ID VSP1_BOTMA Reviewed; 285 AA.
AC P0DJE9;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Thrombin-like enzyme TLBm;
DE Short=SVTLE TLBm;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
OS Bothrops marajoensis (Marajo lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157554;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19931298; DOI=10.1016/j.toxicon.2009.11.006;
RA Vilca-Quispe A., Ponce-Soto L.A., Winck F.V., Marangoni S.;
RT "Isolation and characterization of a new serine protease with thrombin-like
RT activity (TLBm) from the venom of the snake Bothrops marajoensis.";
RL Toxicon 55:745-753(2010).
CC -!- FUNCTION: Thrombin-like enzyme that induces the formation of fibrin
CC clot. Cleaves the Aalpha-chain of fibrinogen (FGA) with higher activity
CC than the Bbeta-chain (FGB). Induces platelet aggregation in both
CC platelet-rich plasma and in washed platelet preparations. This
CC aggregation is strongly inhibited by preincubation of the enzyme with
CC PMSF. {ECO:0000269|PubMed:19931298}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF, disodium-EDTA, S(Dm) and
CC soybean trypsin inhibitor (SBTI). SBTI and S(Dm) (the anti-hemorrhagic
CC protein) acts as a non-competitive inhibitors that decrease the
CC enzymatic activity. {ECO:0000269|PubMed:19931298}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 M for N-alpha-benzoyl-DL-arginine-p-nitroanilide
CC {ECO:0000269|PubMed:19931298};
CC Vmax=0.052 nmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-
CC nitroanilide {ECO:0000269|PubMed:19931298};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19931298};
CC Temperature dependence:
CC Optimum temperature is 38-40 degrees Celsius.
CC {ECO:0000269|PubMed:19931298};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Homologous thrombin-like enzymes are N-glycosylated. This enzyme
CC does not contain the consensus glycosylation sites, suggesting it is
CC not glycosylated.
CC -!- MASS SPECTROMETRY: Mass=33332.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19931298};
CC -!- MISCELLANEOUS: Negative results: has no activity on the gamma-chain of
CC fibrinogen (FGG). In vivo, does not induce a significant edema activity
CC in mice (PubMed:19931298). {ECO:0000305|PubMed:19931298}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DJE9; -.
DR SMR; P0DJE9; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044478; P:envenomation resulting in positive regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1.
DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Hemostasis impairing toxin; Hydrolase;
KW Platelet aggregation activating toxin; Protease; Secreted; Serine protease;
KW Toxin.
FT CHAIN 1..285
FT /note="Thrombin-like enzyme TLBm"
FT /id="PRO_0000416019"
FT DOMAIN 1..273
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 45
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 7..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 30..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 94..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 156..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 192..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 224..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 285 AA; 33241 MW; 7F761F39ADE0CF13 CRC64;
VIGGDECNIN ESPFLAFLYS QLLSSRRYFC GMTLINQEWV LTAAHCNLYP DRKDMNWWLL
IKLGKHSGST RRWVANYDEQ VRYWPKEKFI WWYCPNKKKD VINNYVWVWW DKDILLWELW
MLIRLNRPVK YSEHIAPLSL PSSPPSAKWW HVGSVCRIMG WGQITETWWN SEDTLPDVPR
CANINLFNYE VCRAYNQRWW RGLPAKTLCA GDLEGIIRGG WDTCVGDSGG PLICDGQYQG
IAYWGSKPCA EPDEPAAYSK VFDHLDWSQS VIAGGTWWRG DDTCP
//
