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Thrombin-like enzyme TLBm (SVTLE TLBm) (EC 3 4 21 -) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)

 VSP1_BOTMA              Reviewed;         285 AA.
P0DJE9;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 1.
02-DEC-2020, entry version 24.
RecName: Full=Thrombin-like enzyme TLBm;
Short=SVTLE TLBm;
EC=3.4.21.-;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Bothrops marajoensis (Marajo lancehead).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=157554;
[1]
PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=19931298; DOI=10.1016/j.toxicon.2009.11.006;
Vilca-Quispe A., Ponce-Soto L.A., Winck F.V., Marangoni S.;
"Isolation and characterization of a new serine protease with thrombin-like
activity (TLBm) from the venom of the snake Bothrops marajoensis.";
Toxicon 55:745-753(2010).
-!- FUNCTION: Thrombin-like enzyme that induces the formation of fibrin
clot. Cleaves the Aalpha-chain of fibrinogen (FGA) with higher activity
than the Bbeta-chain (FGB). Induces platelet aggregation in both
platelet-rich plasma and in washed platelet preparations. This
aggregation is strongly inhibited by preincubation of the enzyme with
PMSF. {ECO:0000269|PubMed:19931298}.
-!- ACTIVITY REGULATION: Inhibited by PMSF, disodium-EDTA, S(Dm) and
soybean trypsin inhibitor (SBTI). SBTI and S(Dm) (the anti-hemorrhagic
protein) acts as non-competitive inhibitors that decrease the enzymatic
activity. {ECO:0000269|PubMed:19931298}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.23 M for N-alpha-benzoyl-DL-arginine-p-nitroanilide
{ECO:0000269|PubMed:19931298};
Vmax=0.052 nmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-
nitroanilide {ECO:0000269|PubMed:19931298};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:19931298};
Temperature dependence:
Optimum temperature is 38-40 degrees Celsius.
{ECO:0000269|PubMed:19931298};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: Homologous thrombin-like enzymes are N-glycosylated. This enzyme
does not contain the consensus glycosylation sites, suggesting it is
not glycosylated.
-!- MASS SPECTROMETRY: Mass=33332.5; Method=MALDI;
Evidence={ECO:0000269|PubMed:19931298};
-!- MISCELLANEOUS: Has no activity on the gamma-chain of fibrinogen (FGG).
In vivo, does not induces a significant edema activity in mice
(PubMed:19931298). {ECO:0000305|PubMed:19931298}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in other organism; IDA:UniProtKB.
GO; GO:0044478; P:envenomation resulting in positive regulation of platelet aggregation in other organism; IDA:UniProtKB.
GO; GO:0044481; P:envenomation resulting in proteolysis in other organism; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin; Direct protein sequencing;
Disulfide bond; Hemostasis impairing toxin; Hydrolase;
Platelet aggregation activating toxin; Protease; Secreted; Serine protease;
Toxin.
CHAIN 1..285
/note="Thrombin-like enzyme TLBm"
/id="PRO_0000416019"
DOMAIN 1..273
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 45
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 113
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 228
/note="Charge relay system"
/evidence="ECO:0000250"
DISULFID 7..181
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
DISULFID 30..46
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
DISULFID 94..284
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
DISULFID 156..234
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
DISULFID 192..209
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
DISULFID 224..249
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
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


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Related Genes :
[] Thrombin-like enzyme cerastocytin (SVTLE) (EC 3.4.21.-) (C.cerastes platelet proaggregant protein) (CC-PPP) (Factor VIII activator) (Fibrinogen-clotting enzyme) (Proaggregant serine proteinase) (Snake venom serine protease) (SVSP)
[] Thrombin-like enzyme BJ-48 (SVTLE BJ-48) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Fragment)
[] Thrombin-like enzyme stejnobin (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
[] Thrombin-like enzyme BpirSP27 (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Fragment)
[] Thrombin-like enzyme bhalternin (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
[] Thrombin-like enzyme LMR-47 (SVTLE LM-47) (SVTLE LMR-47) (EC 3.4.21.74) (Fibrinogen-clotting enzyme) (Gyroxin analog) (Snake venom serine protease) (SVSP) (Venombin A) (Fragment)
[] Thrombin-like enzyme BpirSP41 (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Fragment)
[] Thrombin-like enzyme ancrod (SVTLE) (EC 3.4.21.74) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Venombin A)
[] Thrombin-like enzyme elegaxobin-1 (SVTLE) (EC 3.4.21.-) (Elegaxobin I) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
[] Thrombin-like enzyme BpSP-1 (SVTLE BpSP-1) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Thrombin-like enzyme BpSP-I) (SVTLE BpSP-I) (Fragment)
[] Thrombin-like enzyme Cdc SI (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Fragment)
[] Thrombin-like enzyme Cdc SII (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Fragment)
[] Thrombin-like enzyme gyroxin B1.4 (SVTLE gyroxin B1.4) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
[] Thrombin-like enzyme gyroxin B1.3 (SVTLE gyroxin B1.3) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
[] Thrombin-like enzyme gyroxin B1.7 (SVTLE gyroxin B1.7) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
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[] Thrombin-like enzyme gyroxin B2.1 (SVTLE gyroxin B2.1) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
[] Venom plasminogen activator LV-PA (EC 3.4.21.-) (LMUT0402S) (Plasminogen activating proteinase) (Snake venom serine protease) (SVSP)
[] Chymotrypsin-like protease VLCTLP (EC 3.4.21.-) (Snake venom serine protease) (SVSP) (Vipera Lebetina with chymotrypsin-like proteolytic activity)
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Bibliography :