Anti-ADAM1 antibody - Metalloproteinase domain (ab65877)

Relevance

ADAM-1, also known as PH-30 alpha and Fertilin-alpha, was first described as a sperm-egg fusion protein from guinea pig. A member of the metalloproteinase family containing disintigrin-like domains (ADAMs), the function of ADAM-1 is still poorly understood. ADAM-1 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active. Like the other ADAMs, ADAM1 domain structure consists of a signal sequence followed by a propeptide domain, a metalloproteinase domain, a disintegrin domain cysteine-rich domain, an EGF-like domain, a transmembrane domain, and a cytoplasmic domain. ADAM1 is produced as two isoforms in the mouse, ADAM1 alpha and ADAM1 beta, which share 77% identity overall. The two sequences differ at the amino and carboxy termini, but are identical from residue 63 of ADAM1 alpha to residue 456, in the disintegrin domain. Both sequences are coded from intronless genes. Human ADAM1 is thought to be a pseudogene of the ADAM1 alpha sequence, and there is no report of a human homologue to mouse ADAM1 beta. The human gene has a stop codon and numerous insertions that change the reading frame of the gene, as well as a 26 bp deletion relative to the murine gene. It is interesting to note that abundant message for human ADAM1 is found in the testis, although there is report of protein produced. The mouse ADAM1 alpha message encodes a protein of 791 amino acids, with a predicted mass of 87.5 kDa and a pI of 5.2. The protein is reported at 100 kDa on SDS PAGE gels, and is processed to a 48 kDa form. ADAM1 beta message encodes a 806 amino acid protein, with predicted mass of 89.4 kDa and pI of4.66, seen as a 120 kDa precursor, processed to a 63-60 kDa form. Localized on the surface of sperm, the ADAM1 isoforms are thought to form a heterodimer with ADAM2 (fertilin-ß), and facilitate sperm-egg fusion, although there is some controversy about the precise actions the proteins play.

Cellular localization

Membrane; single-pass type I membrane protein

Alternative names

Database links