Reviewed, UniProtKB/Swiss-Prot P84475 (PA21A_BUNCA)

Names and origin

Protein names	Recommended name:     Phospholipase A2, neurotoxin T1-1 A chain     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase T1-1 A
Organism	Bungarus candidus (Malayan krait)
Taxonomic identifier	92438 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	14 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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 + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion By similarity.
Subunit structure	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.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium
Molecular function	Hydrolase Neurotoxin Presynaptic neurotoxin Toxin
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW synaptic transmission Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›14	›14	Phospholipase A2, neurotoxin T1-1 A chain		PRO_0000161630
Experimental info
	Non-terminal residue	14	1

Sequences

	Sequence		Length	Mass (Da)
	P84475-1 [UniParc]. Last modified April 12, 2005. Version 1. Checksum: 6E91DBA06720A09B	FASTA	14	1,816
	10 NLYQFKEMIR YTIP

References

[1]

"Isolation, toxicity and amino terminal sequences of three major neurotoxins in the venom of Malayan krait (Bungarus candidus) from Thailand." Khow O., Chanhome L., Omori-Satoh T., Ogawa Y., Yanoshita R., Samejima Y., Kuch U., Mebs D., Sitprija V. J. Biochem. 134:799-804(2003) [PubMed: 14769867] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LETHAL DOSE. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P84475.
Family and domain databases
InterPro	IPR013090. Phospholipase_A2_AS. [Graphical view]
PROSITE	PS00119. PA2_ASP. Partial match. PS00118. PA2_HIS. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21A_BUNCA

Accession

Primary (citable) accession number: P84475

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	April 12, 2005
Last modified:	November 4, 2008
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)