VSPF1_CALRH
ID VSPF1_CALRH Reviewed; 234 AA.
AC P26324;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Thrombin-like enzyme ancrod;
DE Short=SVTLE;
DE EC=3.4.21.74;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Venombin A;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=1544412; DOI=10.1016/0014-5793(92)80559-y;
RA Burkhart W., Simth G.F.H., Su J.-L., Parikh I., Levine H. III;
RT "Amino acid sequence determination of ancrod, the thrombin-like alpha-
RT fibrinogenase from the venom of Akistrodon rhodostoma.";
RL FEBS Lett. 297:297-301(1992).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that acts as an
CC anticoagulant. It cleaves fibrinogen (FGA) to split off the A-
CC fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The
CC resulting fibrin polymers are imperfectly formed and much smaller in
CC size (1 to 2 um long) than the fibrin polymers produced by the action
CC of thrombin. These ancrod-induced microthrombi are friable, unstable,
CC urea-soluble and have significantly degraded alpha chains. They do not
CC cross-link to form thrombi. They are markedly susceptible to digestion
CC by plasmin and are rapidly removed from circulation by either
CC reticuloendothelial phagocytosis or normal fibrinolysis, or both.
CC Anticoagulation through the removal of fibrinogen from the blood is
CC rapid, occurring within hours following its administration. It does not
CC activate plasminogen and does not degrade preformed, fully cross-linked
CC thrombin fibrin. It also reduces the level of plasminogen activator
CC inhibitor (PAI) and may stimulate the release of tissue plasminogen
CC activator (PLAT) from the endothelium. The profibrinolytic effect of
CC these 2 actions appears to be limited to local microthrombus
CC degradation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form
CC fibrin, and release fibrinopeptide A. The specificity of further
CC degradation of fibrinogen varies with species origin of the enzyme.;
CC EC=3.4.21.74;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PHARMACEUTICAL: Used for the treatment of acute ischemic stroke. Until
CC 2002 was available under the brand name Arvin or Arwin (Knoll). Is
CC actually available under the brand name Viprinex (Abbott).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ancrod entry;
CC URL="https://en.wikipedia.org/wiki/Ancrod";
CC -!- WEB RESOURCE: Name=RxMed; Note=Viprinex entry;
CC 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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DR PIR; S20407; S20407.
DR AlphaFoldDB; P26324; -.
DR SMR; P26324; -.
DR MEROPS; S01.178; -.
DR GlyConnect; 50; 24 N-Linked glycans.
DR iPTMnet; P26324; -.
DR BRENDA; 3.4.21.74; 198.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Pharmaceutical; Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..234
FT /note="Thrombin-like enzyme ancrod"
FT /id="PRO_0000088730"
FT DOMAIN 1..227
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1544412"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1544412"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1544412"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1544412"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1544412"
FT DISULFID 7..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 28..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 78..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 120..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 178..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ 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
