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P22029 (LECBA_BOTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Snaclec botrocetin subunit alpha
Alternative name(s):
Platelet coagglutinin
OrganismBothrops jararaca (Jararaca)
Taxonomic identifier8724 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet GPIb(alpha)/GP1BA, resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets.

Subunit structure

Heterodimer of subunits alpha and beta; disulfide-linked. Botrocetin and vWF form a soluble complex. Ref.1 Ref.3 Ref.4 Ref.5

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Biotechnological use

Is a standard reagent for testing vWF/platelet interactions and detection of the defects in von Willebrand disease and in GPIb-related disorders such as Bernard-Soulier syndrome.

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Cellular componentSecreted
   LigandLectin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 133133Snaclec botrocetin subunit alpha
PRO_0000046697

Regions

Domain9 – 129121C-type lectin

Amino acid modifications

Disulfide bond2 ↔ 13 Ref.1 Ref.3 Ref.4 Ref.5
Disulfide bond30 ↔ 128 Ref.1 Ref.3 Ref.4 Ref.5
Disulfide bond80Interchain (with C-75 in beta chain) Ref.1 Ref.3 Ref.4 Ref.5
Disulfide bond103 ↔ 120 Ref.1 Ref.3 Ref.4 Ref.5

Secondary structure

...................... 133
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22029 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: E4CF4502946AC74B

FASTA13315,215
        10         20         30         40         50         60 
DCPSGWSSYE GNCYKFFQQK MNWADAERFC SEQAKGGHLV SIKIYSKEKD FVGDLVTKNI 

        70         80         90        100        110        120 
QSSDLYAWIG LRVENKEKQC SSEWSDGSSV SYENVVERTV KKCFALEKDL GFVLWINLYC 

       130 
AQKNPFVCKS PPP 

« Hide

References

[1]"Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca."
Usami Y., Fujimura Y., Suzuki M., Ozeki Y., Nishio K., Fukui H., Titani K.
Proc. Natl. Acad. Sci. U.S.A. 90:928-932(1993) [PubMed: 8430107] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
Tissue: Venom.
[2]"Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca."
Fujimura Y., Titani K., Usami Y., Suzuki M., Oyama R., Matsui T., Fukui H., Sugimoto M., Ruggeri Z.M.
Biochemistry 30:1957-1964(1991) [PubMed: 1993206] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-40.
Tissue: Venom.
[3]"Crystal structure of the von Willebrand factor modulator botrocetin."
Sen U., Vasudevan S., Subbarao G., McClintock R.A., Celikel R., Ruggeri Z.M., Varughese K.I.
Biochemistry 40:345-352(2001) [PubMed: 11148028] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BOND.
[4]"Structural basis of von Willebrand factor activation by the snake toxin botrocetin."
Fukuda K., Doggett T.A., Bankston L.A., Cruz M.A., Diacovo T.G., Liddington R.C.
Structure 10:943-950(2002) [PubMed: 12121649] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), DISULFIDE BOND.
[5]"The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation."
Fukuda K., Doggett T., Laurenzi I.J., Liddington R.C., Diacovo T.G.
Nat. Struct. Mol. Biol. 12:152-159(2005) [PubMed: 15665869] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA47267.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FVUX-ray1.80A/C1-133[»]
1IJKX-ray2.60B1-133[»]
1U0NX-ray2.95B1-133[»]
1U0OX-ray2.70A1-133[»]
ProteinModelPortalP22029.
SMRP22029. Positions 1-133.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004151.

Family and domain databases

InterProIPR002353. AntifreezeII.
IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
Gene3DG3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
PRINTSPR00356. ANTIFREEZEII.
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLECBA_BOTJA
AccessionPrimary (citable) accession number: P22029
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families