P23807 (IXXB_PROFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 78.
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: Coagulation factor IX/factor X-binding protein subunit B Short name=IX/X-BP |
| Organism | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
| Taxonomic identifier | 88087 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Trimeresurus |
Protein attributes
| Sequence length | 146 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | When linked to subunit A of IX/X-bp, anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX and factor X in the presence of calcium with a 1 to 1 stoichiometry. Ref.3 Ref.4 When linked to subunit A of IX-bp, anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factor IX (but not to factor X) in the presence of calcium with a 1 to 1 stoichiometry. Ref.3 Ref.4 |
| Subunit structure | Forms an heterodimer with subunit A of IX/X-bp or IX-bp; disulfide-linked. Ref.5 Ref.6 Ref.7 Ref.8 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Miscellaneous | Calcium is required for ligand binding. |
| Sequence similarities | Contains 1 C-type lectin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Lectin Metal-binding |
| Molecular function | Toxin |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sugar bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Ref.2 | ||||||||||||||||||||||||
| Chain | 24 – 146 | 123 | Coagulation factor IX/factor X-binding protein subunit B | PRO_0000017531 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Domain | 24 – 146 | 123 | C-type lectin | ||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||
| Metal binding | 64 | 1 | Calcium; via carbonyl oxygen | ||||||||||||||||||||||||
| Metal binding | 66 | 1 | Calcium | ||||||||||||||||||||||||
| Metal binding | 70 | 1 | Calcium | ||||||||||||||||||||||||
| Metal binding | 143 | 1 | Calcium | ||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Disulfide bond | 25 ↔ 36 | Ref.5 Ref.6 Ref.7 Ref.8 | |||||||||||||||||||||||||
| Disulfide bond | 53 ↔ 142 | Ref.5 Ref.6 Ref.7 Ref.8 | |||||||||||||||||||||||||
| Disulfide bond | 98 | Interchain (with C-102 in subunit A of IX/X-bp or with C-79 in subunit A of IX-bp) Ref.5 Ref.6 Ref.7 Ref.8 | |||||||||||||||||||||||||
| Disulfide bond | 119 ↔ 134 | Ref.5 Ref.6 Ref.7 Ref.8 | |||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Beta strand | 29 – 32 | 4 | |||||||||||||||||||||||||
| Beta strand | 35 – 44 | 10 | |||||||||||||||||||||||||
| Helix | 46 – 56 | 11 | |||||||||||||||||||||||||
| Helix | 68 – 82 | 15 | |||||||||||||||||||||||||
| Beta strand | 86 – 88 | 3 | |||||||||||||||||||||||||
| Beta strand | 100 – 102 | 3 | |||||||||||||||||||||||||
| Beta strand | 118 – 123 | 6 | |||||||||||||||||||||||||
| Beta strand | 129 – 133 | 5 | |||||||||||||||||||||||||
| Beta strand | 138 – 145 | 8 | |||||||||||||||||||||||||
Sequences
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References
| [1] | "cDNA cloning of IX/X-BP, a heterogeneous two-chain anticoagulant protein from snake venom." Matsuzaki R., Yoshihara E., Yamada M., Shima K., Atoda H., Morita T. Biochem. Biophys. Res. Commun. 220:382-387(1996) [PubMed: 8645314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
| [2] | "The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin E." Atoda H., Hyuga M., Morita T. J. Biol. Chem. 266:14903-14911(1991) [PubMed: 1831197] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-146. Tissue: Venom. |
| [3] | "Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis." Atoda H., Yoshida N., Ishikawa M., Morita T. Eur. J. Biochem. 224:703-708(1994) [PubMed: 7925387] [Abstract] Cited for: FUNCTION. |
| [4] | "Blood coagulation factor IX-binding protein from the venom of Trimeresurus flavoviridis: purification and characterization." Atoda H., Ishikawa M., Yoshihara E., Sekiya F., Morita T. J. Biochem. 118:965-973(1995) [PubMed: 8749314] [Abstract] Cited for: FUNCTION. Tissue: Venom. |
| [5] | "Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains." Mizuno H., Fujimoto Z., Koizumi M., Kano H., Atoda H., Morita T. Nat. Struct. Biol. 4:438-441(1997) [PubMed: 9187649] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-146 IN DIMER WITH IX/X-BP, METAL-BINDING SITES, DISULFIDE BONDS. |
| [6] | "Crystal structure of coagulation factor IX-binding protein from habu snake venom at 2.6 A: implication of central loop swapping based on deletion in the linker region." Mizuno H., Fujimoto Z., Koizumi M., Kano H., Atoda H., Morita T. J. Mol. Biol. 289:103-112(1999) [PubMed: 10339409] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-146 IN DIMER WITH IX-BP, METAL-BINDING SITES, DISULFIDE BONDS. |
| [7] | "Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein." Shikamoto Y., Morita T., Fujimoto Z., Mizuno H. J. Biol. Chem. 278:24090-24094(2003) [PubMed: 12695512] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 24-146 IN DIMER WITH IX-BP, METAL-BINDING SITES, DISULFIDE BONDS. |
| [8] | "pH-dependent structural changes at Ca(2+)-binding sites of coagulation factor IX-binding protein." Suzuki N., Fujimoto Z., Morita T., Fukamizu A., Mizuno H. J. Mol. Biol. 353:80-87(2005) [PubMed: 16165155] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 24-146 IN DIMER WITH IX-BP, METAL-BINDING SITES, DISULFIDE BONDS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D83332 mRNA. Translation: BAA11888.1. | ||||||||||||||||||||||||||||||||||||||||||
| PIR | JC4691. | ||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||||||||||||||
| ProteinModelPortal | P23807. | ||||||||||||||||||||||||||||||||||||||||||
| SMR | P23807. Positions 24-146. | ||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||
| HOVERGEN | HBG004151. | ||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR001304. C-type_lectin. IPR016186. C-type_lectin-like. IPR018378. C-type_lectin_CS. IPR016187. C-type_lectin_fold. IPR003990. Pancreatis_ac. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| Gene3D | G3DSA:3.10.100.10. C-type_lectin-like. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF00059. Lectin_C. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| PRINTS | PR01504. PNCREATITSAP. | ||||||||||||||||||||||||||||||||||||||||||
| 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 | IXXB_PROFL | ||||||||
| Accession | Primary (citable) accession number: P23807 Secondary accession number(s): Q91247 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Animal Toxin Annotation Program | ||||||||
| 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 |

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