Paris A, Strukelj B, Pungercar J, Renko M, Dolenc I, Turk V
Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia.
FEBS Lett. 1995 Aug 7;369(2-3):326-30. doi: 10.1016/0014-5793(95)00777-7.
A cDNA clone (C1) coding for human preprocathepsin C was isolated from a human ileum cDNA library using a rat kidney-derived RT-PCR probe and its complete nucleotide sequence determined. The full-length 1857 bp sequence codes for a protein of 463 amino acid residues with a calculated molecular mass of 51848 Da. Comparison of the deduced amino acid sequence with that of rat preprocathepsin C indicates an 87.5% identity. A multiple alignment of the deduced cathepsin C sequence of 233 residues which, by analogy to other cystein proteinases, corresponds to the mature protein, confirms that human cathepsin C belongs to the papain superfamily.
使用大鼠肾脏来源的逆转录聚合酶链反应(RT-PCR)探针,从人回肠cDNA文库中分离出一个编码人组织蛋白酶C前体原的cDNA克隆(C1),并测定了其完整的核苷酸序列。全长1857 bp的序列编码一个由463个氨基酸残基组成的蛋白质,计算分子量为51848 Da。将推导的氨基酸序列与大鼠组织蛋白酶C前体原的序列进行比较,显示出87.5%的同一性。对233个残基的推导组织蛋白酶C序列进行多重比对,该序列与其他半胱氨酸蛋白酶类似,对应于成熟蛋白,证实人组织蛋白酶C属于木瓜蛋白酶超家族。