[1]	PROTEIN SEQUENCE. TISSUE=Venom; DOI=10.1016/0041-0101(87)90073-0; PubMed=3617077 [NCBI, ExPASy, EBI, Israel, Japan] Chen Y.-C., Maraganore J.M., Reardon I., Heinrikson R.L.; "Characterization of the structure and function of three phospholipases A2 from the venom of Agkistrodon halys pallas."; Toxicon 25:401-409(1987).
[2]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), ACTIVE SITE, METAL-BINDING SITES, AND DISULFIDE BONDS. TISSUE=Venom; DOI=10.1006/jmbi.1996.0054; PubMed=8636969 [NCBI, ExPASy, EBI, Israel, Japan] Wang X.-Q., Yang J., Gui L.-L., Lin Z.-J., Chen Y.-C., Zhou Y.-C.; "Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0-A resolution."; J. Mol. Biol. 255:669-676(1996).
[3]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), METAL-BINDING SITES, AND DISULFIDE BONDS. TISSUE=Venom; DOI=10.1016/S0041-0101(97)00169-4; PubMed=9663694 [NCBI, ExPASy, EBI, Israel, Japan] Zhao H., Tang L., Wang X., Zhou Y., Lin Z.; "Structure of a snake venom phospholipase A2 modified by p-bromo-phenacyl-bromide."; Toxicon 36:875-886(1998).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Like most other acidic phospholipases, this protein is not neurotoxic.
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.
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

A26535; A26535.

3D structure databases

PDB

1BK9; X-ray; 2.00 A; A=1-124.	[ExPASy / RCSB / EBI]
1PSJ; X-ray; 2.00 A; A=1-124.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BK9; -.
1PSJ; -.

ModBase

P14418.

Ontologies

GO:0005576;	Cellular component: extracellular region (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:0006644;	Biological process: phospholipid metabolic process (inferred from electronic annotation from InterPro).
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.

ProtoNet

P14418.

Phylogenomic databases

HOVERGEN

P14418; -.

Other

LinkHub

P14418; -.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 124`	`124`	`Phospholipase A2, acidic.`	`PRO_0000161597`
`ACT_SITE`	`47 47`
`ACT_SITE`	`89 89`
`METAL`	`27 27`		`Calcium; via carbonyl oxygen.`
`METAL`	`29 29`		`Calcium; via carbonyl oxygen.`
`METAL`	`31 31`		`Calcium; via carbonyl oxygen.`
`METAL`	`48 48`		`Calcium.`
`DISULFID`	`26 116`
`DISULFID`	`28 44`
`DISULFID`	`43 95`
`DISULFID`	`49 124`
`DISULFID`	`50 88`
`DISULFID`	`57 81`
`DISULFID`	`75 86`
`HELIX`	`2 13`	`12`
`HELIX`	`17 20`	`4`
`STRAND`	`21 24`	`4`
`TURN`	`25 27`	`3`
`STRAND`	`28 31`	`4`
`HELIX`	`39 52`	`14`
`TURN`	`59 61`	`3`
`STRAND`	`65 69`	`5`
`STRAND`	`72 78`	`7`
`HELIX`	`80 98`	`19`
`HELIX`	`99 102`	`4`
`HELIX`	`105 108`	`4`
`HELIX`	`113 115`	`3`
`HELIX`	`118 120`	`3`

Sequence information

Length: 124 AA [This is the length of the unprocessed precursor]

Molecular weight: 13974 Da [This is the MW of the unprocessed precursor]

CRC64: 34BE769D31A45D26 [This is a checksum on the sequence]

        10         20         30         40         50         60 
SLIQFETLIM KVAKKSGMFW YSNYGCYCGW GGQGRPQDAT DRCCFVHDCC YGKVTGCDPK 

        70         80         90        100        110        120 
MDVYSFSEEN GDIVCGGDDP CKKEICECDR AAAICFRDNL TLYNDKKYWA FGAKNCPQEE 


SEPC

P14418 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