[1]	PROTEIN SEQUENCE. TISSUE=Venom; PubMed=1236145 [NCBI, ExPASy, EBI, Israel, Japan] Joubert F.J.; "Hemachatus haemachatus (Ringhals) venom. Purification, some properties and amino-acid sequence of phospholipase A (fraction DE-I)."; Eur. J. Biochem. 52:539-544(1975).
[2]	ACTIVE SITE. DOI=10.1016/0041-0101(80)90081-1; PubMed=7222060 [NCBI, ExPASy, EBI, Israel, Japan] Yang C.C., King K.; "Chemical modification of the histidine residue in phospholipase A2 from the Hemachatus haemachatus snake venom."; Toxicon 18:529-547(1980).

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.
SIMILARITY: Belongs to the phospholipase A2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases
PIR	A00738; PSRIA.
3D structure databases
HSSP	P15445; 1A3D. [HSSP ENTRY / PDB]
SMR	P00595; 1-119.
ModBase	P00595.
Family and domain databases
InterPro	IPR016090; Phospholipase_A2. IPR013090; Phospholipase_A2_AS. IPR001211; Phospholipase_A2_euk. Graphical view of domain structure.
Gene3D	G3DSA:1.20.90.10; Phospholipase_A2; 1.
PANTHER	PTHR11716; Phospholipase_A2; 1.
Pfam	PF00068; Phospholip_A2_1; 1. Pfam graphical view of domain structure.
PRINTS	PR00389; PHPHLIPASEA2.
ProDom	PD000303; PhospholipaseA2; 1. [Domain structure / List of seq. sharing at least 1 domain]
SMART	SM00085; PA2c; 1. SMART graphical view of domain structure.
PROSITE	PS00119; PA2_ASP; 1. PS00118; PA2_HIS; 1.
BLOCKS	P00595.
Phylogenomic databases
HOVERGEN	P00595; -.
Other
ProtoNet	P00595.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Secreted.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 119`	`119`	`Phospholipase A2 isozyme DE-1.`	`PRO_0000161649`
`ACT_SITE`	`93 93`		`By similarity.`
`METAL`	`27 27`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`29 29`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`31 31`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`48 48`		`Calcium (By similarity).`
`SITE`	`47 47`	`1`	`Activity and toxicity lost upon alkylation, Ca(2+) markedly slows inactivation.`
`DISULFID`	`11 71`		`By similarity.`
`DISULFID`	`26 118`		`By similarity.`
`DISULFID`	`28 44`		`By similarity.`
`DISULFID`	`43 99`		`By similarity.`
`DISULFID`	`50 92`		`By similarity.`
`DISULFID`	`60 85`		`By similarity.`
`DISULFID`	`78 90`		`By similarity.`

Sequence information

Length: 119 AA [This is the length of the unprocessed precursor]

Molecular weight: 13519 Da [This is the MW of the unprocessed precursor]

CRC64: 4DEDD044EFA97035 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLYQFKNMIK CTVPSRSWWH FANYGCYCGR GGSGTPVDDL DRCCQTHDNC YSDAEKISGC 

        70         80         90        100        110 
RPYFKTYSYD CTKGKLTCKE GNNECAAFVC KCDRLAAICF AGAHYNDNNN YIDLARHCQ

P00595 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools