[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8344290 [NCBI, ExPASy, EBI, Israel, Japan] Ying Z., Tojo H., Nonaka Y., Okamoto M.; "Cloning and expression of phospholipase A2 from guinea pig gastric mucosa, its induction by carbachol and secretion in vivo."; Eur. J. Biochem. 215:91-97(1993).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the phospholipase A2 family.

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

D00740; BAA00640.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S34049; S34049.

3D structure databases

HSSP

P00592; 1L8S. [HSSP ENTRY / PDB]

SMR

P43434; 19-141.

ModBase

P43434.

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

P43434.

Phylogenomic databases

HOVERGEN

P43434; -.

Other

ProtoNet

P43434.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 15`	`15`	`By similarity.`
`PROPEP`	`16 22`	`7`	`Activation peptide.`	`PRO_0000022735`
`CHAIN`	`23 146`	`124`	`Phospholipase A2.`	`PRO_0000022736`
`ACT_SITE`	`70 70`		`By similarity.`
`ACT_SITE`	`121 121`		`By similarity.`
`METAL`	`50 50`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`52 52`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`54 54`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`71 71`		`Calcium (By similarity).`
`DISULFID`	`33 99`		`By similarity.`
`DISULFID`	`49 146`		`By similarity.`
`DISULFID`	`51 67`		`By similarity.`
`DISULFID`	`66 127`		`By similarity.`
`DISULFID`	`73 120`		`By similarity.`
`DISULFID`	`83 113`		`By similarity.`
`DISULFID`	`106 118`		`By similarity.`

Sequence information

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

Molecular weight: 16187 Da [This is the MW of the unprocessed precursor]

CRC64: 760DE6CD11E20E07 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLLVLAALL SVSAAAHIIT PRALWQFRDM IKCAIPGSRP YSEYNNYGCF CGLGGSGTPV 

        70         80         90        100        110        120 
DELDRCCEIH DACYTQAKHL ESCKSVIDNP YTNSYSFSCS GTNIICSSKN KECEEFICNC 

       130        140 
DRAAAICFSK APYNENNKNI NKKERC

P43434 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