VSP41_BOTPI
ID VSP41_BOTPI Reviewed; 50 AA.
AC P0DL27;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Thrombin-like enzyme BpirSP41;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Fragment;
OS Bothrops pirajai (Piraja's lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=113192;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22819993; DOI=10.1016/j.biochi.2012.07.007;
RA Menaldo D.L., Bernardes C.P., Santos-Filho N.A., Moura Lde A., Fuly A.L.,
RA Arantes E.C., Sampaio S.V.;
RT "Biochemical characterization and comparative analysis of two distinct
RT serine proteases from Bothrops pirajai snake venom.";
RL Biochimie 94:2545-2558(2012).
RN [2]
RP FUNCTION, AND BIOASSAY.
RX PubMed=23499645; DOI=10.1016/j.intimp.2013.02.023;
RA Menaldo D.L., Bernardes C.P., Pereira J.C., Silveira D.S., Mamede C.C.,
RA Stanziola L., de Oliveira F., Pereira-Crott L.S., Faccioli L.H.,
RA Sampaio S.V.;
RT "Effects of two serine proteases from Bothrops pirajai snake venom on the
RT complement system and the inflammatory response.";
RL Int. Immunopharmacol. 15:764-771(2013).
CC -!- FUNCTION: Snake venom serine protease that interferes with the
CC hemostatic system of the prey. It almost completely degrades both
CC Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen. It presents a higher
CC ability to degrade fibrin clots than BpirSP27. It hydrolyzes
CC chromogenic substrates S-2238 (used for testing thrombin activity), S-
CC 2222 (factor Xa), S-2266 (glandular kallikrein and factor XIa), and S-
CC 2302 (plasma kallikrein, factor XIa and XIIa). It shows a decrease in
CC the clotting time of human plasma in the presence of increasing doses
CC of the enzyme. Its minimum coagulant dose (MCD) is 20 ug. It promotes
CC platelet aggregation with a maximum of aggregation of 20%, regardless
CC of the concentration increase or the presence of calcium. It also shows
CC 40% inhibition of the hemolytic activity promoted by the complement
CC pathways and possess only a minor role in the induction of edema and
CC pain in rat. {ECO:0000269|PubMed:22819993,
CC ECO:0000269|PubMed:23499645}.
CC -!- ACTIVITY REGULATION: Inhibited by serine protease inhibitors PMSF,
CC benzamidine, leupeptin and aprotinin, as well as by copper ions (Cu2+).
CC Not inhibited by metalloprotease inhibitors EDTA, EGTA and 1,10-
CC phenanthroline, as well as by barium (Ba2+) and calcium ion (Ca2+).
CC {ECO:0000269|PubMed:22819993}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:22819993};
CC Temperature dependence:
CC Optimum temperature is 4-60 degrees Celsius.
CC {ECO:0000269|PubMed:22819993};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:22819993}.
CC -!- MASS SPECTROMETRY: Mass=40639; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22819993};
CC -!- MISCELLANEOUS: Acidic enzyme (pI is 3.7).
CC {ECO:0000305|PubMed:22819993}.
CC -!- MISCELLANEOUS: Does not degrade the gamma chain of fibrinogen (FGG). It
CC has no activity on S-2251 (used for testing plasmin activity)
CC (PubMed:22819993). {ECO:0000305|PubMed:22819993}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR AlphaFoldDB; P0DL27; -.
DR SMR; P0DL27; -.
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 Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin;
KW Complement system impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase;
KW Platelet aggregation activating toxin; Protease; Secreted; Serine protease;
KW Toxin.
FT CHAIN 1..>50
FT /note="Thrombin-like enzyme BpirSP41"
FT /id="PRO_0000422277"
FT DOMAIN 1..>50
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-
FT ProRule:PRU10079"
FT DISULFID 7..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 25..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 50
SQ SEQUENCE 50 AA; 5836 MW; 11457A5DF16B1303 CRC64;
VVGGDECDIN EHPFLAFLYS HGYFCGLTLI NQEWVLTAAH CDRRFMRIYL
