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首页> 外文期刊>FEBS Letters >Identification and characterization of a 14 kDa human protein as a novel parvulin‐like peptidyl prolyl cis/trans isomerase
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Identification and characterization of a 14 kDa human protein as a novel parvulin‐like peptidyl prolyl cis/trans isomerase

机译：鉴定和表征一种14 kDa的人类蛋白质，它是一种新型的细小蛋白样肽基脯氨酰顺/反异构酶

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>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.
机译：>在人肺cDNA文库中鉴定了肽基脯氨酰顺 / 反转录异构酶的小肠蛋白家族的第二个成员。该基因编码一种名为hPar14的蛋白质，该蛋白质具有131个氨基酸残基，分子量为13 676 Da。序列比较显示与 E的34.5％同一性。大肠杆菌Par10和在人类87位或120个氨基酸残基的C端区域与人Pin1（ h Par18）具有34％的同一性。与 E相比。大肠杆菌 Par10， h Par14具有41个氨基酸残基的N端延伸。该延伸不包含已知的真核小病毒蛋白典型的多脯氨酸II螺旋结合基序。 h Par14不会加速侧链磷酸化Ser（Thr）-Pro部分为的寡肽的 cis 到反式相互转化h Pin1做到了。相比之下，它显示出邻近脯氨酸N端的精氨酸残基。 Northern印迹分析显示该基因在心脏，胎盘，肝脏，肾脏和胰腺等各种人体组织中的表达。

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