*603710	Links
A DISINTEGRIN AND METALLOPROTEINASE DOMAIN 23; ADAM23

Alternative titles; symbols

METALLOPROTEINASE-LIKE, DISINTEGRIN-LIKE, AND CYSTEINE-RICH PROTEIN 3; MDC3

Gene map locus 2q33

TEXT

DESCRIPTION

The cellular disintegrins, also known as ADAM (a disintegrin and metalloproteinase) and MDC (metalloproteinase-like, disintegrin-like, and cysteine-rich) proteins, are a class of potential cell adhesion molecules.

CLONING

By searching an EST database for sequences related to MDC (155120), Sagane et al. (1998) identified a partial MDC3 cDNA. They screened a human brain cDNA library and used 3-prime RACE to clone additional cDNAs corresponding to the entire MDC3 coding region. The predicted 832-amino acid protein contains the typical cellular disintegrin domains (see MDC2, 603709). However, the zinc-binding motif, which is critical for proteinase activity, is disrupted in MDC3 as well as the other MDC proteins. MDC3 shares approximately 52% sequence similarity with MDC and MDC2. Northern blot analysis revealed that MDC3 was expressed predominantly in brain as several transcripts ranging in size from 3.5 to 7 kb.

MAPPING

By radiation hybrid analysis, Poindexter et al. (1999) mapped the ADAM23 gene to chromosome 2q33.

REFERENCES

1. Poindexter, K.; Nelson, N.; DuBose, R. F.; Black, R. A.; Cerretti, D. P. :

The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries. Gene 237: 61-70, 1999.
PubMed ID : 10524237

2. Sagane, K.; Ohya, Y.; Hasegawa, Y.; Tanaka, I. :

Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain. Biochem. J. 334: 93-98, 1998.
PubMed ID : 9693107

CONTRIBUTORS

Carol A. Bocchini - updated : 6/27/2002

CREATION DATE

Rebekah S. Rasooly : 4/8/1999

EDIT HISTORY

terry : 6/27/2002
mgross : 4/13/1999

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