ID   VSP_CRODC               Reviewed;          44 AA.
AC   P0DKY5;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Thrombin-like enzyme F202;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Crotalus durissus cascavella (Northeastern Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184540;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE
RP   BONDS.
RC   TISSUE=Venom;
RX   PubMed=16729248; DOI=10.1007/s10930-006-9001-z;
RA   Fonseca F.V., Antunes E., Morganti R.P., Monteiro H.S., Martins A.M.,
RA   Toyama D.O., Marangoni S., Toyama M.H.;
RT   "Characterization of a new platelet aggregating factor from crotoxin
RT   Crotalus durissus cascavella venom.";
RL   Protein J. 25:183-192(2006).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that coagulates
CC       fibrinogen by inducing a fast degradation of the alpha chain (FGA) from
CC       human citrated plasma, and a slow degradation of beta chain (FGB).
CC       Potently induces platelet aggregation in both platelet rich plasma and
CC       washed platelet preparations in a concentration-dependent fashion.
CC       Shows amidolytic activities. {ECO:0000269|PubMed:16729248}.
CC   -!- ACTIVITY REGULATION: Enzyme activity is markedly inhibited by TLCK and
CC       PMSF, and moderately by SBTi. Platelet aggregating activity is strongly
CC       inhibited by TLCK.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.58 mM for BApNA {ECO:0000269|PubMed:16729248};
CC         Vmax=5.64 umol/min/mg enzyme {ECO:0000269|PubMed:16729248};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 6 disulfide bonds.
CC   -!- MISCELLANEOUS: Does not affect the gamma chain of fibrinogen (FGG).
CC       {ECO:0000305|PubMed:16729248}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DKY5; -.
DR   SMR; P0DKY5; -.
DR   SABIO-RK; P0DKY5; -.
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   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Disulfide bond; Fibrinogenolytic toxin; Hemostasis impairing toxin;
KW   Hydrolase; Platelet aggregation activating toxin; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           1..>44
FT                   /note="Thrombin-like enzyme F202"
FT                   /id="PRO_0000421798"
FT   DOMAIN          1..>44
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        41
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-
FT                   ProRule:PRU10079"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         44
SQ   SEQUENCE   44 AA;  4815 MW;  65CAD53DA8E51230 CRC64;
     VVGGDECNIN EHRFLVALYA NSSLLCGGTL INQEWVLIAA HCDR