NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
DOI=10.1016/S0041-0101(99)00165-8; PubMed=10669032 [NCBI, ExPASy, EBI, Israel, Japan]
Chuman Y., Nobuhisa I., Ogawa T., Deshimaru M., Chijiwa T., Tan N.-T., Fukumaki Y., Shimohigashi Y., Ducancel F., Boulain J.-C., Menez A., Ohno M.;
"Regional and accelerated molecular evolution in group I snake venom gland phospholipase A2 isozymes.";
Toxicon 38:449-462(2000).

[2]

PROTEIN SEQUENCE OF 28-146.
TISSUE=Venom;
PubMed=7460933 [NCBI, ExPASy, EBI, Israel, Japan]
Joubert F.J., Taljaard N.;
"Purification, some properties and amino-acid sequences of two phospholipases A (CM-II and CM-III) from Naja naja kaouthia venom.";
Eur. J. Biochem. 112:493-499(1980).

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.
TISSUE SPECIFICITY: Expressed by the venom gland.
TOXIC DOSE: LD₅₀ is 10 mg/kg by intravenous injection.
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

AB011388; BAA36403.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P15445; 1A3D. [HSSP ENTRY / PDB]

SMR

P00596; 28-146.

ModBase

P00596.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
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.

Phylogenomic databases

HOVERGEN

P00596; -.

Other

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 21`	`21`	`Potential.`
`PROPEP`	`22 27`	`6`		`PRO_0000022920`
`CHAIN`	`28 146`	`119`	`Phospholipase A2 isozyme 1.`	`PRO_0000022921`
`ACT_SITE`	`74 74`		`By similarity.`
`ACT_SITE`	`120 120`		`By similarity.`
`METAL`	`54 54`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`56 56`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`58 58`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`75 75`		`Calcium (By similarity).`
`DISULFID`	`38 98`		`By similarity.`
`DISULFID`	`53 145`		`By similarity.`
`DISULFID`	`55 71`		`By similarity.`
`DISULFID`	`70 126`		`By similarity.`
`DISULFID`	`77 119`		`By similarity.`
`DISULFID`	`87 112`		`By similarity.`
`DISULFID`	`105 117`		`By similarity.`
`CONFLICT`	`79 79`		`N -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`107 110`		`GDND -> NGNN (in Ref. 2; AA sequence).`

Sequence information

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

Molecular weight: 16271 Da [This is the MW of the unprocessed precursor]

CRC64: F3FBB7172A829588 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPAHLLILA AVCVSPLGAF SNRPMPLNLY QFKNMIQCTV PNRSWWDFAD YGCYCGRGGS 

        70         80         90        100        110        120 
GTPVDDLDRC CQVHDNCYNE AEKISRCWPY FKTYSYECSQ GTLTCKGDND ACAAAVCDCD 

       130        140 
RLAAICFAGA PYNNNNYNID LKARCQ

P00596 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