Antistasin-like domain (IPR004094)

Short name: Antistasin-like

Overlapping homologous superfamilies


Domain relationships



Antistatin is a small, disulphide cross-linked serine protease inhibitor isolated from the salivary glands of the Mexican leech. It is a potent anticoagulant by virtue of its ability to inhibit factor Xa in the coagulation cascade. Antistatin also exhibits a strong antimetastatic activity. It contains internal repeats of a 25-26 amino acid sequence with a highly conserved pattern of 6 cysteine (Cys) and 2 glycine residues [PMID: 1516699]. Many metazoan proteins share sequence homology with this antistasin-like domain. The unique physical properties of these related Cys-rich proteins (protease resistance; heat, chemical resilience) appear to stem from the common six Cys loop that is cross-linked by three disulfide bonds [PMID: 15013771]. Disulfide linkages are between Cys1-Cys4, Cys2-Cys5, and Cys3-Cys6 [PMID: 16523290, PMID: 10512718].

The antistasin-like domain consists of very short antiparallel beta-sheets and interacts with proteinases [PMID: 10512718].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004867 serine-type endopeptidase inhibitor activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles