VSPA_BOTJA
ID VSPA_BOTJA Reviewed; 232 AA.
AC P81661;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Thrombin-like enzyme bothrombin;
DE Short=SVTLE;
DE EC=3.4.21.74;
DE AltName: Full=Factor VIII activator;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Venombin A;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=8110787; DOI=10.1021/bi00173a030;
RA Nishida S., Fujimura Y., Miura S., Ozaki Y., Usami Y., Suzuki M.,
RA Titani K., Yoshida E., Sugimoto M., Yoshioka A., Fukui H.;
RT "Purification and characterization of bothrombin, a fibrinogen-clotting
RT serine protease from the venom of Bothrops jararaca.";
RL Biochemistry 33:1843-1849(1994).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=12037309; DOI=10.1107/s0907444902003645;
RA Watanabe L., Vieira D.F., Bortoleto R.K., Arni R.K.;
RT "Crystallization of bothrombin, a fibrinogen-converting serine protease
RT isolated from the venom of Bothrops jararaca.";
RL Acta Crystallogr. D 58:1036-1038(2002).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that clots
CC fibrinogen by releasing fibrinopeptide A from the alpha chain of
CC fibrinogen (FGA), induces platelet aggregation through its interaction
CC with GPIb (GP1BA/GP1BB), and activates factor VIII (F8).
CC {ECO:0000269|PubMed:8110787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form
CC fibrin, and release fibrinopeptide A. The specificity of further
CC degradation of fibrinogen varies with species origin of the enzyme.;
CC EC=3.4.21.74;
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP), but
CC not by hirudin. {ECO:0000269|PubMed:8110787}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4-8.0 for the clotting activity.
CC {ECO:0000269|PubMed:8110787};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8110787}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8110787}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:8110787}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; A54361; A54361.
DR AlphaFoldDB; P81661; -.
DR SMR; P81661; -.
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 Toxin.
FT CHAIN 1..232
FT /note="Thrombin-like enzyme bothrombin"
FT /id="PRO_0000088731"
FT DOMAIN 1..223
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 41
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 7..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 26..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 74..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 118..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 150..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 232 AA; 25584 MW; BFCD46A729D3E8AA CRC64;
VIGGDECDIN EHPFLAFMYY SPQYFCGMTL INQEWVLTAA HCDKTYMRIY LGIHTRSVAN
DDEVIRYPKE KFICPNKKKN VITDKDIMLI RLNRPVKNST HIAPISLPSN PPSVGSVCRI
MGWGAITTSE DTYPDVPHCA NINLFNNTVC REAYNGLPAK TLCAGVLQGG IDTCGGDSGG
PLICNGQFQG ILSWGSDPCA EPRKPAFYTK VFDYLPWIQS IIAGNKTATC PP
