[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 131-158. DOI=10.1016/j.cbpb.2005.10.001; PubMed=16275035 [NCBI, ExPASy, EBI, Israel, Japan] Ota E., Nagai H., Nagashima Y., Shiomi K.; "Molecular cloning of two toxic phospholipases A2 from the crown-of-thorns starfish Acanthaster planci venom."; Comp. Biochem. Physiol. 143B:54-60(2006).
[2]	PROTEIN SEQUENCE OF 24-85, AND FUNCTION. TISSUE=Spine; DOI=10.1016/S0041-0101(97)00085-8; PubMed=9643471 [NCBI, ExPASy, EBI, Israel, Japan] Shiomi K.A., Kazama A., Shimakura K., Nagashima Y.; "Purification and properties of phospholipases A2 from the crown-of-thorns starfish (Acanthaster planci) venom."; Toxicon 36:589-599(1998).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has hemorrhagic and capillary permeability-increasing activities and hence is considered to be deeply involved in the local inflammation. Shows hemolytic activity only in the presence of phosphatidylcholine (PC).
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: Monomer.
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

EMBL

AB211368; BAE46766.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q3C2C1.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0019835;	Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0019836;	Biological process: hemolysis by symbiont of host red blood cells (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
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; FALSE_NEG.
PS00118; PA2_HIS; 1.

Other

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

Keywords

Calcium; Cytolysis; Direct protein sequencing; Hemolysis; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal; Toxin.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`PROPEP`	`17 23`	`7`		`PRO_0000272035`
`CHAIN`	`24 158`	`135`	`Phospholipase A2 AP-PLA2-II.`	`PRO_0000272036`
`ACT_SITE`	`72 72`		`By similarity.`
`ACT_SITE`	`132 132`		`By similarity.`
`METAL`	`54 54`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`56 56`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`73 73`		`Calcium (By similarity).`
`DISULFID`	`51 158`		`By similarity.`
`DISULFID`	`53 69`		`By similarity.`
`DISULFID`	`68 138`		`By similarity.`
`DISULFID`	`75 131`		`By similarity.`
`DISULFID`	`85 124`		`By similarity.`
`DISULFID`	`109 129`		`By similarity.`
`CONFLICT`	`30 30`		`K -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`65 65`		`T -> L (in Ref. 2; AA sequence).`

Sequence information

Length: 158 AA [This is the length of the unprocessed precursor]

Molecular weight: 17490 Da [This is the MW of the unprocessed precursor]

CRC64: A013B58205747C22 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTFLILAMA VALAKAQSTD EITNLVQFGK LVMCLGNIGY TEGLEYDGYG CFCGKGGKGT 

        70         80         90        100        110        120 
PVDATDRCCE VHDNCYGQAV EEGKCWSVET YGTTYWYDQS TSGSCSIRCW EEGDYNSLVP 

       130        140        150 
RKACKAAICE CDRKAAQCFA DNRPTFNRKY LNYAKDTC

Q3C2C1 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