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Reviewed, UniProtKB/Swiss-Prot P04971 (VSPA_BOTAT)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Thrombin-like enzyme batroxobin
      Short name=BX
    EC=3.4.21.74
Alternative name(s):
    Bothrops atrox serine proteinase
    Venombin-A
    Defibrase
    Reptilase
OrganismBothrops atrox (Barba amarilla) (Fer-de-lance)
Taxonomic identifier8725 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Thrombin-like snake venom serine protease. Cleaves Arg-Gly bonds in fibrinogen alpha chains; does not cleave fibrinogen beta chains.

Catalytic activity

Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Biotechnological use

Is used for the investigation of the last phase of blood coagulation. Due to its heparin insensitivity it can detect fibrinogen polymerization disorders even in the presence of heparin.

Pharmaceutical use

Available under the name Defibrase (Pentapharm) for the treatment of thrombotic diseases.

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termPharmaceutical
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Propeptide19 – 246
PRO_0000028379
Chain25 – 255231Thrombin-like enzyme batroxobin
PRO_0000028380

Regions

Domain25 – 247223Peptidase S1

Sites

Active site651Charge relay system By similarity
Active site1101Charge relay system By similarity
Active site2021Charge relay system By similarity
Site1961Required for specificity By similarity

Amino acid modifications

Glycosylation1701N-linked (GlcNAc...)
Glycosylation2491N-linked (GlcNAc...)
Disulfide bond31 ↔ 163 By similarity
Disulfide bond50 ↔ 66 By similarity
Disulfide bond98 ↔ 254 By similarity
Disulfide bond142 ↔ 208 By similarity
Disulfide bond174 ↔ 187 By similarity
Disulfide bond198 ↔ 223 By similarity

Sequences

Sequence LengthMass (Da)Tools
P04971-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: BE155BBC5DF8431B

FASTA25528,189
        10         20         30         40         50         60 
MVLIRVIANL LILQVSYAQK SSELVIGGDE CDINEHPFLA FMYYSPRYFC GMTLINQEWV 

        70         80         90        100        110        120 
LTAAHCNRRF MRIHLGKHAG SVANYDEVVR YPKEKFICPN KKKNVITDKD IMLIRLDRPV 

       130        140        150        160        170        180 
KNSEHIAPLS LPSNPPSVGS VCRIMGWGAI TTSEDTYPDV PHCANINLFN NTVCREAYNG 

       190        200        210        220        230        240 
LPAKTLCAGV LQGGIDTCGG DSGGPLICNG QFQGILSWGS DPCAEPRKPA FYTKVFDYLP 

       250 
WIQSIIAGNK TATCP 

« Hide

References

[1]"Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme."
Itoh N., Tanaka N., Mihashi S., Yamashina I.
J. Biol. Chem. 262:3132-3135(1987) [PubMed: 3546302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family."
Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S., Yamashina I.
J. Biol. Chem. 263:7628-7631(1988) [PubMed: 3163691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete nucleotide sequence of the gene for batroxobin, a thrombin-like snake venom enzyme."
Itoh N., Tanaka N., Funakoshi I., Kawasaki T., Mihashi S., Yamashima I.
Nucleic Acids Res. 16:10377-10378(1988) [PubMed: 3194214] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The coagulant enzyme from Bothrops atrox venom (batroxobin)."
Stocker K., Barlow G.H.
Methods Enzymol. 45:214-223(1976) [PubMed: 1011993] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Carbohydrate structure analysis of batroxobin, a thrombin-like serine protease from Bothrops moojeni venom."
Lochnit G., Geyer R.
Eur. J. Biochem. 228:805-816(1995) [PubMed: 7737180] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE ON ASN-170 AND ASN-249.

Cross-references

Sequence databases

J02684 mRNA. Translation: AAA48552.1.
X12747 Genomic DNA. Translation: CAA31240.1.
M20894 expand/collapse EMBL AC list , M20890, M20891, M20892, M20893 Genomic DNA. Translation: AAA48553.1. Sequence problems.
PIRA28169.

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBaseSearch...

Protein family/group databases

MEROPSS01.176.

Phylogenomic databases

HOVERGENP04971.

Enzyme and pathway databases

BRENDA3.4.21.74. 18615.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVSPA_BOTAT
AccessionPrimary (citable) accession number: P04971
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents