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Thrombin-like enzyme ancrod (SVTLE) (EC 3.4.21.74) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Venombin A)

 VSPF1_CALRH             Reviewed;         234 AA.
P26324;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
25-APR-2018, entry version 96.
RecName: Full=Thrombin-like enzyme ancrod;
Short=SVTLE;
EC=3.4.21.74;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Snake venom serine protease;
Short=SVSP;
AltName: Full=Venombin A;
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Calloselasma.
NCBI_TaxID=8717;
[1]
PROTEIN SEQUENCE.
TISSUE=Venom;
PubMed=1544412; DOI=10.1016/0014-5793(92)80559-Y;
Burkhart W., Simth G.F.H., Su J.-L., Parikh I., Levine H. III;
"Amino acid sequence determination of ancrod, the thrombin-like alpha-
fibrinogenase from the venom of Akistrodon rhodostoma.";
FEBS Lett. 297:297-301(1992).
-!- FUNCTION: Thrombin-like snake venom serine protease that acts as
an anticoagulant. It cleaves fibrinogen (FGA) to split off the A-
fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The
resulting fibrin polymers are imperfectly formed and much smaller
in size (1 to 2 um long) than the fibrin polymers produced by the
action of thrombin. These ancrod-induced microthrombi are friable,
unstable, urea-soluble and have significantly degraded alpha
chains. They do not cross-link to form thrombi. They are markedly
susceptible to digestion by plasmin and are rapidly removed from
circulation by either reticuloendothelial phagocytosis or normal
fibrinolysis, or both. Anticoagulation through the removal of
fibrinogen from the blood is rapid, occurring within hours
following its administration. It does not activate plasminogen and
does not degrade preformed, fully cross-linked thrombin fibrin. It
also reduces the level of plasminogen activator inhibitor (PAI)
and may stimulate the release of tissue plasminogen activator
(PLAT) from the endothelium. The profibrinolytic effect of these 2
actions appears to be limited to local microthrombus degradation.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Xaa bond in
fibrinogen, to form fibrin, and release fibrinopeptide A. The
specificity of further degradation of fibrinogen varies with
species origin of the enzyme.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PHARMACEUTICAL: Used for the treatment of acute ischemic stroke.
Until 2002 was available under the brand name Arvin or Arwin
(Knoll). Is actually available under the brand name Viprinex
(Abbott).
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Ancrod entry;
URL="https://en.wikipedia.org/wiki/Ancrod";
-!- WEB RESOURCE: Name=RxMed; Note=Viprinex entry;
URL="https://www.rxmed.com/b.main/b2.pharmaceutical/b2.1.monographs/CPS-%20Monographs/CPS-%20%28General%20Monographs-%20V%29/VIPRINEX.html";
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PIR; S20407; S20407.
ProteinModelPortal; P26324; -.
SMR; P26324; -.
MEROPS; S01.178; -.
GlyConnect; 50; -.
iPTMnet; P26324; -.
UniCarbKB; P26324; -.
HOVERGEN; HBG013304; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
1: Evidence at protein level;
Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
Pharmaceutical; Protease; Secreted; Serine protease; Toxin.
CHAIN 1 234 Thrombin-like enzyme ancrod.
/FTId=PRO_0000088730.
DOMAIN 1 227 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 43 43 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 88 88 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 182 182 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
CARBOHYD 23 23 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1544412}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1544412}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1544412}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1544412}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1544412}.
DISULFID 7 141 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 28 44 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 78 232 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 120 188 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 152 167 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 178 203 {ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 234 AA; 26570 MW; 3C55F0276B65E5CF CRC64;
VIGGDECNIN EHRFLVAVYE GTNWTFICGG VLIHPEWVIT AEHCARRRMN LVFGMHRKSE
KFDDEQERYP KKRYFIRCNK TRTSWDEDIM LIRLNKPVNN SEHIAPLSLP SNPPIVGSDC
RVMGWGSINR RIDVLSDEPR CANINLHNFT MCHGLFRKMP KKGRVLCAGD LRGRRDSCNS
DSGGPLICNE ELHGIVARGP NPCAQPNKPA LYTSIYDYRD WVNNVIAGNA TCSP


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