[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; DOI=10.1006/bbrc.1994.1324; PubMed=7510963 [NCBI, ExPASy, EBI, Israel, Japan] Pan F.M., Yeh M.S., Chang W.C., Hung C.C., Chiou S.H.; "Sequence analysis and expression of phospholipase A2 from Taiwan cobra."; Biochem. Biophys. Res. Commun. 199:969-976(1994).
[2]	PROTEIN SEQUENCE OF 28-146. TISSUE=Venom; DOI=10.1016/0041-0101(81)90126-4; PubMed=7222082 [NCBI, ExPASy, EBI, Israel, Japan] Tsai I.-H., Wu S.-H., Lo T.-B.; "Complete amino acid sequence of a phospholipase A2 from the venom of Naja naja atra (Taiwan cobra)."; Toxicon 19:141-152(1981).
[3]	PROTEIN SEQUENCE OF 28-43, FUNCTION, AND MASS SPECTROMETRY. TISSUE=Venom; DOI=10.1016/j.toxicon.2008.01.006; PubMed=18281071 [NCBI, ExPASy, EBI, Israel, Japan] Huang L.-F., Zheng J.-B., Xu Y., Song H.-T., Yu C.-X.; "A snake venom phospholipase A(2) with high affinity for muscarinic acetylcholine receptors acts on guinea pig ileum."; Toxicon 51:1008-1016(2008).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=2274787 [NCBI, ExPASy, EBI, Israel, Japan] White S.P., Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B.; "Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue."; Science 250:1560-1563(1990).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=2274785 [NCBI, ExPASy, EBI, Israel, Japan] Scott D.L., White S.P., Otwinowski Z., Yuan W., Gelb M.H., Sigler P.B.; "Interfacial catalysis: the mechanism of phospholipase A2."; Science 250:1541-1546(1990).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In guinea-pig ileum, this protein produces an onset and dose-dependent contraction. Has a high affinity for muscarinic acetylcholine receptors mAChRs and has the ability to activate them.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
MASS SPECTROMETRY: Mass=13260; Method=Unknown; Range=28-146; Source=PubMed:18281071;.
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

X73225; CAA51694.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC2137; PSNJAF.

3D structure databases

PDB

1POA; X-ray; 1.50 A; A=28-145.	[ExPASy / RCSB / EBI]
1POB; X-ray; 2.00 A; A/B=28-145.	[ExPASy / RCSB / EBI]
2OSH; X-ray; 2.20 A; A=28-146.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1POA; -.
1POB; -.
2OSH; -.

ModBase

P00598.

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

P00598.

Phylogenomic databases

HOVERGEN

P00598; -.

Other

P00598; -.

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

Keywords

3D-structure; Acetylcholine receptor inhibitor; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 27`	`6`		`PRO_0000022916`
`CHAIN`	`28 146`	`119`	`Phospholipase A2 1.`	`PRO_0000022917`
`ACT_SITE`	`74 74`
`ACT_SITE`	`120 120`
`METAL`	`54 54`		`Calcium; via carbonyl oxygen.`
`METAL`	`56 56`		`Calcium; via carbonyl oxygen.`
`METAL`	`58 58`		`Calcium; via carbonyl oxygen.`
`METAL`	`75 75`		`Calcium.`
`DISULFID`	`38 98`
`DISULFID`	`53 145`
`DISULFID`	`55 71`
`DISULFID`	`70 126`
`DISULFID`	`77 119`
`DISULFID`	`87 112`
`DISULFID`	`105 117`
`CONFLICT`	`111 112`		`AC -> CA (in Ref. 2; AA sequence).`
`CONFLICT`	`134 136`		`NNN -> DND (in Ref. 2; AA sequence).`
`CONFLICT`	`140 140`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`146 146`		`Q -> QE (in Ref. 2; AA sequence).`
`HELIX`	`29 39`	`11`
`HELIX`	`45 48`	`4`
`TURN`	`52 54`	`3`
`STRAND`	`55 57`	`3`
`HELIX`	`66 81`	`16`
`TURN`	`89 91`	`3`
`STRAND`	`96 99`	`4`
`STRAND`	`102 105`	`4`
`HELIX`	`111 127`	`17`
`HELIX`	`134 136`	`3`
`HELIX`	`141 144`	`4`

Sequence information

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

Molecular weight: 16013 Da [This is the MW of the unprocessed precursor]

CRC64: 862EDF47654BFF93 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTPAHLLILA AVCVSPLGAS SNRPMPLNLY QFKNMIQCTV PSRSWWDFAD YGCYCGRGGS 

        70         80         90        100        110        120 
GTPVDDLDRC CQVHDNCYNE AEKISGCWPY FKTYSYECSQ GTLTCKGGNN ACAAAVCDCD 

       130        140 
RLAAICFAGA PYNNNNYNID LKARCQ

P00598 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