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ADAMs are transmembrane proteins containing both a disintegrin (see <PDOC00351>) and a metalloprotease domain [1]. About two third of the proteins with an ADAM type metalloprotease domain also contain the zinc protease pattern (see <PDOC00129>) which locates the active site of these proteases. As they contain an adhesion domain and a protease domain, ADAM proteins potentially have both cell adhesion and protease activities. They play a role in various biological processes, including fertilization, neurogenesis, myogenesis, embryonic TGF-α release and inflammatory response [2].

ADAMTS proteins [3] form a closely related family of proteases. In these proteins, the metalloprotease and disintegrin domains are flanked by thrombospondin type I (TSP1) repeat (see <PDOC50092>). ADAMTS proteins are soluble, extracellular matrix proteases those known substrates are other extracellular matrix proteins [2].

ADAM proteins also share the metalloprotease and disintegrin domains with the disintegrin class of peptides that are present in snake venom [2,4]. Together, they form the adamlysin/reprolysin subfamily of the metzincin superfamily of Zn-dependent metalloproteinases [4].

Some proteins known to contain an ADAM metalloprotease domain are listed below:

• Human ADAM 1 and 2 (fertilin α and β). Fertilins are sperm surface membrane proteins that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. They lack proteolytic activity.
• Human ADAM 8. It may be involved in immune function.
• Drosophila Kuzbanian. It is involved in neurogenesis. Kuzbanian is a sheddase that has been found to release a soluble form of Delta, a Notch ligand.
• Vertebrate ADAM 10, the homologue of Kuzbanian.
• Caenorhabditis elegans Sup-17, the homologue of Kuzbanian. It is involved in Lin-12/NOTCH signaling.
• Human ADAM 12 (meltrin α). It may be involved in myogenesis.
• Several snake venom metalloproteinases of the disintegrin family. They are not transmembrane proteins.
• Mammalian ADAMTS-1. Protease those expression is associated with acute inflammation as well as development of cancer cachexia.

December 2001 / First entry.

PROSITE method (with tools and information) covered by this documentation:

ADAM_MEPRO, PS50215; ADAM type metalloprotease domain profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Domain architecture view of Swiss-Prot proteins matching PS50215 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50215 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50215 • Scan Swiss-Prot/TrEMBL entries against PS50215 • view ligand binding statistics

Matching PDB structures: 1ATL 1BKC 1BSW 1BUD ... [ALL]

1	Authors	Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.P., Primakoff P., Myles D.G., White J.M.
	Title	ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain.
	Source	Dev. Biol. 169:378-383(1995).
	PubMed ID	7750654

2	Authors	Primakoff P., Myles D.G.
	Title	The ADAM gene family: surface proteins with adhesion and protease activity.
	Source	Trends Genet. 16:83-87(2000).
	PubMed ID	10652535

3	Authors	Tang B.L., Hong W.
	Title	ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats.
	Source	FEBS Lett. 445:223-225(1999).
	PubMed ID	10094461

4	Authors	Black R.A., White J.M.
	Title	ADAMs: focus on the protease domain.
	Source	Curr. Opin. Cell Biol. 10:654-659(1998).
	PubMed ID	9818177

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