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[1]
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PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND LETHAL DOSE.
TISSUE=Venom;
DOI=10.1093/jb/mvg187; PubMed=14769867 [NCBI, ExPASy, EBI, Israel, Japan]
Khow O.,
Chanhome L.,
Omori-Satoh T.,
Ogawa Y.,
Yanoshita R.,
Samejima Y.,
Kuch U.,
Mebs D.,
Sitprija V.;
"Isolation, toxicity and amino terminal sequences of three major neurotoxins in the venom of Malayan krait (Bungarus candidus) from Thailand.";
J. Biochem. 134:799-804(2003).
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- FUNCTION: Neurotoxin T1-1 is a presynaptic neurotoxin of the venom that exhibits indirect hemolytic activity against human erythrocytes. PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini.
- CATALYTIC ACTIVITY: Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
- COFACTOR: Binds 1 calcium ion (By similarity).
- SUBUNIT: Heterodimer; disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors.
- SUBCELLULAR LOCATION: Secreted.
- TISSUE SPECIFICITY: Expressed by the venom gland.
- TOXIC DOSE: LD50 is 0.26 mg/kg by intravenous injection in mice.
- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
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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: 14 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 1816 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 6E91DBA06720A09B [This is a checksum on the sequence] |
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