Reviewed, UniProtKB/Swiss-Prot P25072 (PA21B_MICFM)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme 1     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Micrurus fulvius microgalbineus (Mexican coral snake)
Taxonomic identifier	8636 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Micrurus

Protein attributes

Sequence length	12 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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.
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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – ›12	›12	Phospholipase A2 isozyme 1		PRO_0000161657
Experimental info
	Non-terminal residue	12	1

Sequences

	Sequence		Length	Mass (Da)
	P25072-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: CC21992A899F0339	FASTA	12	1,398
	10 SLLBFKBMIE ST

References

[1]

"Purification and characterization of a phospholipase A2 from the venom of the coral snake, Micrurus fulvius microgalbineus (Brown and Smith)." Possani L.D., Alagon A.C., Fletcher P.L. Jr., Varela M.J., Julia J.Z. Biochem. J. 179:603-606(1979) [PubMed: 475771] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P25072.
Enzyme and pathway databases
BRENDA	3.1.1.4. 294499.
Family and domain databases
InterPro	IPR013090. Phospholipase_A2_AS. [Graphical view]
PROSITE	PS00119. PA2_ASP. Partial match. PS00118. PA2_HIS. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21B_MICFM

Accession

Primary (citable) accession number: P25072

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)