Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 2.
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.
Meng
Xianfang
X
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai, People's Republic of China.
Zhang
Chun
C
Chen
Jinzhong
J
Peng
Shuying
S
Cao
Yaoqiong
Y
Ying
Kang
K
Xie
Yi
Y
Mao
Yumin
Y
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D015152:Blotting, Northern; D002462:Cell Membrane / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D020626:Oncogene Proteins v-myb / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000235:genetics* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013879:Thioredoxins / Q000235:genetics* / Q000378:metabolism*
D018076:DNA, Complementary; D008565:Membrane Proteins; D020626:Oncogene Proteins v-myb; D011506:Proteins; C478605:TMX2 protein, human; D013879:Thioredoxins