PROTEIN SEQUENCE.
TISSUE=Venom;
DOI=10.1006/abbi.1998.0685; PubMed=9637731 [NCBI, ExPASy, EBI, Israel, Japan]
Chow G., Subburaju S., Kini R.M.;
"Purification, characterization, and amino acid sequence determination of acanthins, potent inhibitors of platelet aggregation from Acanthophis antarcticus (common death adder) venom.";
Arch. Biochem. Biophys. 354:232-238(1998).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Exhibits antiplatelet activity.
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

3D structure databases

HSSP

P00609; 2NOT. [HSSP ENTRY / PDB]

ModBase

P81237.

Ontologies

GO:0005576;	Cellular component: extracellular region (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; 1.
PS00118; PA2_HIS; 1.

Phylogenomic databases

HOVERGEN

P81237; -.

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`	`1 118`	`118`	`Phospholipase A2.`	`PRO_0000161592`
`ACT_SITE`	`48 48`		`By similarity.`
`ACT_SITE`	`92 92`		`By similarity.`
`METAL`	`28 28`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`30 30`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`32 32`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`49 49`		`Calcium (By similarity).`
`DISULFID`	`11 71`		`By similarity.`
`DISULFID`	`27 117`		`By similarity.`
`DISULFID`	`29 45`		`By similarity.`
`DISULFID`	`44 98`		`By similarity.`
`DISULFID`	`51 91`		`By similarity.`
`DISULFID`	`60 84`		`By similarity.`
`DISULFID`	`78 89`		`By similarity.`

Sequence information

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

Molecular weight: 12884 Da [This is the MW of the unprocessed precursor]

CRC64: E1477D186C06B3EB [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLYQFGGMIQ CANKGARSWL SYVNYGCYCG WGGSGTPVDE LDRCCQIHDN CYGEAEKKRC 

        70         80         90        100        110 
GPKMTLYSWE CANDVPVCNS KSACEGFVCD CDAAAAKCFA KAPYNKNNIG IGSKTRCQ

P81237 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