PROTEIN SEQUENCE.
TISSUE=Venom;
DOI=10.1016/0041-0101(91)90103-X; PubMed=2048137 [NCBI, ExPASy, EBI, Israel, Japan]
Takasaki C., Yoshida H., Shimazu T., Teruuchi T., Toriba M., Tamiya N.;
"Studies on the venom components of the long-glanded coral snake, Maticora bivirgata.";
Toxicon 29:191-200(1991).

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.
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.
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

A39558; A39558.

3D structure databases

HSSP

P00598; 1POA. [HSSP ENTRY / PDB]

ModBase

P24644.

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:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from InterPro).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from InterPro).
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; PARTIAL.
PS00118; PA2_HIS; PARTIAL.

ProtoNet

P24644.

Phylogenomic databases

HOVERGEN

P24644; -.

Other

UniRef

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

Keywords

Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >38`	`>38`	`Phospholipase A2 isozyme 1.`	`PRO_0000161655`
`NON_TER`	`38 38`

Sequence information

Length: 38 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 4179 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 66CDEEE7034718A3 [This is a checksum on the sequence]

        10         20         30 
NLYQFGNMIQ CTIPKRLSWS SFVDYGCYCG KGGSGTPV

P24644 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