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

AY178051; AAO21118.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00609; 2NOT. [HSSP ENTRY / PDB]

SMR

P59359; 28-145.

ModBase

P59359.

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

P59359.

Phylogenomic databases

HOVERGEN

P59359; -.

Other

ProtoNet

P59359.

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_0000022785`
`CHAIN`	`28 145`	`118`	`Phospholipase A2 isozyme S2-22.`	`PRO_0000022786`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`121 121`		`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 99`		`By similarity.`
`DISULFID`	`54 144`		`By similarity.`
`DISULFID`	`56 72`		`By similarity.`
`DISULFID`	`71 127`		`By similarity.`
`DISULFID`	`78 120`		`By similarity.`
`DISULFID`	`88 113`		`By similarity.`
`DISULFID`	`106 118`		`By similarity.`

Sequence information

Length: 145 AA [This is the length of the unprocessed precursor]

Molecular weight: 16133 Da [This is the MW of the unprocessed precursor]

CRC64: D38F999D2C7B5C82 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAS DIPPQPLNLV QFSNMIQCAN HGRRPTSNYM DYGCYCGKGG 

        70         80         90        100        110        120 
SGTPVDELDR CCKIHDDCYG EAEKSQKCAP YWTWYTWKCG SDGPQCDDSK TGCQRFVCDC 

       130        140 
DATAAKCFAK APYNKENYNI KTRCQ

P59359 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