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Open Access Research article

Identification and preliminary characterization of mouse Adam33

Teresa M Gunn13*, Arezou Azarani14, Philip H Kim1, Richard W Hyman2, Ronald W Davis2 and Gregory S Barsh1

Author Affiliations

1 Departments of Pediatrics and Genetics, and the Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA, USA

2 Department of Biochemistry and the Stanford DNA Sequencing and Technology Center, Stanford University School of Medicine, Stanford, CA, USA

3 Current address: Department of Biomedical Sciences, Cornell University, Ithaca, NY, USA

4 Current address: Robbins Scientific, Sunnyvale, CA, USA

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BMC Genetics 2002, 3:2  doi:10.1186/1471-2156-3-2

Published: 13 February 2002



The metalloprotease-disintegrin family, or ADAM, proteins, are implicated in cell-cell interactions, cell fusion, and cell signaling, and are widely distributed among metazoan phyla. Orthologous relationships have been defined for a few ADAM proteins including ADAM10 (Kuzbanian), and ADAM17 (TACE), but evolutionary relationships are not clear for the majority of family members. Human ADAM33 refers to a testis cDNA clone that does not contain a complete open reading frame, but portions of the predicted protein are similar to Xenopus laevis ADAM13.


In a 48 kb region of mouse DNA adjacent to the Attractin gene on mouse chromosome 2, we identified sequences very similar to human ADAM33. A full-length mouse cDNA was identified by a combination of gene prediction programs and RT-PCR, and the probable full-length human cDNA was identified by comparison to human genomic sequence in the homologous region on chromosome 20p13. Mouse ADAM33 is 44% identical to Xenopus laevis ADAM13, however a phylogenetic alignment and consideration of functional domains suggests that the two genes are not orthologous. Mouse Adam33 is widely expressed, most highly in the adult brain, heart, kidney, lung and testis.


While mouse ADAM33 is similar to Xenopus ADAM13 in sequence, further examination of its embryonic expression pattern, catalytic activity and protein interactions will be required to assess the functional relationship between these two proteins. Adam33 is expressed in the mouse adult brain and could play a role in complex processes that require cell-cell communication.