P24644 (PA21B_MATBI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 isozyme 1 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase Phospholipase A2 isozyme I
Organism	Maticora bivirgata (Blue Malaysian coral snake) (Calliophis bivirgata)
Taxonomic identifier	8633 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Maticora

Protein attributes

Sequence length	38 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. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Acts presynaptically.
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.
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 Neurotoxin Presynaptic neurotoxin Toxin
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – ›38	›38	Phospholipase A2 isozyme 1		PRO_0000161655
Sites
	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
Experimental info
	Non-terminal residue	38	1

Sequences

	Sequence		Length	Mass (Da)
	P24644 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 66CDEEE7034718A3	FASTA	38	4,179
	10 20 30 NLYQFGNMIQ CTIPKRLSWS SFVDYGCYCG KGGSGTPV

References

[1]	"Studies on the venom components of the long-glanded coral snake, Maticora bivirgata." Takasaki C., Yoshida H., Shimazu T., Teruuchi T., Toriba M., Tamiya N. Toxicon 29:191-200(1991) [PubMed: 2048137] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	A39558.
3D structure databases
ProteinModelPortal	P24644.
SMR	P24644. Positions 1-38.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR016090. PLipase_A2. 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. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21B_MATBI

Accession

Primary (citable) accession number: P24644

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	November 16, 2011
This is version 68 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