Reviewed, UniProtKB/Swiss-Prot P00595 (PA21_HEMHA)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme DE-1     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Hemachatus haemachatus (Ringhals) (Sepedon haemachatus)
Taxonomic identifier	8626 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Hemachatus

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
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.
Toxic dose	LD50 is 8.6 mg/kg by intravenous injection.
Miscellaneous	Two forms of phospholipase A2 are found in Ringhals venom.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
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: 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 – 119	119	Phospholipase A2 isozyme DE-1		PRO_0000161649
Sites
	Active site	93	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
	Site	47	1	Activity and toxicity lost upon alkylation, Ca(2+) markedly slows inactivation Ref.2
Amino acid modifications
	Disulfide bond	11 ↔ 71		By similarity
	Disulfide bond	26 ↔ 118		By similarity
	Disulfide bond	28 ↔ 44		By similarity
	Disulfide bond	43 ↔ 99		By similarity
	Disulfide bond	50 ↔ 92		By similarity
	Disulfide bond	60 ↔ 85		By similarity
	Disulfide bond	78 ↔ 90		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00595-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 4DEDD044EFA97035	FASTA	119	13,519
	10 20 30 40 50 60 NLYQFKNMIK CTVPSRSWWH FANYGCYCGR GGSGTPVDDL DRCCQTHDNC YSDAEKISGC 70 80 90 100 110 RPYFKTYSYD CTKGKLTCKE GNNECAAFVC KCDRLAAICF AGAHYNDNNN YIDLARHCQ

References

[1]	"Hemachatus haemachatus (Ringhals) venom. Purification, some properties and amino-acid sequence of phospholipase A (fraction DE-I)." Joubert F.J. Eur. J. Biochem. 52:539-544(1975) [PubMed: 1236145] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.
[2]	"Chemical modification of the histidine residue in phospholipase A2 from the Hemachatus haemachatus snake venom." Yang C.C., King K. Toxicon 18:529-547(1980) [PubMed: 7222060] [Abstract] Cited for: ACTIVE SITE.

Cross-references

Sequence databases
PIR	PSRIA. A00738.
3D structure databases
HSSP	HSSP built from PDB template 1A3D based on UniProtKB P15445.
SMR	P00595. Positions 1-119.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00595.
Enzyme and pathway databases
BRENDA	3.1.1.4. 74541.
Family and domain databases
InterPro	IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. 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.
ProDom	PD000303. PhospholipaseA2. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00085. PA2c. 1 hit. [Graphical view]
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21_HEMHA

Accession

Primary (citable) accession number: P00595

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)