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.
PTM: This enzyme lacks one of the seven disulfide bonds found in similar PA2 proteins.
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

AF184142; AAD56409.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P80966; 1GP7. [HSSP ENTRY / PDB]

ModBase

Q9PUG8.

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; FALSE_NEG.

BLOCKS

Q9PUG8.

Phylogenomic databases

HOVERGEN

Q9PUG8; -.

Other

ProtoNet

Q9PUG8.

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_0000022815`
`CHAIN`	`28 152`	`125`	`Phospholipase A2 isozyme S16-19.`	`PRO_0000022816`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`126 126`		`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`	`38 104`		`By similarity.`
`DISULFID`	`54 151`		`By similarity.`
`DISULFID`	`71 132`		`By similarity.`
`DISULFID`	`78 125`		`By similarity.`
`DISULFID`	`88 118`		`By similarity.`
`DISULFID`	`111 123`		`By similarity.`

Sequence information

Length: 152 AA [This is the length of the unprocessed precursor]

Molecular weight: 16690 Da [This is the MW of the unprocessed precursor]

CRC64: 5C5E4EE5C4C33FDD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAS NIPLPSLDFE QFGKMIQCTI PCEESCLAYM DYGCYCGPGG 

        70         80         90        100        110        120 
SGTPLDELDR CRQTHDNCYA EAGKLPACKA MLSEPYNDTY SYGCIERQLT CNDDNDECKA 

       130        140        150 
FICNCDRAAV ICFSGAPYND SNYDIGTIEH CK

Q9PUG8 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