[1]	PROTEIN SEQUENCE. TISSUE=Venom; DOI=10.1007/BF01026040; PubMed=8489705 [NCBI, ExPASy, EBI, Israel, Japan] Welches W., Reardon I.M., Heinrikson R.L.; "An examination of structural interactions presumed to be of importance in the stabilization of phospholipase A2 dimers based upon comparative protein sequence analysis of a monomeric and dimeric enzyme from the venom of Agkistrodon p. piscivorus."; J. Protein Chem. 12:187-193(1993).
[2]	PROTEIN SEQUENCE OF 1-23, AND PALMITOYLATION AT LYS-7 AND LYS-10. TISSUE=Venom; PubMed=3403524 [NCBI, ExPASy, EBI, Israel, Japan] Cho W., Tomasselli A.G., Heinrikson R.L., Kezdy F.J.; "The chemical basis for interfacial activation of monomeric phospholipases A2. Autocatalytic derivatization of the enzyme by acyl transfer from substrate."; J. Biol. Chem. 263:11237-11241(1988).
[3]	CHARACTERIZATION. TISSUE=Venom; PubMed=6438084 [NCBI, ExPASy, EBI, Israel, Japan] Maraganore J.M., Merutka G., Cho W., Welches W., Kezdy F.J., Heinrikson R.L.; "A new class of phospholipases A2 with lysine in place of aspartate 49. Functional consequences for calcium and substrate binding."; J. Biol. Chem. 259:13839-13843(1984).
[4]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). TISSUE=Venom; DOI=10.1074/jbc.272.26.16152; PubMed=9013608 [NCBI, ExPASy, EBI, Israel, Japan] Han S.K., Yoon E.T., Scott D.L., Sigler P.B., Cho W.; "Structural aspects of interfacial adsorption. A crystallographic and site-directed mutagenesis study of the phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus."; J. Biol. Chem. 272:3573-3582(1997).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit.
SUBUNIT: Monomer or homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Acylation causes dimerization.
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

B53872; B53872.

3D structure databases

PDB

1VAP; X-ray; 1.60 A; A/B=1-123.

[ExPASy / RCSB / EBI]

PDBsum

1VAP; -.

ModBase

P51972.

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

P51972.

Phylogenomic databases

HOVERGEN

P51972; -.

Other

P51972; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 123`	`123`	`Phospholipase A2.`	`PRO_0000161605`
`ACT_SITE`	`47 47`		`By similarity.`
`ACT_SITE`	`89 89`		`By similarity.`
`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.`
`LIPID`	`7 7`		`N6-palmitoyl lysine.`
`LIPID`	`10 10`		`N6-palmitoyl lysine.`
`DISULFID`	`26 116`
`DISULFID`	`28 44`
`DISULFID`	`43 95`
`DISULFID`	`49 123`
`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 30`	`3`
`HELIX`	`39 52`	`14`
`TURN`	`59 61`	`3`
`STRAND`	`66 69`	`4`
`STRAND`	`72 75`	`4`
`HELIX`	`80 98`	`19`
`HELIX`	`100 102`	`3`
`HELIX`	`105 108`	`4`
`HELIX`	`113 115`	`3`

Sequence information

Length: 123 AA [This is the length of the unprocessed precursor]

Molecular weight: 13989 Da [This is the MW of the unprocessed precursor]

CRC64: C39986552D990D72 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLFQFEKLIK KMTGKSGMLW YSAYGCYCGW GGQGRPKDAT DRCCFVHDCC YGKVTGCNPK 

        70         80         90        100        110        120 
MDIYTYSVDN GNIVCGGTNP CKKQICECDR AAAICFRDNL KTYDSKTYWK YPKKNCKEES 


EPC

P51972 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