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Thrombin-like enzyme cerastocytin (SVTLE) (EC 3.4.21.-) (C.cerastes platelet proaggregant protein) (CC-PPP) (Factor VIII activator) (Fibrinogen-clotting enzyme) (Proaggregant serine proteinase) (Snake venom serine protease) (SVSP)

 VSPP_CERCE              Reviewed;         256 AA.
Q7SYF1; Q9PRT4;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
23-MAY-2018, entry version 71.
RecName: Full=Thrombin-like enzyme cerastocytin;
Short=SVTLE;
EC=3.4.21.-;
AltName: Full=C.cerastes platelet proaggregant protein;
Short=CC-PPP;
AltName: Full=Factor VIII activator;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Proaggregant serine proteinase;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Flags: Precursor;
Cerastes cerastes (Horned desert viper).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
NCBI_TaxID=8697;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
TISSUE=Venom gland;
PubMed=12962484; DOI=10.1021/bi034790b;
Dekhil H., Wisner A., Marrakchi N., El Ayeb M., Bon C., Karoui H.;
"Molecular cloning and expression of a functional snake venom serine
proteinase, with platelet aggregating activity, from the Cerastes
cerastes viper.";
Biochemistry 42:10609-10618(2003).
[2]
PROTEIN SEQUENCE OF 25-74, FUNCTION, ENZYME REGULATION, AND SUBUNIT.
TISSUE=Venom;
PubMed=7766651; DOI=10.1016/0304-4165(94)00216-K;
Marrakchi N., Zingali R.B., Karoui H., Bon C., el Ayeb M.;
"Cerastocytin, a new thrombin-like platelet activator from the venom
of the Tunisian viper Cerastes cerastes.";
Biochim. Biophys. Acta 1244:147-156(1995).
[3]
FUNCTION.
PubMed=9080583; DOI=10.1016/S0041-0101(96)00116-X;
Marrakchi N., Barbouche R., Guermazi S., Bon C., el Ayeb M.;
"Procoagulant and platelet-aggregating properties of cerastocytin from
Cerastes cerastes venom.";
Toxicon 35:261-272(1997).
-!- FUNCTION: Thrombin-like snake venom serine protease which potently
induces platelet aggregation and has fibrinogenolytic activities.
Clots purified fibrinogen and hydrolyzes alpha-chains (FGA). High
concentrations of this enzyme also cleave prothrombin (F2) and
factor X (F10). Is also able to activate factor XIII (F8).
{ECO:0000269|PubMed:12962484, ECO:0000269|PubMed:7766651,
ECO:0000269|PubMed:9080583}.
-!- ENZYME REGULATION: Its platelets aggregating activity is inhibited
by chlorpromazine, theophylline mepacrine. Its platelet
aggregating activity and its amidolytic activity are inhibited by
PMSF, TPCK, TLCK and soybean trypsin inhibitors. Is unaffected by
hirudin or by antithrombin-III in the presence of heparin.
{ECO:0000269|PubMed:7766651}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=309 uM for S-2238 {ECO:0000269|PubMed:12962484};
KM=850 uM for S-2251 {ECO:0000269|PubMed:12962484};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7766651}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: Lacks the conserved Cys-50-Cys-66 disulfide bridge due to
the replacement of Cys-50 by a Gly. {ECO:0000305}.
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EMBL; AJ553977; CAD86932.1; -; mRNA.
PIR; S55674; S55674.
ProteinModelPortal; Q7SYF1; -.
SMR; Q7SYF1; -.
MEROPS; S01.497; -.
PRIDE; Q7SYF1; -.
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.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
Platelet aggregation activating toxin; Protease; Secreted;
Serine protease; Signal; Toxin; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 24 {ECO:0000269|PubMed:7766651}.
/FTId=PRO_0000294994.
CHAIN 25 256 Thrombin-like enzyme cerastocytin.
/FTId=PRO_0000294995.
DOMAIN 25 247 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system. {ECO:0000250}.
ACT_SITE 108 108 Charge relay system. {ECO:0000250}.
ACT_SITE 202 202 Charge relay system. {ECO:0000250}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 161 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 98 254 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 140 208 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 172 187 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 198 223 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 44 44 N -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 256 AA; 27974 MW; 62F57976F89ECED1 CRC64;
MVLISVLASL LVLQLSYAQK SSELVIGGAE CNINEHRSLV LLYNSSRLFG GGTLINKEWV
LSAAHCDGEN MKIYLGLHHF RLPNKDRQIR VAKEKYFCRD RKSIVDKDIM LIKLNKPVNN
STHIAPLSLP SSPPSVGSDC RIMGWGTITS PNDTYPKVPH CANINILEHS LCERAYNDLS
ASSRTLCAGI EKGGIDTCKG DSGGPLICNG QIQGIVSWGD EVCGKPNKPG VYTKVFDYTD
WIRNIIAGNT AATCPQ


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