14 that has 131 amino acid residues and a molecular mass of 13 676 Da. Sequence comparison showed 34.5% identity to E. coli Par10 and 34% identity to human Pin1 (hPar18) within a C-terminal region of 87 or 120 amino acid residues, respectively. In comparison to the E. coli Par10, hPar14 possesses a N-terminal extension of 41 amino acid residues. This extension does not contain a polyproline II helix-binding motif typical of the known eukaryotic parvulins. The hPar14 does not accelerate the cis to trans interconversion of oligopeptides with side chain-phosphorylated Ser(Thr)-Pro moieties as hPin1 did. In contrast, it showed preference of an arginine residue adjacent N-terminal to proline. Northern blot analysis revealed expression of the gene within various human tissues like heart, placenta, liver, kidney and pancreas. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)278-282
Number of pages5
JournalFEBS Letters
Volume446
Issue number2-3
DOIs
Publication statusPublished - 1999 Mar 12

Keywords

  • Gene
  • Human
  • Parvulin
  • Peptidyl-prolyl cis/trans isomerase
  • Pin1
  • Sequence

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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