Q8QFW3 (PA22_BUNCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2, beta bungarotoxin A2 chain EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase
Organism	Bungarus caeruleus (Indian krait)
Taxonomic identifier	132961 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. Acts presynaptically By similarity.
Catalytic activity	Phosphatidylcholine + H2O = 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 By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Neurotoxin Presynaptic neurotoxin Toxin
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	other organism presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro 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
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 27	8	By similarity		PRO_0000022825
	Chain	28 – 147	120	Phospholipase A2, beta bungarotoxin A2 chain		PRO_0000022826
Sites
	Active site	75	1	By similarity
	Active site	121	1	By similarity
	Metal binding	55	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	57	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	59	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	76	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	42		Interchain (with a B chain) By similarity
	Disulfide bond	54 ↔ 146		By similarity
	Disulfide bond	56 ↔ 72		By similarity
	Disulfide bond	71 ↔ 127		By similarity
	Disulfide bond	78 ↔ 120		By similarity
	Disulfide bond	88 ↔ 113		By similarity
	Disulfide bond	106 ↔ 118		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8QFW3 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3B72A0EEE323EADF	FASTA	147	16,120
	10 20 30 40 50 60 MYPAHLLVLS AVCVSLLGAA NIPPYPLNLI NFMEMIRYTI PCDKTWGHYA DYGCYCGAGG 70 80 90 100 110 120 SGTPVDALDR CCYVHDNCYG VAENKHKCNP KTQSCSYKLT KRTIICYGAA GTCGRIVCDC 130 140 DRTAALCFGD SEYIGAHKNI DTKRHCQ

References

[1]	"Bungarus caeruleus mRNA for phospholipase A2, beta bungarotoxin A2 chain complete coding region." Paramasivam M., Srinivasan A., Singh T.P. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY081147 mRNA. Translation: AAL87004.1.
3D structure databases
ProteinModelPortal	Q8QFW3.
SMR	Q8QFW3. Positions 28-147.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG008137.
Family and domain databases
InterPro	IPR016090. PLipase_A2. IPR013090. PLipase_A2_AS. IPR001211. PLipase_A2_euk. [Graphical view]
Gene3D	G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHER	PTHR11716. Phospholipase_A2. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA22_BUNCE

Accession

Primary (citable) accession number: Q8QFW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	June 1, 2002
Last modified:	November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program