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UniProtKB/Swiss-Prot entry Q9TWL9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COMA_CONMA
Primary accession number Q9TWL9
Secondary accession numbers None
Integrated into Swiss-Prot on May 2, 2002
Sequence was last modified on May 2, 2002 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 31)
Name and origin of the protein
Protein name Conodipine-M alpha chain
Synonym EC 3.1.1.4
Gene name None
From
Conus magus (Magus cone) (Magician's cone snail) [TaxID: 6492] 
Taxonomy Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; Apogastropoda; Caenogastropoda; Sorbeoconcha; Hypsogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
TISSUE=Venom;
DOI=10.1074/jbc.270.8.3518; PubMed=7876086 [NCBI, ExPASy, EBI, Israel, Japan]
McIntosh J.M., Ghomashchi F., Gelb M.H., Dooley D.J., Stoehr S.J., Giordani A.B., Naisbitt S.R., Olivera B.M.;
"Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus.";
J. Biol. Chem. 270:3518-3526(1995).
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: Conodipine-M consists of 2 subunits alpha and beta, which may be linked to each other through one or more disulfide bonds.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the venom duct.
  • MASS SPECTROMETRY: Mass=8571; Method=Electrospray; Range=1-77; Source=PubMed:7876086;.
  • SIMILARITY: Belongs to the phospholipase A2 family. Highly divergent.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
3D structure databases
ModBase Q9TWL9.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004623; Molecular function: phospholipase A2 activity (inferred from electronic annotation from EC).
GO:0016042; Biological process: lipid catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009405; Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
BLOCKS Q9TWL9.
ProtoNet Q9TWL9.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Pyrrolidone carboxylic acid; Secreted; Toxin.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   77  77     Conodipine-M alpha chain. PRO_0000086866
ACT_SITE   36   36        Potential. 
MOD_RES   1    1        Pyrrolidone carboxylic acid. 
Sequence information
Length: 77 AA [This is the length of the unprocessed precursor] Molecular weight: 8492 Da [This is the MW of the unprocessed precursor] CRC64: 73861D7587479D8C [This is a checksum on the sequence]
        10         20         30         40         50         60 
QXPSTAELCK INSNACSVPF SXIPCQKXFL AACDRHDTCY HCGKHFGFKQ DDCDDAFFRD 

        70 
MTALCAHGTD DEGXCPX 

Q9TWL9 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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