TY - JOUR
T1 - Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity
AU - Yoshinaka, Tsuyoshi
AU - Nishii, Kazuhiro
AU - Yamada, Kouji
AU - Sawada, Hirohide
AU - Nishiwaki, Eiji
AU - Smith, Katherine
AU - Yoshino, Kohichiro
AU - Ishiguro, Hiroshi
AU - Higashiyama, Shigeki
N1 - Funding Information:
We thank Drs Douglas DeSimone, Judith White, and Tyra Wolfsberg for helpful discussions. This work was supported by a grant-in-aid from Fujita Health University High-tech Research Center from Ministry of Education, Science, Sports and Culture of Japan. Katherine Smith's research was supported by a grant from the NIH (HD26402) to Dr Douglas DeSimone, Univ. of Virginia.
PY - 2002/1/9
Y1 - 2002/1/9
N2 - 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.
AB - 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.
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U2 - 10.1016/S0378-1119(01)00818-6
DO - 10.1016/S0378-1119(01)00818-6
M3 - Article
C2 - 11814695
AN - SCOPUS:0037045406
SN - 0378-1119
VL - 282
SP - 227
EP - 236
JO - Gene
JF - Gene
IS - 1-2
ER -