[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3754861 [NCBI, ExPASy, EBI, Israel, Japan] Ohara O., Tamaki M., Nakamura E., Tsuruta Y., Fujii Y., Shin M., Teraoka H., Okamoto M.; "Dog and rat pancreatic phospholipases A2: complete amino acid sequences deduced from complementary DNAs."; J. Biochem. 99:733-739(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0167-4781(89)90141-3; PubMed=2909239 [NCBI, ExPASy, EBI, Israel, Japan] Sakata T., Nakamura E., Tsuruta Y., Tamaki M., Teraoka H., Tojo H., Ono T., Okamoto M.; "Presence of pancreatic-type phospholipase A2 mRNA in rat gastric mucosa and lung."; Biochim. Biophys. Acta 1007:124-126(1989).
[3]	PROTEIN SEQUENCE OF 23-54. PubMed=6501264 [NCBI, ExPASy, EBI, Israel, Japan] Ono T., Tojo H., Inoue K., Kagamiyama H., Yamano T., Okamoto M.; "Rat pancreatic phospholipase A2: purification, characterization, and N-terminal amino acid sequence."; J. Biochem. 96:785-792(1984).

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

D00036; BAA00024.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A92008; PSRT.

NP_113773.1; -.

3D structure databases

HSSP

P00593; 4BP2. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P04055.

Organism-specific databases

RGD

61949; Pla2g1b.

Gene expression databases

ArrayExpress

P04055; -.

GermOnline

ENSRNOG00000001153; Rattus norvegicus.

Ontologies

GO:0043498;	Molecular function: cell surface binding (inferred from direct assay from UniProtKB).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from direct assay from UniProtKB).
GO:0005102;	Molecular function: receptor binding (inferred from direct assay from UniProtKB).
GO:0032869;	Biological process: cellular response to insulin stimulus (inferred from sequence or structural similarity from UniProtKB).
GO:0006633;	Biological process: fatty acid biosynthetic process (inferred from direct assay from UniProtKB).
GO:0015758;	Biological process: glucose transport (inferred from sequence or structural similarity from UniProtKB).
GO:0045740;	Biological process: positive regulation of DNA replication (inferred from direct assay from UniProtKB).
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.

BLOCKS

P04055.

Genome annotation databases

Ensembl

ENSRNOG00000001153; Rattus norvegicus. [Contig view]

GeneID

29526; -.

KEGG

rno:29526; -.

Phylogenomic databases

HOVERGEN

P04055; -.

Other

ProtoNet

P04055.

UniRef

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

Keywords

Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 15`	`15`
`PROPEP`	`16 22`	`7`	`Activation peptide.`	`PRO_0000022747`
`CHAIN`	`23 146`	`124`	`Phospholipase A2.`	`PRO_0000022748`
`ACT_SITE`	`70 70`
`ACT_SITE`	`121 121`
`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: 16424 Da [This is the MW of the unprocessed precursor]

CRC64: 7EC4F7A491B913D0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLLLLAALL TAGVTAHSIS TRAVWQFRNM IKCTIPGSDP LREYNNYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DDLDRCCQTH DHCYNQAKKL ESCKFLIDNP YTNTYSYKCS GNVITCSDKN NDCESFICNC 

       130        140 
DRQAAICFSK VPYNKEYKDL DTKKHC

P04055 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