Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC50215ADAM type metalloprotease domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50215
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:
| 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 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.