Reviewed, UniProtKB/Swiss-Prot P04056 (PA21B_PSEAU)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme PA-11     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Pseudechis australis (Mulga snake) (King brown snake)
Taxonomic identifier	8670 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Pseudechis

Protein attributes

Sequence length	118 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Toxic dose	LD50 is 0.24 mg/kg by intravenous injection.
Miscellaneous	There are many protein components with phospholipase A2 activity in the Mulga snake venom and some of them are myotoxic.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 118	118	Phospholipase A2 isozyme PA-11		PRO_0000161686
Sites
	Active site	48	1	By similarity
	Active site	92	1	By similarity
	Metal binding	28	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	30	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	32	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	49	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	11 ↔ 71		By similarity
	Disulfide bond	27 ↔ 117		By similarity
	Disulfide bond	29 ↔ 45		By similarity
	Disulfide bond	44 ↔ 98		By similarity
	Disulfide bond	51 ↔ 91		By similarity
	Disulfide bond	60 ↔ 84		By similarity
	Disulfide bond	78 ↔ 89		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P04056-1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: F7C90529BB12D5A1	FASTA	118	12,966
	10 20 30 40 50 60 NLIQFGNMIQ CANKGSRPSL DYADYGCYCG WGGSGTPVDE LDRCCQVHDN CYEQAGKKGC 70 80 90 100 110 FPKLTLYSWK CTGNVPTCNS KPGCKSFVCA CDAAAAKCFA KAPYKKENYN IDTKKRCK

References

[1]	"Amino acid sequences of phospholipases A2 from the venom of an Australian elapid snake (king brown snake, Pseudechis australis)." Nishida S., Terashima M., Tamiya N. Toxicon 23:87-104(1985) [PubMed: 3887651] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

Sequence databases
PIR	PSSNK1. A00747.
3D structure databases
SMR	P04056. Positions 1-118.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P04056.
Enzyme and pathway databases
BRENDA	3.1.1.4. 276288.
Family and domain databases
InterPro	IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_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]
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21B_PSEAU

Accession

Primary (citable) accession number: P04056

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	January 19, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)