Cell-cell and cell-extracellular matrix interactions are vital for the development and maintenance of an organism (Cal, Arguelles et al. 2001). In the same way, proteolysis of the extracellular matrix is very important for the tissue-remodeling processes occurring during both normal and pathological conditions. These events are mediated by a variety of cell surface adhesion proteins and proteases, with different structural and functional characteristics Among them, are the so called ADAM proteins that have raised considerable interest because of their potential ability to perform both functions, adhesion and proteolysis (Wolfsberg, Primakoff et al. 1995) (Blobel 1997). ADAMs are also associated with reproductive processes like spermatogenesis, sperm-egg binding and fusion (Wolfsberg and White 1996). Nevertheless, these are not the only functions of this kind of proteins, because they have been related to other processes such as myogenesis (Gilpin, Loechel et al. 1998) (5), osteoblast differentiation (6) (Inoue, Reid et al. 1998), and host defense (7) (Mueller, Rissoan et al. 1997). Furthermore, some ADAM family members, including TACE (tumor necrosis factor--converting enzyme), ADAM-12 (meltrin), and ADAM-23, have been suggested to play important roles in the development and progression of inflammatory and tumor processes (8-15) (Emi, Katagiri et al. 1993) (Kratzschmar, Lum et al. 1996).

ADAMs are transmembrane proteins containing both a disintegrin and a metalloprotease domain (Wolfsberg, Straight et al. 1995). About two third of the proteins with an ADAM type metalloprotease domain also contain the zinc protease pattern which locates the active site of these proteases. As they contain an adhesion domain and a protease domain, ADAMs play an important role in adhesion and proteolityc processes.

ADAMTS proteins (Tang and Hong 1999)constitute a related family of proteases. In these proteins, the metalloprotease and disintegrin domains are flanked by thrombospondin type I (TSP1) repeat.

The proposed domain is always found in ADAM-TS family and usually lies between the TSP1 domain (PF00090) and right N-ter of the pfam :ADAM_spacer1 (PF05986).

The TSP1 domain, also known as Thrombospondin type 1, is a repeat that was first described in 1986 by Lawler (Lawler and Hynes 1986). It was found in the thrombospondin protein where it is repeated 3 times. The number of proteins that posses this domain have grown substantially and several proteins involved in the complement pathway (properdin, C6, C7, C8A, C8B, C9) (Patthy 1988) as well as extracellular matrix protein like mindin, F-spondin (Feinstein, Borrell et al. 1999), SCO-spondin and even the circumsporozoite surface protein 2 and TRAP proteins of Plasmodium(Wengelnik, Spaccapelo et al. 1999) (Rogers, Rogers et al. 1992) contain one or more instance of this repeat.

On the other hand, the ADAM_spacer1 represents the Spacer-1 region from the ADAM-TS family of metalloproteinases (Cal, Arguelles et al. 2001).

The matched region was matched as a cysteine-rich region, but no more annotations have been made to this region.


Taxonomic Distribution

Vertebrates: Homo sapiens, Pongo pygmaeus, Mus musculus, Rattus norvegicus, Gallus gallus.
Insects: Drosophila melanogaster, Anopheles gambiae.
Invertebrates: Caenorhabditis elegans, Caenorhabditis brigssae, Haemonchus contortus

PSI-BLAST against ensembl (Apis mellifera)

PSI-BLAST against ensembl (no taxonomic restriction)

Comparison against UNIPROT

Retrived sequences in UNIPROT (txt format)

Downloadable files

Multiple Alignment
PSI-BLAST against ensembl (Apis mellifera)
PSI-BLAST against ensembl (no taxonomic restriction)


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