Anti-ADAM30 antibody - Metalloproteinase domain (ab40136)

Relevance

ADAM30 was first cloned along with ADAM29 from human testis cDNA, in a search for novel ADAMs. The ADAM29 and ADAM30 sequences are dissimilar, and share 37% identity on the amino acid level. Two different ADAM30 sequences were identified in the initial paper, 790 amino acids and 781 amino acids. The 9 amino acid deletion in the shorter form is in the cytoplasmic domain, and may affect interaction with cytoplasmic elements. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs), the function of ADAM23 is still poorly understood. ADAM30 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and is not thought to be proteolytically active. ADAM29 does not have this conserved zinc binding motif, and it is tempting to speculate that the two proteins form a heterodimer, such as ADAM1 and ADAM2 do (although there is no direct evidence to date for such an interaction). Other ADAMs family members (ADAM10, ADAM17) have been more thoroughly studied, and are known to play key roles in inflammation, growth factor maturation and release, and a wide range of other functions. The full length ADAM30 sequence codes for a 790 amino acid protein, containing a Type I transmembrane domain, with a predicted mass of 88.94 kDa and a pI of 8.16. The shorter form is 781 amino acids, with predicted mass of 88 kDa and 8.50 pI.

Cellular localization

Membrane; single pass type I membrane protein

Alternative names

Database links