mp23, a Theileria parva transmembrane protein with homology to the protein disulfide isomerase family
mp23, a Theileria parva transmembrane protein with homology to the protein disulfide isomerase family
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DOI:
10.1016/s0166-6851(02)00036-1
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发表时间:
2002-05-01
影响因子:
1.5
通讯作者:
Lipp, J
中科院分区:
文献类型:
--
作者:
Ebel, T;Bender, K;Lipp, J
In order to identifyT. parvacomplementary DNAs (cDNA) encoding secretory and membrane proteins, which can be translocated across enodoplasmic reticulum (ER)-derived microsomal membranes (rough microsomes (RM)), 200 individual clones were screened. It was found that clone 17 transcribed the T7 RNA polymerase promoter crosses RM. Sequence analysis revealed that clone 17 comprises a cDNA of 755 bp including a 28 bp poly-A tail. Synthesis in the presence of RM led to an additional product of 23 kDa, termed mp23. Only one open reading frame of clone 17 had sufficient length to encode a polypeptide larger than 14 kDa. Starting with the first ATG codon the resulting in 220 amino acid polypeptide, termed p25, had a calculated molecular mass of 24 682 Da. It is deduced that mp23 is a transmembrane protein, with a single membrane-spanning segment and a short C-terminal cytosolic tail. Performing database searches, it was found that the N-terminal region of p25 shows significant similarity to redox-active thioredoxin homology domains of members of the protein disulfide isomerase (PDI) family. Based on the presence of a complete PDI-thioredoxin homology segment and its signal peptide-mediated translocation into the lumen of ER-derived membrane vesicles,T. parvamp23 is regarded as PDI-related protein. Nucleotide sequence data reported are available from the EMBL database under accession number AJ300678.