VSPL_BOTLC
ID VSPL_BOTLC Reviewed; 231 AA.
AC P0DJ86;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Thrombin-like enzyme leucurobin;
DE Short=Leuc;
DE Short=SVTLE;
DE EC=3.4.21.74;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
OS Bothrops leucurus (Whitetail lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157295;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=16481207; DOI=10.1016/j.cbpa.2005.12.033;
RA Magalhaes A., Magalhaes H.P.B., Richardson M., Gontijo S., Ferreira R.N.,
RA Almeida A.P., Sanchez E.F.;
RT "Purification and properties of a coagulant thrombin-like enzyme from the
RT venom of Bothrops leucurus.";
RL Comp. Biochem. Physiol. 146:565-575(2007).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that cleaves Arg-
CC Gly bonds in alpha-chain of fibrinogen (FGA). Induces temporary
CC episodes of opisthotonos and rapid rolling around the long axis of the
CC animal (gyroxin-like effect), when injected into the tail veins of mice
CC (0.143 ug/g mouse). {ECO:0000269|PubMed:16481207}.
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; Evidence={ECO:0000269|PubMed:16481207};
CC -!- ACTIVITY REGULATION: Inhibited by PMSF and benzamidine. Its clotting
CC effect is strongly inhibited by antibothropic serum. Is not inhibited
CC by heparin. {ECO:0000269|PubMed:16481207}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.9 uM for H-D-Val-Leu-Arg-pNA (S-2266)
CC {ECO:0000269|PubMed:16481207};
CC KM=7.9 uM for H-D-Pro-Phe-Arg-pNA (S-2302)
CC {ECO:0000269|PubMed:16481207};
CC KM=2.7 uM for Bz-Phe-Val-Arg-pNA (S-2160)
CC {ECO:0000269|PubMed:16481207};
CC KM=5.7 uM for H-D-Val-Leu-Lys-pNA (S-2251)
CC {ECO:0000269|PubMed:16481207};
CC pH dependence:
CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:16481207};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16481207}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16481207}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated.
CC -!- MASS SPECTROMETRY: Mass=30475.93; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16481207};
CC -!- MISCELLANEOUS: Does not activate factor XIII (F13A) and is unable to
CC release kinins from heat-treated bovine plasma. Does not cleave beta-
CC chain of fibrinogen (FGB) (PubMed:16481207).
CC {ECO:0000305|PubMed:16481207}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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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 Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..231
FT /note="Thrombin-like enzyme leucurobin"
FT /id="PRO_0000413952"
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 SITE 172
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 231 AA; 25425 MW; 818FB388C3729A98 CRC64;
VIGGDECDIN EHPFLAFMYY SPRYFCGMTL INQEWVLTAA HCNRRFMRIX XXXHAGSVAN
YDEVVRXXXX XFICPNKKKN VITDKDIMLI RLDRPVKNSE HIAPLSLPSN PPSVGSVCRI
MGWGAITTSE DTYPDVPHCA NINLFNNTVC REAYNGLPAK TLCAGVLQGG IDTCGGDSGG
PLICNGQFQG ILSWGSDPCA EPRKPAFYTK VFDYLPWIQS IIAGNKTATC P
