Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 2.

Xianfang Meng, Chun Zhang, Jinzhong Chen, Shuying Peng, Yaoqiong Cao, Kang Ying, Yi Xie, Yumin Mao

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai, People's Republic of China.

Biochemical genetics 2003 Apr

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Thioredoxin plays an important role in various cellular processes through redox regulation. Here we report the molecular cloning and characterization of one member of the thioredoxin superfamily, designated as TMX2. The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail. Northern blot analysis shows it is widely expressed in human tissues.

Citation

Xianfang Meng, Chun Zhang, Jinzhong Chen, Shuying Peng, Yaoqiong Cao, Kang Ying, Yi Xie, Yumin Mao. Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 2. Biochemical genetics. 2003 Apr;41(3-4):99-106