NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
DOI=10.1016/j.toxicon.2005.12.004; PubMed=16458338 [NCBI, ExPASy, EBI, Israel, Japan]
Yanoshita R., Ogawa Y., Murayama N., Omori-Satoh T., Saguchi K., Higuchi S., Khow O., Chanhome L., Samejima Y., Sitprija V.;
"Molecular cloning of the major lethal toxins from two kraits (Bungarus flaviceps and Bungarus candidus).";
Toxicon 47:416-424(2006).

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).
SUBCELLULAR LOCATION: Secreted (By similarity).
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

AB158302; BAD06270.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P15445; 1A3D. [HSSP ENTRY / PDB]

ModBase

Q75S48.

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

Q75S48.

Phylogenomic databases

HOVERGEN

Q75S48; -.

Other

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 19`	`19`	`Potential.`
`PROPEP`	`20 27`	`8`	`By similarity.`	`PRO_0000271454`
`CHAIN`	`28 152`	`125`	`Phospholipase A2-1.`	`PRO_5000051030`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`126 126`		`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`	`38 104`		`By similarity.`
`DISULFID`	`54 151`		`By similarity.`
`DISULFID`	`56 72`		`By similarity.`
`DISULFID`	`71 132`		`By similarity.`
`DISULFID`	`78 125`		`By similarity.`
`DISULFID`	`88 118`		`By similarity.`
`DISULFID`	`111 123`		`By similarity.`

Sequence information

Length: 152 AA [This is the length of the unprocessed precursor]

Molecular weight: 16855 Da [This is the MW of the unprocessed precursor]

CRC64: 4E1FF5C59401F763 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPAYFLVLA AVCVSLLGAA NIPPQPLSFY RYTEMIQCTI RGSLTYLDYM DYGCYCGTGS 

        70         80         90        100        110        120 
RGTPVDELDR CCQTHDNCYA EAEEHPKCSS LVKSPYMNLY SYTCSGGTIT CNADNDECGA 

       130        140        150 
FICNCDRTAA LCFAKAPYNE ENKEIDISKR CQ

Q75S48 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