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 22-FEB-2023, entry version 18.
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: Negative results: does not induce myotoxicity or
CC hemorrhage, when injected intramuscularly. Is not lethal when
CC administered either intravenously or intraperitoneally into mice
CC (maximum dose tested is 50 ug) (PubMed:23178323).
CC {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
//
