Reviewed,
UniProtKB/Swiss-Prot Q9TWL9 (COMA_CONMA)
Last modified
June 16, 2009.
Version 34.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Conodipine-M alpha chain EC=3.1.1.4 |
| Organism | Conus magus (Magus cone) (Magician's cone snail) |
| Taxonomic identifier | 6492 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Mollusca › Gastropoda › Orthogastropoda › Apogastropoda › Caenogastropoda › Sorbeoconcha › Hypsogastropoda › Neogastropoda › Conoidea › Conidae › Conus |
Protein attributes
| Sequence length | 77 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Conodipine-M catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This activity may be supported by the alpha chain. Conodipine-M inhibits the binding of isradipine (a ligand specific for L-type calcium channel) to L-type calcium channels. It is inhibited by linoleoyl amide and MG14. |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Calcium. |
| Subunit structure | Conodipine-M consists of 2 subunits alpha and beta, which may be linked to each other through one or more disulfide bonds. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom duct. |
| Sequence similarities | Belongs to the phospholipase A2 family. Highly divergent. |
| Mass spectrometry | Molecular mass is 8571 Da from positions 1 - 77. Determined by ESI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Ligand | Calcium |
| Molecular function | Hydrolase Toxin |
| PTM | Disulfide bond Pyrrolidone carboxylic acid |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus." McIntosh J.M., Ghomashchi F., Gelb M.H., Dooley D.J., Stoehr S.J., Giordani A.B., Naisbitt S.R., Olivera B.M. J. Biol. Chem. 270:3518-3526(1995) [PubMed: 7876086] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Venom. |
Cross-references
Entry information
| Entry name | COMA_CONMA | ||||||||
| Accession | Primary (citable) accession number: Q9TWL9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

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