ID   VSP2_CRODM              Reviewed;          20 AA.
AC   P0DKX3;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Thrombin-like enzyme Cdc SII;
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 cumanensis (South American rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184542;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=23178323; DOI=10.1016/j.toxicon.2012.11.010;
RA   Patino A.C., Pereanez J.A., Gutierrez J.M., Rucavado A.;
RT   "Biochemical and biological characterization of a two serine proteinases
RT   from Colombian Crotalus durissus cumanensis snake venom.";
RL   Toxicon 63:32-43(2013).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease that coagulates
CC       human plasma and bovine fibrinogen by hydrolysis of the alpha chains
CC       (FGA) (minimum coagulation dose is 60 ug on fibrinogen). Has
CC       fibrinogenolytic activities, and degrades preferentially the Aalpha
CC       chain (FGA). Shows amidolytic activity toward N-benzoyl-L-Arg-p-
CC       nitroanilide, has a higher activity than Cdc SI. In vivo, intravenous
CC       injection induces defibrin(ogen)ation and a loss of the righting reflex
CC       and opisthotoxins, together with a typical gyroxin-like effect (18-20
CC       minutes). Subcutaneous injection into the footpads induces moderate
CC       edema. Potentiates local hemorrhagic activity induced by
CC       metalloproteinases (BaP1). {ECO:0000269|PubMed:23178323}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by PMSF and moderately
CC       inhibited by leupeptin. Not inhibited by EDTA, aprotinin, pepstatin,
CC       and bestatin. {ECO:0000269|PubMed:23178323}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.145 mM for N-benzoyl-L-Arg-p-nitroanilide
CC         {ECO:0000269|PubMed:23178323};
CC         Vmax=0.267 nmol/min/mg enzyme {ECO:0000269|PubMed:23178323};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=28799.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23178323};
CC   -!- MISCELLANEOUS: Does not induce myotoxicity or hemorrhage, when injected
CC       intramuscularly. Is not lethal when administered either intravenously
CC       or intraperitoneally into mice (maximum dose tested is 50 ug)
CC       (PubMed:23178323). {ECO:0000305|PubMed:23178323}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P0DKX3; -.
DR   SABIO-RK; P0DKX3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>20
FT                   /note="Thrombin-like enzyme Cdc SII"
FT                   /id="PRO_0000421250"
FT   DOMAIN          1..?
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2234 MW;  0459EF62F343FCBD CRC64;
     VIGGDICNIN EHNFLVALYE