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一种含有膜结合结构域和GLGF重复序列的新型蛋白酪氨酸磷酸酶的分子克隆

Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats.

作者信息

Maekawa K, Imagawa N, Nagamatsu M, Harada S

机构信息

Shionogi Institute for Medical Science, Osaka, Japan.

出版信息

FEBS Lett. 1994 Jan 10;337(2):200-6. doi: 10.1016/0014-5793(94)80273-4.

DOI:10.1016/0014-5793(94)80273-4
PMID:8287977
Abstract

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 cytoskeleton-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.

摘要

从人嗜碱性粒细胞中克隆出一个编码新型胞质蛋白酪氨酸磷酸酶(PTP)即PTP - BAS的全长cDNA。由于编码区存在读框内缺失,PTP - BAS以三种同工型存在:1型为7455 bp(2485个氨基酸),2型为7398 bp(2466个氨基酸),3型为6882 bp(2294个氨基酸)。所有这三种同工型在羧基末端均含有一个单一的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骨架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在多种人体组织中表达,在肾脏和肺中表达尤其高。有趣的是,胎儿大脑中的BAS mRNA水平非常高。

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