VSPP_CERCE
ID VSPP_CERCE Reviewed; 256 AA.
AC Q7SYF1; Q9PRT4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Thrombin-like enzyme cerastocytin;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=C.cerastes platelet proaggregant protein;
DE Short=CC-PPP;
DE AltName: Full=Factor VIII activator;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Proaggregant serine proteinase;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Cerastes cerastes (Horned desert viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX NCBI_TaxID=8697;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom gland;
RX PubMed=12962484; DOI=10.1021/bi034790b;
RA Dekhil H., Wisner A., Marrakchi N., El Ayeb M., Bon C., Karoui H.;
RT "Molecular cloning and expression of a functional snake venom serine
RT proteinase, with platelet aggregating activity, from the Cerastes cerastes
RT viper.";
RL Biochemistry 42:10609-10618(2003).
RN [2]
RP PROTEIN SEQUENCE OF 25-74, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=7766651; DOI=10.1016/0304-4165(94)00216-k;
RA Marrakchi N., Zingali R.B., Karoui H., Bon C., el Ayeb M.;
RT "Cerastocytin, a new thrombin-like platelet activator from the venom of the
RT Tunisian viper Cerastes cerastes.";
RL Biochim. Biophys. Acta 1244:147-156(1995).
RN [3]
RP FUNCTION.
RX PubMed=9080583; DOI=10.1016/s0041-0101(96)00116-x;
RA Marrakchi N., Barbouche R., Guermazi S., Bon C., el Ayeb M.;
RT "Procoagulant and platelet-aggregating properties of cerastocytin from
RT Cerastes cerastes venom.";
RL Toxicon 35:261-272(1997).
CC -!- FUNCTION: Thrombin-like snake venom serine protease which potently
CC induces platelet aggregation and has fibrinogenolytic activities. Clots
CC purified fibrinogen and hydrolyzes alpha-chains (FGA). High
CC concentrations of this enzyme also cleave prothrombin (F2) and factor X
CC (F10). Is also able to activate factor XIII (F8).
CC {ECO:0000269|PubMed:12962484, ECO:0000269|PubMed:7766651,
CC ECO:0000269|PubMed:9080583}.
CC -!- ACTIVITY REGULATION: Its platelets aggregating activity is inhibited by
CC chlorpromazine, theophylline mepacrine. Its platelet aggregating
CC activity and its amidolytic activity are inhibited by PMSF, TPCK, TLCK
CC and soybean trypsin inhibitors. Is unaffected by hirudin or by
CC antithrombin-III in the presence of heparin.
CC {ECO:0000269|PubMed:7766651}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=309 uM for S-2238 {ECO:0000269|PubMed:12962484};
CC KM=850 uM for S-2251 {ECO:0000269|PubMed:12962484};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7766651}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Lacks the conserved Cys-50-Cys-66 disulfide bridge due to the
CC replacement of Cys-50 by a Gly. {ECO:0000305}.
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DR EMBL; AJ553977; CAD86932.1; -; mRNA.
DR PIR; S55674; S55674.
DR AlphaFoldDB; Q7SYF1; -.
DR SMR; Q7SYF1; -.
DR MEROPS; S01.497; -.
DR SABIO-RK; Q7SYF1; -.
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 InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
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.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Platelet aggregation activating toxin; Protease; Secreted; Serine protease;
KW Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:7766651"
FT /id="PRO_0000294994"
FT CHAIN 25..256
FT /note="Thrombin-like enzyme cerastocytin"
FT /id="PRO_0000294995"
FT DOMAIN 25..247
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 98..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 140..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 198..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 44
FT /note="N -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
