[1]	PROTEIN SEQUENCE. TISSUE=Venom; PubMed=1158892 [NCBI, ExPASy, EBI, Israel, Japan] Halpert J., Eaker D.; "Amino acid sequence of a presynaptic neurotoxin from the venom of Notechis scutatus scutatus (Australian tiger snake)."; J. Biol. Chem. 250:6990-6997(1975).
[2]	PROTEIN SEQUENCE (NOTEXIN-S). TISSUE=Venom; DOI=10.1016/0014-5793(90)80559-2; PubMed=2155818 [NCBI, ExPASy, EBI, Israel, Japan] Chwetzoff S., Mollier P., Bouet F., Rowan E.G., Harvey A.L., Menez A.; "On the purification of notexin. Isolation of a single amino acid variant from the venom of Notechis scutatus scutatus."; FEBS Lett. 261:226-230(1990).
[3]	ACTIVE SITE. DOI=10.1016/0014-5793(76)80174-3; PubMed=1245225 [NCBI, ExPASy, EBI, Israel, Japan] Halpert J., Eaker D., Karlsson E.; "The role of phospholipase activity in the action of a presynaptic neurotoxin from the venom of Notechis scutatus scutatus (Australian tiger snake)."; FEBS Lett. 61:72-76(1976).
[4]	INVOLVEMENT OF TRP-110 IN TOXICITY. PubMed=2583182 [NCBI, ExPASy, EBI, Israel, Japan] Mollier P., Chwetzoff S., Bouet F., Harvey A.L., Menez A.; "Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin."; Eur. J. Biochem. 185:263-270(1989).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/0014-5793(92)81238-H; PubMed=1568473 [NCBI, ExPASy, EBI, Israel, Japan] Westerlund B., Nordlund P., Uhlim U., Eaker D., Eklund H.; "The three-dimensional structure of notexin, a presynaptic neurotoxic phospholipase A2 at 2.0-A resolution."; FEBS Lett. 301:159-164(1992).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Acts presynaptically. Is directly toxic to skeletal muscle upon local application in vivo (dystrophic effect).
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
TOXIC DOSE: LD₅₀ is 0.025 mg/kg by intravenous injection.
MISCELLANEOUS: Activity and lethal neurotoxicity are lost upon modification with p-bromophenacyl bromide.
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

PIR

A00749; PSNOAT.
S08258; PSNOAS.

3D structure databases

PDB

1AE7; X-ray; 2.00 A; A=1-119.

[ExPASy / RCSB / EBI]

PDBsum

1AE7; -.

ModBase

P00608.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0042734;	Cellular component: presynaptic membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0007268;	Biological process: synaptic transmission (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

P00608; -.

Other

LinkHub

P00608; -.

UniRef

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

Keywords

3D-structure; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 119`	`119`	`Phospholipase A2.`	`PRO_0000161675`
`ACT_SITE`	`48 48`
`ACT_SITE`	`93 93`
`METAL`	`28 28`		`Calcium; via carbonyl oxygen.`
`METAL`	`30 30`		`Calcium; via carbonyl oxygen.`
`METAL`	`32 32`		`Calcium; via carbonyl oxygen.`
`METAL`	`49 49`		`Calcium.`
`DISULFID`	`11 71`
`DISULFID`	`27 118`
`DISULFID`	`29 45`
`DISULFID`	`44 99`
`DISULFID`	`51 92`
`DISULFID`	`60 85`
`DISULFID`	`78 90`
`VARIANT`	`16 16`	`1`	`K -> R (in variant S).`
`HELIX`	`2 12`	`11`
`TURN`	`13 15`	`3`
`HELIX`	`19 22`	`4`
`STRAND`	`23 25`	`3`
`TURN`	`26 28`	`3`
`STRAND`	`29 31`	`3`
`HELIX`	`40 57`	`18`
`STRAND`	`69 72`	`4`
`STRAND`	`75 78`	`4`
`STRAND`	`81 83`	`3`
`HELIX`	`84 102`	`19`
`HELIX`	`107 109`	`3`
`HELIX`	`114 117`	`4`

Sequence information

Length: 119 AA [This is the length of the unprocessed precursor]

Molecular weight: 13593 Da [This is the MW of the unprocessed precursor]

CRC64: 23D8BF780221D852 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLVQFSYLIQ CANHGKRPTW HYMDYGCYCG AGGSGTPVDE LDRCCKIHDD CYDEAGKKGC 

        70         80         90        100        110 
FPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ

P00608 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