Human cathepsin X:: A novel cysteine protease of the papain family with a very short proregion and unique insertions
Human cathepsin X:: A novel cysteine protease of the papain family with a very short proregion and unique insertions
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DOI:
10.1016/s0014-5793(98)00964-8
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发表时间:
1998-08-28
期刊:
影响因子:
3.5
通讯作者:
Ménard, R
中科院分区:
文献类型:
--
作者:
Nägler, DK;Ménard, R
A novel cDNA encoding a cysteine protease of the papain family named cathepsin X was obtained by PCR amplification from a human ovary cDNA library. The cathepsin X cDNA is ubiquitously expressed in human tissues and contains an open reading frame of 912 nucleotides encoding a predicted protein of 303 amino acids. All highly conserved regions in papain-like cysteine proteases including the catalytic residues are present in cathepsin X. The mature part of cathepsin X is 26-32% identical to human cathepsins B, C, H, K, L, O, S and W, The cathepsin X sequence contains several unique features: (i) a very short proregion; (ii) a three amino acid residue insertion in a highly conserved region between the glutamine of the putative oxyanion hole and the active site cysteine; and (iii) a second insertion of 15 amino acid residues that can be aligned with the occluding loop region in cathepsin B. Published by Elsevier on behalf of the Federation of European Biochemical Societies.