VSPG_BITGA
ID VSPG_BITGA Reviewed; 19 AA.
AC P0C577;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Thrombin-like enzyme gabonase;
DE Short=SVTLE;
DE EC=3.4.21.55;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Venombin-AB;
DE Flags: Fragment;
OS Bitis gabonica (Gaboon adder) (Gaboon viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX NCBI_TaxID=8694;
RN [1]
RP PROTEIN SEQUENCE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Venom;
RX PubMed=3522580; DOI=10.1016/s0021-9258(19)84456-3;
RA Pirkle H., Theodor I., Miyada D., Simmons G.;
RT "Thrombin-like enzyme from the venom of Bitis gabonica. Purification,
RT properties, and coagulant actions.";
RL J. Biol. Chem. 261:8830-8835(1986).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. Releases both
CC fibrinopeptides A and B from fibrinogen (FGA and FGB) to form fibrin
CC clots. Also activates factor XIII (F13A). The activity of the enzyme is
CC stabilized by calcium ion.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa bonds in fibrinogen to form
CC fibrin and release fibrinopeptides A and B.; EC=3.4.21.55;
CC -!- ACTIVITY REGULATION: Inhibited by PMSF, but not by heparin, hirudin and
CC antithrombin-III. {ECO:0000269|PubMed:3522580}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for Tosyl-L-arginine methyl ester (TAME)
CC {ECO:0000269|PubMed:3522580};
CC KM=0.13 mM for Tosyl-Gly-Pro-Arg 4-nitroanilide
CC {ECO:0000269|PubMed:3522580};
CC KM=0.82 mM for H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide
CC {ECO:0000269|PubMed:3522580};
CC KM=0.88 mM for H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide
CC {ECO:0000269|PubMed:3522580};
CC KM=2.72 mM for Tosyl-Gly-Pro-Lys 4-nitroanilide
CC {ECO:0000269|PubMed:3522580};
CC KM=3.4 mM for H-D-Phenylglycine-Phe-Arg 4-nitroanilide
CC {ECO:0000269|PubMed:3522580};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius with tosyl-Arg-methyl ester
CC (TAME) as substrate and 37 degrees Celsius with natural substrates.
CC {ECO:0000269|PubMed:3522580};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3522580}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated.
CC -!- PTM: Contains five disulfide bonds. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR AlphaFoldDB; P0C577; -.
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; Calcium;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Toxin.
FT CHAIN 1..>19
FT /note="Thrombin-like enzyme gabonase"
FT /id="PRO_0000295177"
FT DOMAIN 1..>19
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 19
SQ SEQUENCE 19 AA; 2017 MW; 4B7BA6C802F4E553 CRC64;
VVGGAECKID GHRCLALLY
