P21792 (PA23_MICNI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 3 Short name=svPLA2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase
Organism	Micrurus nigrocinctus (Central American coral snake) (Gargantilla)
Taxonomic identifier	8635 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Micrurus

Protein attributes

Sequence length	28 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 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 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 Lipid metabolism
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
Cellular_component	other organism presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	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 – ›28	›28	Phospholipase A2 3		PRO_0000161660
Experimental info
	Non-terminal residue	28	1

Sequences

	Sequence		Length	Mass (Da)
	P21792 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 315FB012F69098B1	FASTA	28	3,394
	10 20 NLYQFKNMIK CTNTRMWWSF TNAGCYDG

References

[1]	"Isolation and characterization of three toxic phospholipases from the venom of the coral snake Micrurus nigrocinctus." Mochca-Morales J., Martin B.M., Zamudio F.Z., Possani L.D. Toxicon 28:616-617(1990) Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

Sequence databases
PIR	C35948.
3D structure databases
ProteinModelPortal	P21792.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR016090. PLipase_A2_dom. [Graphical view]
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PROSITE	PS00119. PA2_ASP. Partial match. PS00118. PA2_HIS. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA23_MICNI

Accession

Primary (citable) accession number: P21792

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 70 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