P0C932 (PA21_LACMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 LM-PLA2-I Alternative name(s): LM-PLA2 EC=3.1.1.4 Phosphatidylcholine 2-acylhydrolase
Organism	Lachesis muta muta (Bushmaster)
Taxonomic identifier	8753 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Lachesis

Protein attributes

Sequence length	50 AA.
Sequence status	Fragment.
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. This protein displays a potent enzymatic activity as measured by indirect hemolysis of red blood cells. Is neither lethal when injected into mice nor does it present anticoagulant activity. Displays a moderate inhibitory activity on the aggregation of platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, strongly inhibits platelet aggregation induced by high doses of collagen. Shows myotoxic activity, increases the plasma creatine-kinase activity and induces edema and myonecrosis of mouse skeletal muscles. Ref.1 Ref.2 Ref.3
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Myotoxin Toxin
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: 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
	Chain	1 – ›50	›50	Phospholipase A2 LM-PLA2-I		PRO_0000370688
Sites
	Active site	47	1	By similarity
	Metal binding	27	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	29	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	31	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	48	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	28 ↔ 44		By similarity
Experimental info
	Non-terminal residue	50	1

Sequences

	Sequence		Length	Mass (Da)
	P0C932 [UniParc]. Last modified May 5, 2009. Version 1. Checksum: 3CB009973459362B	FASTA	50	5,642
	10 20 30 40 50 HLLQFGDLID KIAGRSGFWY YGFYGCYCGL GGRGRPQDAT DRCCFVHDCC

References

[1]	"Mechanism of inhibitory action on platelet activation of a phospholipase A2 isolated from Lachesis muta (Bushmaster) snake venom." Fuly A.L., Machado O.L., Alves E.W., Carlini C.R. Thromb. Haemost. 78:1372-1380(1997) [PubMed: 9408022] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT. Tissue: Venom.
[2]	"Myotoxic activity of an acidic phospholipase A2 isolated from Lachesis muta (Bushmaster) snake venom." Fuly A.L., Calil-Elias S., Zingali R.B., Guimaraes J.A., Melo P.A. Toxicon 38:961-972(2000) [PubMed: 10728833] [Abstract] Cited for: FUNCTION. Tissue: Venom.
[3]	"Purification and characterization of a phospholipase A2 isoenzyme isolated from Lachesis muta snake venom." Fuly A.L., de Miranda A.L.P., Zingali R.B., Guimaraes J.A. Biochem. Pharmacol. 63:1589-1597(2002) [PubMed: 12007562] [Abstract] Cited for: FUNCTION. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. Partial match. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21_LACMU

Accession

Primary (citable) accession number: P0C932

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	October 19, 2011
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program