{PDOC51252}
{PS51252; ANTISTASIN}
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* Antistasin-like domain profile *
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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 beta-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2006 / First entry.

[ 1] Holstein T.W., Mala C., Kurz E., Bauer K., Greber M., David C.N.
     "The primitive metazoan Hydra expresses antistasin, a serine protease
     inhibitor of vertebrate blood coagulation: cDNA cloning, cellular
     localisation and developmental regulation."
     FEBS Lett. 309:288-292(1992).
     PubMed=1516699
[ 2] Mason T.A., McIlroy P.J., Shain D.H.
     "A cysteine-rich protein in the Theromyzon (Annelida: Hirudinea)
     cocoon membrane."
     FEBS Lett. 561:167-172(2004).
     PubMed=15013771; DOI=10.1016/S0014-5793(04)00167-X
[ 3] Mason T.A., McIlroy P.J., Shain D.H.
     "Structural model of an antistasin/notch-like fusion protein from the
     cocoon wall of the aquatic leech, Theromyzon tessulatum."
     J. Mol. Model. (Online). 0:0-0(2006).
     PubMed=16523290; DOI=10.1007/s00894-006-0107-1
[ 4] Rester U., Bode W., Moser M., Parry M.A.A., Huber R., Auerswald E.
     "Structure of the complex of the antistasin-type inhibitor
     bdellastasin with trypsin and modelling of the
     bdellastasin-microplasmin system."
     J. Mol. Biol. 293:93-106(1999).
     PubMed=10512718; DOI=10.1006/jmbi.1999.3162
[ 5] Chopin V., Salzet M., Baert J.-L., Vandenbulcke F., Sautiere P.-E.,
     Kerckaert J.-P., Malecha J.
     "Therostasin, a novel clotting factor Xa inhibitor from the
     rhynchobdellid leech, Theromyzon tessulatum."
     J. Biol. Chem. 275:32701-32707(2000).
     PubMed=10852926; DOI=10.1074/jbc.M909217199

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