Reviewed, UniProtKB/Swiss-Prot P24644 (PA21B_MATBI)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme 1     EC=3.1.1.4 Alternative name(s):     Phospholipase A2 isozyme I     Phosphatidylcholine 2-acylhydrolase
Organism	Maticora bivirgata (Long-glanded 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
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-SubCell 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 – ›38	›38	Phospholipase A2 isozyme 1		PRO_0000161655
Experimental info
	Non-terminal residue	38	1

Sequences

	Sequence		Length	Mass (Da)
	P24644-1 [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.

Cross-references

Sequence databases
PIR	A39558.
3D structure databases
SMR	P24644. Positions 1-38.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P24644.
Family and domain databases
InterPro	IPR016090. Phospholipase_A2. 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. 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:	January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)