VSP27_BOTPI
ID VSP27_BOTPI Reviewed; 50 AA.
AC P0DL26;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Thrombin-like enzyme BpirSP27;
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, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, 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 preferentially degrades the Bbeta
CC chain (FGB) of fibrinogen, with minor effects on the Aalpha chain
CC (FGA). It presents a lower ability to degrade fibrin clots than
CC BpirSP41. It hydrolyzes chromogenic substrates S-2238 (used for testing
CC thrombin activity), S-2222 (factor Xa), S-2266 (glandular kallikrein
CC and factor XIa), S-2302 (plasma kallikrein, factor XIa and XIIa), and
CC S-2251 (plasmin). It shows a decrease in the clotting time of human
CC plasma in the presence of increasing doses of the enzyme. Its minimum
CC coagulant dose (MCD) is 3.5 ug. It also promotes platelet aggregation
CC in a concentration-dependent manner in the presence or absence of
CC calcium. It also shows 20% inhibition of the hemolytic activity
CC promoted by the complement pathways and possess only a minor role in
CC the induction of edema and 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 (Cu2+) and
CC manganese (Mn2+) ions. Not inhibited by metalloprotease inhibitors
CC EDTA, EGTA and 1,10-phenanthroline, as well as by barium (Ba2+) and
CC calcium ion (Ca2+). {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=27121; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22819993};
CC -!- MISCELLANEOUS: Acidic enzyme (pI is 4.7).
CC {ECO:0000305|PubMed:22819993}.
CC -!- MISCELLANEOUS: Does not degrade the gamma chain of fibrinogen (FGG).
CC {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; P0DL26; -.
DR SMR; P0DL26; -.
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 BpirSP27"
FT /id="PRO_0000422276"
FT DOMAIN 1..>50
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 41
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 CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 26..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 50
SQ SEQUENCE 50 AA; 5534 MW; 6593C96FF11E0C03 CRC64;
VVGGDECNIN EHRSLVAIFN STGFFCSGIL LNQEWVLTAS HCDSTNFQMK
