VSP1_BOTJR
ID VSP1_BOTJR Reviewed; 232 AA.
AC Q2PQJ3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Thrombin-like enzyme BjussuSP-1;
DE Short=SVTLE BjussuSP-1;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Jararacussin-I;
DE AltName: Full=Snake venom serine protease 1;
DE Short=SVSP;
DE AltName: Full=Thrombin-like enzyme BjussuSP-I;
DE Short=SVTLE BjussuSP-I;
OS Bothrops jararacussu (Jararacussu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8726;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND
RP GLYCOSYLATION.
RC TISSUE=Venom gland;
RX PubMed=17996740; DOI=10.1016/j.biochi.2007.10.005;
RA Sant'Ana C.D., Bernardes C.P., Izidoro L.F., Mazzi M.V., Soares S.G.,
RA Fuly A.L., Zingali R.B., Magro A.J., Braz A.S., Fontes M.R., Stabeli R.G.,
RA Sampaio S.V., Soares A.M.;
RT "Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with
RT procoagulant and kallikrein-like activity isolated from Bothrops
RT jararacussu snake venom.";
RL Biochimie 90:500-507(2008).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, SUBUNIT, ACTIVITY REGULATION,
RP GLYCOSYLATION, AND SIALIC ACID.
RC TISSUE=Venom;
RX PubMed=17466550; DOI=10.1016/j.cbpa.2007.02.036;
RA Sant'Ana C.D., Ticli F.K., Oliveira L.L., Giglio J.R., Rechia C.G.,
RA Fuly A.L., Selistre de Araujo H.S., Franco J.J., Stabeli R.G., Soares A.M.,
RA Sampaio S.V.;
RT "BjussuSP-I: a new thrombin-like enzyme isolated from Bothrops jararacussu
RT snake venom.";
RL Comp. Biochem. Physiol. 151:443-454(2008).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=17292935; DOI=10.1016/j.toxicon.2006.12.011;
RA Perez A.V., Saravia P., Rucavado A., Sant'Ana C.D., Soares A.M.,
RA Gutierrez J.M.;
RT "Local and systemic pathophysiological alterations induced by a serine
RT proteinase from the venom of the snake Bothrops jararacussu.";
RL Toxicon 49:1063-1069(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=23139169; DOI=10.1002/pro.2189;
RA Ullah A., Souza T.A., Zanphorlin L.M., Mariutti R.B., Santana V.S.,
RA Murakami M.T., Arni R.K.;
RT "Crystal structure of jararacussin-I: the highly negatively charged
RT catalytic interface contributes to macromolecular selectivity in snake
RT venom thrombin-like enzymes.";
RL Protein Sci. 22:128-132(2013).
CC -!- FUNCTION: Thrombin-like enzyme that shows clotting activity upon human
CC plasma. Shows specific fibrinogenolytic activity for Aalpha chain
CC (FGA). Hydrolyzes fibrin, BAPNA and TAME, as well as chromogenic
CC artificial substrates of the blood coagulation cascasde: S-27654 for
CC factor X (F10), S-2302 for kallikrein (KLK), factor XIa (F11), and XIIa
CC (F12), and S-2266 for kallikrein and factor XIa (F11). Subcutaneous
CC injection into mice induces a mild edema. Intravenous and intramuscular
CC injection reduce plasma fibrinogen concentration and increase the
CC levels of fibrin(ogen) degradation products. Intramuscular injection
CC also promotes an increase in the expression of proMMP-9, but is unable
CC to activate it. {ECO:0000269|PubMed:17292935,
CC ECO:0000269|PubMed:17466550, ECO:0000269|PubMed:17996740}.
CC -!- ACTIVITY REGULATION: Inhibited by leupeptin, heparin, and 1.10-
CC phenantroline. {ECO:0000269|PubMed:17466550,
CC ECO:0000269|PubMed:17996740}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17466550}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated. Contains sialic acid residues. Deglycosylation
CC reduces in 50% the formation of fibrin clot.
CC {ECO:0000269|PubMed:17466550, ECO:0000269|PubMed:17996740}.
CC -!- MISCELLANEOUS: Does not show hemorrhagic and myotoxic activities
CC (PubMed:17466550), as well as activity on platelet aggregation and
CC plasmin (represented by the chromogenic substrate S-2251)
CC (PubMed:17996740). {ECO:0000305|PubMed:17466550,
CC ECO:0000305|PubMed:17996740}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; DQ307451; ABC24687.1; -; mRNA.
DR PDB; 4GSO; X-ray; 2.60 A; A=1-232.
DR PDBsum; 4GSO; -.
DR AlphaFoldDB; Q2PQJ3; -.
DR SMR; Q2PQJ3; -.
DR MEROPS; S01.023; -.
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 CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 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 3D-structure; Blood coagulation cascade activating toxin;
KW Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Sialic acid; Toxin.
FT CHAIN 1..232
FT /note="Thrombin-like enzyme BjussuSP-1"
FT /id="PRO_0000296362"
FT DOMAIN 1..223
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..138
FT /evidence="ECO:0000269|PubMed:23139169,
FT ECO:0007744|PDB:4GSO"
FT DISULFID 25..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23139169, ECO:0007744|PDB:4GSO"
FT DISULFID 73..230
FT /evidence="ECO:0000269|PubMed:23139169,
FT ECO:0007744|PDB:4GSO"
FT DISULFID 117..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23139169, ECO:0007744|PDB:4GSO"
FT DISULFID 149..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23139169, ECO:0007744|PDB:4GSO"
FT DISULFID 174..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23139169, ECO:0007744|PDB:4GSO"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 15..29
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4GSO"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:4GSO"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:4GSO"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4GSO"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4GSO"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:4GSO"
SQ SEQUENCE 232 AA; 25163 MW; 14C6B2DE6A97064D CRC64;
VLGGDECDIN EHPFLAFLYS HGYFCGLTLI NQEWVVTAAH CDSTNFQMQL GVHSKKVLNE
DEQTRNPKEK FICPNKNMSE VLDKDIMLIK LDKPISNSKH IAPLSLPSNP PSVGSVCRIM
GWGSITIPNE TYPDVPYCAN INLVDYEVCQ GAYNGLPAKT TLCAGVLEGG KDTCVGDSGG
PLICNGQFQG IVSYGAHSCG QGPKPGIYTN VFDYTDWIQR NIAGNTDATC PP
