PROSITE documentation PDOC51252
Antistasin-like domain profile


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 [1]. 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 [2]. Disulfide linkages are between Cys1-Cys4, Cys2-Cys5, and Cys3-Cys6 [3,4].

The antistasin-like domain consists of very short antiparallel β-sheets and interacts with proteinases (see <PDB:1C9T>) [4].

Some proteins known to contain a antistasin-like domain are listed below:

  • Hydra magnipapillata (Hydra) antistasin, a potent inhibitor of factor Xa.
  • Haementeria officinalis (Mexican leech) antistasin, an anticoagulant that displays proteolytic resistance.
  • Haementeria ghilianii (Amazon leech) ghilanten, a potent inhibitor of factor Xa.
  • Hirudo medicinalis (Medicinal leech) hirustasin, it acts as an inhibitor of tissue kallikrein, trypsin, chymotrypsin and neutrophil cathepsin G.
  • Hirudo medicinalis (Medicinal leech) bdellastasin, a strong inhibitor of mammalian trypsin, plasmin and acrosin.
  • Hirudo nipponia (Korean leech) guamerin, it inhibits mammalian elastases.
  • Hirudo nipponia (Korean leech) piguamerin, it inhibits plasma and tissue kallikrein, and trypsin.
  • Theromyzon rude cocoon protein (Tcp), a Cys-rich protein that constitutes a major protein component of the cocoon wall.
  • Theromyzon testulatum therostasin, a potent tight-binding inhibitor of mammalian Factor Xa [5].
  • Caenorhabditis elegans hypothetical protein C08G9.2.
  • Vertebrate cysteine-rich motor neuron 1 protein.

The profile we developed covers the entire antistasin-like domain.

Last update:

August 2006 / First entry.


Technical section

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

ANTISTASIN, PS51252; Antistasin-like domain profile  (MATRIX)


1AuthorsHolstein T.W. Mala C. Kurz E. Bauer K. Greber M. David C.N.
TitleThe primitive metazoan Hydra expresses antistasin, a serine protease inhibitor of vertebrate blood coagulation: cDNA cloning, cellular localisation and developmental regulation.
SourceFEBS Lett. 309:288-292(1992).
PubMed ID1516699

2AuthorsMason T.A. McIlroy P.J. Shain D.H.
TitleA cysteine-rich protein in the Theromyzon (Annelida: Hirudinea) cocoon membrane.
SourceFEBS Lett. 561:167-172(2004).
PubMed ID15013771

3AuthorsMason T.A. McIlroy P.J. Shain D.H.
TitleStructural model of an antistasin/notch-like fusion protein from the cocoon wall of the aquatic leech, Theromyzon tessulatum.
SourceJ. Mol. Model. (Online). 0:0-0(2006).
PubMed ID16523290

4AuthorsRester U. Bode W. Moser M. Parry M.A.A. Huber R. Auerswald E.
TitleStructure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system.
SourceJ. Mol. Biol. 293:93-106(1999).
PubMed ID10512718

5AuthorsChopin V. Salzet M. Baert J.-L. Vandenbulcke F. Sautiere P.-E. Kerckaert J.-P. Malecha J.
TitleTherostasin, a novel clotting factor Xa inhibitor from the rhynchobdellid leech, Theromyzon tessulatum.
SourceJ. Biol. Chem. 275:32701-32707(2000).
PubMed ID10852926

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