[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; DOI=10.1093/nar/15.14.5892; PubMed=3615209 [NCBI, ExPASy, EBI, Israel, Japan] Guignery Frelat G., Ducancel F., Menez A., Boulain J.-C.; "Sequence of a cDNA encoding a snake venom phospholipase A2."; Nucleic Acids Res. 15:5892-5892(1987).

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 (By similarity).
SUBUNIT: In contrast to the pancreatic enzymes, the molecules of venom phospholipases A2 are dimers of identical chains; the monomers appear to be inactive.
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

EMBL

Y00377; CAA68449.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A27099; A27099.

3D structure databases

HSSP

P00608; 1AE7. [HSSP ENTRY / PDB]

SMR

P19000; 28-145.

ModBase

P19000.

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.

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

P19000.

Phylogenomic databases

HOVERGEN

P19000; -.

Other

ProtoNet

P19000.

UniRef

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

Keywords

Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 27`	`6`		`PRO_0000022886`
`CHAIN`	`28 145`	`118`	`Phospholipase A2 P'513.`	`PRO_0000022887`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`119 119`		`By similarity.`
`METAL`	`55 55`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`57 57`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`59 59`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`76 76`		`Calcium (By similarity).`
`DISULFID`	`38 98`		`By similarity.`
`DISULFID`	`54 144`		`By similarity.`
`DISULFID`	`56 72`		`By similarity.`
`DISULFID`	`71 125`		`By similarity.`
`DISULFID`	`78 118`		`By similarity.`
`DISULFID`	`87 111`		`By similarity.`
`DISULFID`	`105 116`		`By similarity.`

Sequence information

Length: 145 AA [This is the length of the unprocessed precursor]

Molecular weight: 16242 Da [This is the MW of the unprocessed precursor]

CRC64: C6C2A9B4EE653630 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYPAHLLLLL AVCVSLLGAS AIPPLPLNLA QFALVIKCAD KGKRPRWHYM DYGCYCGPGG 

        70         80         90        100        110        120 
SGTPVDELDR CCKTHDQCYA QAEKKGCYPK LTMYSYYCGG DGPYCNSKTE CQRFVCDCDV 

       130        140 
RAADCFARYP YNNKNYNINT SKRCK

P19000 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