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Identification and characterization of a 14 kDa human protein as a novel parvulin‐like peptidyl prolyl cis / trans isomerase
Author(s) -
Uchida Takafumi,
Fujimori Fumihiro,
Tradler Thomas,
Fischer Gunter,
Rahfeld Jens-U
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00239-2
Subject(s) - biochemistry , amino acid , isomerase , peptide sequence , complementary dna , arginine , cdna library , polyproline helix , chemistry , microbiology and biotechnology , gene , biology , stereochemistry , peptide
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 ( h Par18) within a C‐terminal region of 87 or 120 amino acid residues, respectively. In comparison to the E. coli Par10, h Par14 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 h Par14 does not accelerate the cis to trans interconversion of oligopeptides with side chain‐phosphorylated Ser(Thr)‐Pro moieties as h Pin1 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.