Molecular cloning of a novel protein‐tyrosine phosphatase containing a membrane‐binding domain and GLGF repeats-猫眼课题宝

含有膜结合域和 GLGF 重复序列的新型蛋白酪氨酸磷酸酶的分子克隆

DOI：

10.1016/0014-5793(94)80273-4

发表时间：

1994

期刊：

FEBS Letters

影响因子：

3.5

通讯作者：

中科院分区：

生物学3区

文献类型：

作者：

Kazuhiko Maekawa;Noriko Imagawa;Masaaki Nagamatsu;S. Harada

从人嗜碱性粒细胞中克隆了一种新的胞浆蛋白酪氨酸磷酸酶（PTP）的全长cDNA，命名为PTP-BAS。由于编码区的框内缺失，PTP-BAS以三种亚型存在：1型为7，455 bp（2，485 aa），2型为7，398 bp（2，466 aa），3型为6，882 bp（2，294 aa）。所有三种异构体在羧基末端含有单个PTP催化结构域以及两个不同的结构序列。300个氨基酸的氨基末端序列与细胞因子相关蛋白的膜结合结构域同源。三个90个氨基酸的内部重复序列与鸟苷酸激酶蛋白中发现的GLGF重复序列同源。PTP-BAS在人体多种组织中均有表达，尤其在肾和肺组织中表达最高。有趣的是，胎儿脑中的BAS mRNA水平非常高。

A full-length cDNA encoding a novel cytosolic protein-tyrosine phosphatase (PTP), PTP-BAS, was cloned from human basophils. Due to in-frame deletions in the coding region, PTP-BAS exists in three isoforms: 7,455 bp (2,485 aa) for type 1, 7,398 bp (2,466 aa) for type 2 and 6,882 bp (2,294 aa) for type 3. All three isoforms contain a single PTP catalytic domain at the carboxyl termini as well as two distinct structural sequences. Amino terminal sequences of 300 amino acids are homologous to membrane-binding domains of eytoskeleton-associated proteins. Three 90 amino acid internal repetitive sequences are homologous to the GLGF repeats found in guanylate kinase proteins. PTP-BAS was expressed in various human tissues, especially highly in the kidney and lung. Interestingly, the BAS mRNA level in the fetal brain was remarkably high.