[1]	PROTEIN SEQUENCE. TISSUE=Venom; PubMed=1122292 [NCBI, ExPASy, EBI, Israel, Japan] Joubert F.J.; "The amino acid sequence of phospholipase A, fractions DE-I and DE-II."; Biochim. Biophys. Acta 379:345-359(1975).
[2]	DISULFIDE BONDS. PubMed=1122290 [NCBI, ExPASy, EBI, Israel, Japan] Joubert F.J., van der Walt S.J.; "Naja melanoleuca (forest cobra) venom. Purification and some properties of phospholipases A."; Biochim. Biophys. Acta 379:317-328(1975).

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

A00741; PSNJ1W.

3D structure databases

PDB

1OO1; Model; -; A=1-118.

[ExPASy / RCSB / EBI]

1OO1; -.

P00599; 1-118.

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

P00599.

Phylogenomic databases

HOVERGEN

P00599; -.

Other

ProtoNet

P00599.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Secreted.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 118`	`118`	`Phospholipase A2 isozyme DE-I.`	`PRO_0000161663`
`ACT_SITE`	`47 47`		`By similarity.`
`ACT_SITE`	`92 92`		`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 72`		`By similarity.`
`DISULFID`	`26 117`		`By similarity.`
`DISULFID`	`28 44`		`By similarity.`
`DISULFID`	`43 98`		`By similarity.`
`DISULFID`	`50 91`		`By similarity.`
`DISULFID`	`60 84`		`By similarity.`
`DISULFID`	`78 89`		`By similarity.`
`HELIX`	`2 12`	`11`
`HELIX`	`18 22`	`5`
`TURN`	`25 27`	`3`
`STRAND`	`28 30`	`3`
`HELIX`	`39 55`	`17`
`TURN`	`62 64`	`3`
`STRAND`	`69 71`	`3`
`STRAND`	`76 78`	`3`
`HELIX`	`83 101`	`19`
`HELIX`	`106 108`	`3`
`HELIX`	`113 116`	`4`

Sequence information

Length: 118 AA [This is the length of the unprocessed precursor]

Molecular weight: 13473 Da [This is the MW of the unprocessed precursor]

CRC64: 0B2792570FF5D94D [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLYQFKNMIH CTVPNRPWWH FANYGCYCGR GGKGTPVDDL DRCCQIHDKC YDEAEKISGC 

        70         80         90        100        110 
WPYIKTYTYE SCQGTLTCKD GGKCAASVCD CDRVAANCFA RATYNDKNYN IDFNARCQ

P00599 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