Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity
Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity
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DOI：
10.1016/s0378-1119(01)00818-6
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发表时间：
2002-01-09
期刊：
影响因子：
3.5
通讯作者：
Higashiyama, S
中科院分区：
文献类型：
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作者：
Yoshinaka, T;Nishii, K;Higashiyama, S
膜锚定蛋白的ADAM家族具有独特的结构域结构，每个结构域含有去整合素和金属蛋白酶（ADAM）结构域。我们已经分离出编码ADAM家族新成员的小鼠和人cDNA。小鼠和人预测的蛋白质分别由797和813个氨基酸组成，并且它们共享整个氨基酸序列的70%同源性。小鼠ADAM基因存在于单个基因位点。人类基因在肝脏以外的组织中普遍表达，定位于人类染色体20p13，并发现由22个外显子组成。这两种蛋白质的结构域组织与以前报道的ADAM家族成员相同，在其金属蛋白酶结构域中含有典型的锌结合共有序列（HEXGHXXGXXHD），在其EGF样结构域中含有典型的EGF样基序的半胱氨酸定位模式（C（x）（3）C（x）（5）C（x）（5）CxC（x）（8）C）。人蛋白质显示与非洲爪蟾ADAM 13（44%）、人ADAM 19（40%）和人ADAM 12（39%）的同源性。根据基于一级氨基酸序列和mRNA分布的遗传分析结果，这些新的ADAM基因因此被命名为ADAM 33。(C)2002 Elsevier Science B.V.保留所有权利。
The ADAM family of membrane-anchored proteins has a unique domain structure, with each containing a disintegrin and metalloprotease, (ADAM) domain. We have isolated mouse and human cDNAs encoding a novel member of the ADAM family. The mouse and human predicted proteins consisted of 797 and 813 amino acids, respectively, and they shared 70% homology of the entire amino acid sequence. The mouse ADAM gene exists at a single gene locus. The human gene was ubiquitously expressed in tissues other than liver, was mapped to human chromosome 20p13, and was found to consist of 22 exerts. Both proteins have domain organization identical to that of previously reported members of the ADAM family, and contain the typical zinc-binding consensus sequence (HEXGHXXGXXHD) in their metalloprotease domain and a pattern of cysteine localization (C(x)(3)C(x)(5)C(x)(5)CxC(x)(8)C) in their EGF-like domain that is typical of an EGF-like motif. The human protein shows homology with Xenopus ADAM13 (44%), human ADAM19 (40%), and human ADAM12 (39%). From the results of phylogenic analysis based on primary amino acid sequence and distribution of the mRNA, these novel ADAM genes were thus named ADAM33. (C) 2002 Elsevier Science B.V. All rights reserved.