Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity

Tsuyoshi Yoshinaka, Kazuhiro Nishii, Kouji Yamada, Hirohide Sawada, Eiji Nishiwaki, Katherine Smith, Kohichiro Yoshino, Hiroshi Ishiguro, Shigeki Higashiyama

Research output: Contribution to journalArticlepeer-review

112 Citations (Scopus)


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 exons. 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)3C(x)5C(x)5CxC(x)8C) 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.

Original languageEnglish
Pages (from-to)227-236
Number of pages10
Issue number1-2
Publication statusPublished - 09-01-2002

All Science Journal Classification (ASJC) codes

  • Genetics


Dive into the research topics of 'Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity'. Together they form a unique fingerprint.

Cite this