P22029 (LECBA_BOTJA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 74.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Snaclec botrocetin subunit alpha Alternative name(s): Platelet coagglutinin |
| Organism | Bothrops jararaca (Jararaca) |
| Taxonomic identifier | 8724 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops |
Protein attributes
| Sequence length | 133 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| 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 component | Secreted |
| Ligand | Lectin |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | sugar binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 133 | 133 | Snaclec botrocetin subunit alpha | PRO_0000046697 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Domain | 9 – 129 | 121 | C-type lectin | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Disulfide bond | 2 ↔ 13 | Ref.1 Ref.3 Ref.4 Ref.5 | ||||||||||||||||||||||||||||
| Disulfide bond | 30 ↔ 128 | Ref.1 Ref.3 Ref.4 Ref.5 | ||||||||||||||||||||||||||||
| Disulfide bond | 80 | Interchain (with C-75 in beta chain) Ref.1 Ref.3 Ref.4 Ref.5 | ||||||||||||||||||||||||||||
| Disulfide bond | 103 ↔ 120 | Ref.1 Ref.3 Ref.4 Ref.5 | ||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 7 – 9 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 12 – 21 | 10 | ||||||||||||||||||||||||||||
| Helix | 23 – 33 | 11 | ||||||||||||||||||||||||||||
| Helix | 48 – 59 | 12 | ||||||||||||||||||||||||||||
| Beta strand | 66 – 73 | 8 | ||||||||||||||||||||||||||||
| Beta strand | 76 – 80 | 5 | ||||||||||||||||||||||||||||
| Helix | 97 – 99 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 103 – 107 | 5 | ||||||||||||||||||||||||||||
| Turn | 108 – 111 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 114 – 118 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 124 – 130 | 7 | ||||||||||||||||||||||||||||
Sequences
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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 | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A47267. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||
| ProteinModelPortal | P22029. | ||||||||||||||||||||||||||||||
| SMR | P22029. Positions 1-133. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| HOVERGEN | HBG004151. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR002353. AntifreezeII. IPR001304. C-type_lectin. IPR016186. C-type_lectin-like. IPR018378. C-type_lectin_CS. IPR016187. C-type_lectin_fold. [Graphical view] | ||||||||||||||||||||||||||||||
| Gene3D | G3DSA:3.10.100.10. C-type_lectin-like. 1 hit. | ||||||||||||||||||||||||||||||
| Pfam | PF00059. Lectin_C. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PRINTS | PR00356. ANTIFREEZEII. | ||||||||||||||||||||||||||||||
| SMART | SM00034. CLECT. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF56436. C-type_lectin_fold. 1 hit. | ||||||||||||||||||||||||||||||
| PROSITE | PS00615. C_TYPE_LECTIN_1. 1 hit. PS50041. C_TYPE_LECTIN_2. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | LECBA_BOTJA | ||||||||
| Accession | Primary (citable) accession number: P22029 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with