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   04-NOV-2026, entry version 70.
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, 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: Negative results: does not show hemorrhagic and myotoxic
CC       activities (PubMed:17466550), as well as activity on platelet
CC       aggregation and plasmin (represented by the chromogenic substrate S-
CC       2251) (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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ307451; ABC24687.1; -; mRNA.
DR   PDB; 4GSO; X-ray; 2.60 A; A=1-232.
DR   AlphaFoldDB; Q2PQJ3; -.
DR   SMR; Q2PQJ3; -.
DR   MEROPS; S01.023; -.
DR   GlyCosmos; Q2PQJ3; 2 sites, No reported glycans.
DR   EvolutionaryTrace; Q2PQJ3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; IEA:TreeGrafter.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0035821; P:modulation of process of another organism; IEA:UniProtKB-ARBA.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000158; Thrombin-like enzyme saxthrombin; 1.
DR   FunFam; 2.40.10.10:FF:000153; Venom plasminogen activator TSV-PA; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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
//