NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
DOI=10.1006/abbi.1999.1672; PubMed=10700385 [NCBI, ExPASy, EBI, Israel, Japan]
Singh S.B., Armugam A., Kini R.M., Jeyaseelan K.;
"Phospholipase A(2) with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning.";
Arch. Biochem. Biophys. 375:289-303(2000).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits collagen-induced platelet aggregation (By similarity).
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Calcium (Probable).
SUBCELLULAR LOCATION: Secreted (By similarity).
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

AF184140; AAD56563.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00608; 1AE7. [HSSP ENTRY / PDB]

SMR

Q9PUH0; 28-146.

ModBase

Q9PUH0.

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:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

Q9PUH0.

Phylogenomic databases

HOVERGEN

Q9PUH0; -.

Other

UniRef

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

Keywords

Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal; Toxin.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`PROPEP`	`20 27`	`8`	`Potential.`	`PRO_0000022811`
`CHAIN`	`28 146`	`119`	`Phospholipase A2 isozyme S8-51.`	`PRO_0000022812`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`120 120`		`By similarity.`
`METAL`	`55 55`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`57 57`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`59 59`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`76 76`		`Calcium (By similarity).`
`DISULFID`	`38 98`		`By similarity.`
`DISULFID`	`54 145`		`By similarity.`
`DISULFID`	`56 72`		`By similarity.`
`DISULFID`	`71 126`		`By similarity.`
`DISULFID`	`78 119`		`By similarity.`
`DISULFID`	`87 112`		`By similarity.`
`DISULFID`	`105 117`		`By similarity.`

Sequence information

Length: 146 AA [This is the length of the unprocessed precursor]

Molecular weight: 16212 Da [This is the MW of the unprocessed precursor]

CRC64: B3D1EBF6E2134D04 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAA SIPPQPLNLV QFSYLIQCAN HGSRATWHYT DYGCYCGSGG 

        70         80         90        100        110        120 
SGTPVDELDR CCQTHDNCYG EAEKKGCYPK MSAYDYYCGG DGPYCRNIRK ECQRFVCDCD 

       130        140 
AIAAKCFARA PYNDANWDID TETRCQ

Q9PUH0 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