FKBPs define a subfamily of peptidyl-prolyl cis/trans isomerases (PPlases). PPlases are known to play roles in cellular protein folding, protein interactions and signal transduction. Here we describe NcFKBP22 from Neurospora crassa, a novel type of FKBP. NcFKBP22 is synthesized as a precursor protein with a cleavable signal sequence. In addition to a typical FKBP domain in the amino-terminal part mature NcFKBP22 contains a novel second domain which is unique amongst all known FKBPs. The amino acid composition of this carboxyterminal domain is highly biased. Secondary structure predictions suggest that this domain may form an amphipathic alpha-helix. The carboxy-terminus of NcFKBP22 is -HNEL, a potential endoplasmic reticulum (ER) retention signal, suggesting that NcFKBP22 is a resident protein of the ER.

译文

:FKBP定义了肽基-脯氨酰顺/反异构酶(PPlases)的亚家族。已知PP酶在细胞蛋白质折叠,蛋白质相互作用和信号转导中发挥作用。在这里,我们描述了一种新的FKBP类型,来自Neurospora crassa的NcFKBP22。 NcFKBP22被合成为具有可裂解信号序列的前体蛋白。除了氨基末端部分的典型FKBP结构域外,成熟的NcFKBP22还包含一个新颖的第二结构域,该结构域在所有已知的FKBP中都是唯一的。该羧基末端结构域的氨基酸组成高度偏向。二级结构预测表明,该结构域可能形成两亲性α-螺旋。 NcFKBP22的羧基末端是-HNEL,这是潜在的内质网(ER)保留信号,表明NcFKBP22是ER的驻留蛋白。

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