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[1]
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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).
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- 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.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| 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] |
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10 20 30 40 50 60
QXPSTAELCK INSNACSVPF SXIPCQKXFL AACDRHDTCY HCGKHFGFKQ DDCDDAFFRD
70
MTALCAHGTD DEGXCPX
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Q9TWL9 in FASTA format |
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