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Thrombin-like enzyme BpirSP27 (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Fragment)

 VSP27_BOTPI             Reviewed;          50 AA.
P0DL26;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-2013, sequence version 1.
22-NOV-2017, entry version 19.
RecName: Full=Thrombin-like enzyme BpirSP27;
Short=SVTLE;
EC=3.4.21.-;
AltName: Full=Fibrinogen-clotting enzyme;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Flags: Fragment;
Bothrops pirajai (Piraja's lance0 head).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=113192;
[1]
PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, AND MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=22819993; DOI=10.1016/j.biochi.2012.07.007;
Menaldo D.L., Bernardes C.P., Santos-Filho N.A., Moura Lde A.,
Fuly A.L., Arantes E.C., Sampaio S.V.;
"Biochemical characterization and comparative analysis of two distinct
serine proteases from Bothrops pirajai snake venom.";
Biochimie 94:2545-2558(2012).
[2]
FUNCTION, AND BIOASSAY.
PubMed=23499645; DOI=10.1016/j.intimp.2013.02.023;
Menaldo D.L., Bernardes C.P., Pereira J.C., Silveira D.S.,
Mamede C.C., Stanziola L., de Oliveira F., Pereira-Crott L.S.,
Faccioli L.H., Sampaio S.V.;
"Effects of two serine proteases from Bothrops pirajai snake venom on
the complement system and the inflammatory response.";
Int. Immunopharmacol. 15:764-771(2013).
-!- FUNCTION: Snake venom serine protease that interferes with the
hemostatic system of the prey. It preferentially degrades the
Bbeta chain (FGB) of fibrinogen, with minor effects on the Aalpha
chain (FGA). It presents a lower ability to degrade fibrin clots
than BpirSP41. It hydrolyzes chromogenic substrates S-2238 (used
for testing thrombin activity), S-2222 (factor Xa), S-2266
(glandular kallikrein and factor XIa), S-2302 (plasma kallikrein,
factor XIa and XIIa), and S-2251 (plasmin). It shows a decrease in
the clotting time of human plasma in the presence of increasing
doses of the enzyme. Its minimum coagulant dose (MCD) is 3.5 ug.
It also promotes platelet aggregation in a concentration-dependent
manner in the presence or absence of calcium. It also shows 20%
inhibition of the hemolytic activity promoted by the complement
pathways and possess only a minor role in the induction of edema
and pain in rat. {ECO:0000269|PubMed:22819993,
ECO:0000269|PubMed:23499645}.
-!- ENZYME REGULATION: Inhibited by serine protease inhibitors PMSF,
benzamidine, leupeptin and aprotinin, as well as by copper (Cu2+)
and manganese (Mn2+) ions. Not inhibited by metalloprotease
inhibitors EDTA, EGTA and 1,10-phenanthroline, as well as by
barium (Ba2+) and calcium ion (Ca2+).
{ECO:0000269|PubMed:22819993}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:22819993};
Temperature dependence:
Optimum temperature is 4-60 degrees Celsius.
{ECO:0000269|PubMed:22819993};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:22819993}.
-!- MASS SPECTROMETRY: Mass=27121; Method=MALDI; Range=1-?;
Evidence={ECO:0000269|PubMed:22819993};
-!- MISCELLANEOUS: Acidic enzyme (pI is 4.7).
{ECO:0000305|PubMed:22819993}.
-!- MISCELLANEOUS: Does not degrade the gamma chain of fibrinogen
(FGG). {ECO:0000305|PubMed:22819993}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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SMR; P0DL26; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
Pfam; PF00089; Trypsin; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
1: Evidence at protein level;
Blood coagulation cascade activating toxin;
Complement system impairing toxin; Direct protein sequencing;
Disulfide bond; Fibrinolytic toxin; Glycoprotein;
Hemostasis impairing toxin; Hydrolase;
Platelet aggregation activating toxin; Protease; Secreted;
Serine protease; Toxin.
CHAIN 1 >50 Thrombin-like enzyme BpirSP27.
/FTId=PRO_0000422276.
DOMAIN 1 >50 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 41 41 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000255|PROSITE-ProRule:PRU10078,
ECO:0000255|PROSITE-ProRule:PRU10079}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 7 ? {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 26 42 {ECO:0000255|PROSITE-ProRule:PRU00274}.
NON_TER 50 50
SEQUENCE 50 AA; 5534 MW; 6593C96FF11E0C03 CRC64;
VVGGDECNIN EHRSLVAIFN STGFFCSGIL LNQEWVLTAS HCDSTNFQMK


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