[1]	PROTEIN SEQUENCE. TISSUE=Venom; Ovchinnikov Y.A., Miroshnikov A.I., Nazimov I.V., Apsalaon U.R., Soldatova L.N.; "Complete amino acid sequence of phospholipase A2 (isozyme E3) from the venom of middle Asian cobra Naja naja oxiana."; Bioorg. Khim. 5:805-813(1979).

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.
SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.

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

JN0403; JN0403.

3D structure databases

HSSP

P15445; 1A3D. [HSSP ENTRY / PDB]

SMR

P25498; 1-119.

ModBase

P25498.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from InterPro).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from InterPro).
GO:0006644;	Biological process: phospholipid metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

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.

Phylogenomic databases

HOVERGEN

P25498; -.

Other

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 E.`	`PRO_0000161670`
`ACT_SITE`	`47 47`		`By similarity.`
`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).`
`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: 13229 Da [This is the MW of the unprocessed precursor]

CRC64: CC856D62685AA172 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLYQFKNMIK CTVPSRSWLD FANYGCYCGR GGSGTPVDDL DRCCQIHDNC YNEAGKISGC 

        70         80         90        100        110 
WPYFKTYSYE CSQGTLTCKG DNNSCAASVC DCDRLAAICF AGAPYNNDNY NINLKARCQ

P25498 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