[1]	PROTEIN SEQUENCE. STRAIN=Bulgarian; TISSUE=Venom; PubMed=3606821 [NCBI, ExPASy, EBI, Israel, Japan] Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G.; "Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes)."; Biol. Chem. Hoppe-Seyler 368:343-352(1987).
[2]	CRYSTALLIZATION. TISSUE=Venom; DOI=10.1006/jmbi.1993.1109; PubMed=8445639 [NCBI, ExPASy, EBI, Israel, Japan] Devedjiev Y., Atanasov B., Mancheva I., Aleksiev B.; "Crystals of phospholipase A2 inhibitor. The non-toxic component of vipoxin from the venom of Bulgarian viper (Vipera ammodytes)."; J. Mol. Biol. 229:1147-1149(1993).
[3]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). TISSUE=Venom; DOI=10.1006/jmbi.1993.1297; PubMed=8510159 [NCBI, ExPASy, EBI, Israel, Japan] Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B., Singh T.P.; "Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor."; J. Mol. Biol. 231:498-500(1993).
[4]	X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS). DOI=10.1016/S0014-5793(97)00853-3; PubMed=9276469 [NCBI, ExPASy, EBI, Israel, Japan] Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B., Genov N., Willingmann P., Weber W., Singh T.P., Betzel C.; "Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution."; FEBS Lett. 412:573-577(1997).
[5]	X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). DOI=10.1107/S0907444901013543; PubMed=11679719 [NCBI, ExPASy, EBI, Israel, Japan] Banumathi S., Rajashankar K.R., Notzel C., Aleksiev B., Singh T.P., Genov N., Betzel C.; "Structure of the neurotoxic complex vipoxin at 1.4 A resolution."; Acta Crystallogr. D 57:1552-1559(2001).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
FUNCTION: The vipoxin complex show postsynaptic neurotoxicity, while the isolated phospholipase A2 is a presynaptic neurotoxin.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: The main toxin of this snake venom is vipoxin, a complex of a toxic basic protein (B chain) having phospholipase A2 activity and a nontoxic acidic protein (A chain) functioning as its inhibitor. Without the inhibitor, the basic protein becomes unstable and within 12-14 days loses its enzymatic activity.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
MISCELLANEOUS: The supposed calcium binding region close to Asp-48 of the basic phospholipase A2 is blocked by the side chain of Lys-60 of its inhibitor.
SIMILARITY: Belongs to the phospholipase A2 family. Group II 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

A29290; A29290.

3D structure databases

PDB

1AOK; X-ray; 2.00 A; B=1-122.	[ExPASy / RCSB / EBI]
1JLT; X-ray; 1.40 A; B=1-122.	[ExPASy / RCSB / EBI]
1RGB; X-ray; 3.30 A; A/B/K/L=1-122.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AOK; -.
1JLT; -.
1RGB; -.

ModBase

P14420.

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

P14420.

Phylogenomic databases

HOVERGEN

P14420; -.

Other

P14420; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 122`	`122`	`Phospholipase A2.`	`PRO_0000161712`
`ACT_SITE`	`47 47`		`By similarity.`
`ACT_SITE`	`89 89`		`By similarity.`
`METAL`	`27 27`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`29 29`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`31 31`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`48 48`		`Calcium (By similarity).`
`DISULFID`	`26 115`
`DISULFID`	`28 44`
`DISULFID`	`43 95`
`DISULFID`	`49 122`
`DISULFID`	`50 88`
`DISULFID`	`57 81`
`DISULFID`	`75 86`
`HELIX`	`2 13`	`12`
`HELIX`	`17 21`	`5`
`STRAND`	`22 24`	`3`
`TURN`	`25 27`	`3`
`STRAND`	`28 30`	`3`
`HELIX`	`39 52`	`14`
`TURN`	`59 61`	`3`
`STRAND`	`66 69`	`4`
`STRAND`	`72 75`	`4`
`HELIX`	`81 98`	`18`
`HELIX`	`100 102`	`3`
`HELIX`	`105 107`	`3`
`HELIX`	`112 115`	`4`

Sequence information

Length: 122 AA [This is the length of the unprocessed precursor]

Molecular weight: 13828 Da [This is the MW of the unprocessed precursor]

CRC64: 94438F9F1285FC7D [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLFQFAKMIN GKLGAFSVWN YISYGCYCGW GGQGTPKDAT DRCCFVHDCC YGRVRGCNPK 

        70         80         90        100        110        120 
LAIYSYSFKK GNIVCGKNNG CLRDICECDR VAANCFHQNK NTYNKNYKFL SSSRCRQTSE 


QC

P14420 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