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Protein

Thrombin-like enzyme BjussuSP-1

Gene
N/A
Organism
Bothrops jararacussu (Jararacussu)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thrombin-like enzyme that shows clotting activity upon human plasma. Shows specific fibrinogenolytic activity for Aalpha chain (FGA). Hydrolyzes fibrin, BAPNA and TAME, as well as chromogenic artificial substrates of the blood coagulation cascasde: S-27654 for factor X (F10), S-2302 for kallikrein (KLK), factor XIa (F11), and XIIa (F12), and S-2266 for kallikrein and factor XIa (F11). Subcutaneous injection into mice induces a mild edema. Intravenous and intramuscular injection reduce plasma fibrinogen concentration and increase the levels of fibrin(ogen) degradation products. Intramuscular injection also promotes an increase in the expression of proMMP-9, but is unable to activate it.3 Publications

Enzyme regulationi

Inhibited by leupeptin, heparin, and 1.10-phenantroline.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei40Charge relay systemBy similarity1
Active sitei85Charge relay systemBy similarity1
Active sitei178Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Fibrinolytic toxin, Hemostasis impairing toxin, Hydrolase, Protease, Serine protease, Toxin

Keywords - Ligandi

Sialic acid

Protein family/group databases

MEROPSiS01.023.

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombin-like enzyme BjussuSP-1 (EC:3.4.21.-)
Short name:
SVTLE BjussuSP-1
Alternative name(s):
Fibrinogen-clotting enzyme
Jararacussin-I
Snake venom serine protease 1
Short name:
SVSP
Thrombin-like enzyme BjussuSP-I
Short name:
SVTLE BjussuSP-I
OrganismiBothrops jararacussu (Jararacussu)
Taxonomic identifieri8726 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002963621 – 232Thrombin-like enzyme BjussuSP-1Add BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi7 ↔ 138PROSITE-ProRule annotation1 Publication
Disulfide bondi25 ↔ 41PROSITE-ProRule annotation1 Publication
Disulfide bondi73 ↔ 230PROSITE-ProRule annotation1 Publication
Glycosylationi77N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi117 ↔ 184PROSITE-ProRule annotation1 Publication
Glycosylationi129N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi149 ↔ 163PROSITE-ProRule annotation1 Publication
Disulfide bondi174 ↔ 199PROSITE-ProRule annotation1 Publication

Post-translational modificationi

N-glycosylated. Contains sialic acid residues. Deglycosylation reduces in 50% the formation of fibrin clot.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni9 – 11Combined sources3
Beta strandi15 – 29Combined sources15
Beta strandi31 – 37Combined sources7
Helixi39 – 41Combined sources3
Beta strandi47 – 51Combined sources5
Beta strandi63 – 65Combined sources3
Beta strandi67 – 72Combined sources6
Beta strandi87 – 93Combined sources7
Beta strandi116 – 123Combined sources8
Beta strandi126 – 129Combined sources4
Beta strandi137 – 143Combined sources7
Helixi147 – 150Combined sources4
Beta strandi161 – 165Combined sources5
Beta strandi181 – 184Combined sources4
Beta strandi187 – 194Combined sources8
Beta strandi206 – 210Combined sources5
Helixi211 – 214Combined sources4
Helixi215 – 223Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GSOX-ray2.60A1-232[»]
ProteinModelPortaliQ2PQJ3.
SMRiQ2PQJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 223Peptidase S1PROSITE-ProRule annotationAdd BLAST223

Sequence similaritiesi

Belongs to the peptidase S1 family. Snake venom subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2PQJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VLGGDECDIN EHPFLAFLYS HGYFCGLTLI NQEWVVTAAH CDSTNFQMQL
60 70 80 90 100
GVHSKKVLNE DEQTRNPKEK FICPNKNMSE VLDKDIMLIK LDKPISNSKH
110 120 130 140 150
IAPLSLPSNP PSVGSVCRIM GWGSITIPNE TYPDVPYCAN INLVDYEVCQ
160 170 180 190 200
GAYNGLPAKT TLCAGVLEGG KDTCVGDSGG PLICNGQFQG IVSYGAHSCG
210 220 230
QGPKPGIYTN VFDYTDWIQR NIAGNTDATC PP
Length:232
Mass (Da):25,163
Last modified:January 24, 2006 - v1
Checksum:i14C6B2DE6A97064D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ307451 mRNA. Translation: ABC24687.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ307451 mRNA. Translation: ABC24687.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GSOX-ray2.60A1-232[»]
ProteinModelPortaliQ2PQJ3.
SMRiQ2PQJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVSP1_BOTJR
AccessioniPrimary (citable) accession number: Q2PQJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not show hemorrhagic and myotoxic activities (PubMed:17466550), as well as activity on platelet aggregation and plasmin (represented by the chromogenic substrate S-2251) (PubMed:17996740).2 Publications

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.