NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Zha H., Zhang Y.;
"cDNA cloning and characterization of phospholipase A2 from the snake Bungarus fasciatus.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [MRNA] OF 11-145, PROTEIN SEQUENCE OF 28-47, AND MASS SPECTROMETRY.
TISSUE=Venom, and Venom gland;
DOI=10.1111/j.1742-4658.2006.05598.x; PubMed=17166178 [NCBI, ExPASy, EBI, Israel, Japan]
Tsai I.-H., Tsai H.-Y., Saha A., Gomes A.;
"Sequences, geographic variations and molecular phylogeny of venom phospholipases and threefinger toxins of eastern India Bungarus fasciatus and kinetic analyses of its Pro31 phospholipases A2.";
FEBS J. 274:512-525(2007).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).
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.
MASS SPECTROMETRY: Mass=13003; Mass_error=1; Method=Electrospray; Range=18-135; Note=In KBf-2; Source=PubMed:17166178;.
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

DQ508412; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
AF387594; AAK62361.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q9DF52; 1FE5. [HSSP ENTRY / PDB]

ModBase

Q90WA8.

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

Q90WA8.

Phylogenomic databases

HOVERGEN

Q90WA8; -.

Other

ProtoNet

Q90WA8.

UniRef

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

Keywords

Calcium; Direct protein sequencing; 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`		`PRO_0000022831`
`CHAIN`	`28 145`	`118`	`Phospholipase A2 isozyme 2.`	`PRO_0000022832`
`ACT_SITE`	`73 73`		`By similarity.`
`ACT_SITE`	`119 119`		`By similarity.`
`METAL`	`53 53`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`55 55`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`56 56`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`74 74`		`Calcium (By similarity).`
`DISULFID`	`38 97`		`By similarity.`
`DISULFID`	`52 144`		`By similarity.`
`DISULFID`	`54 70`		`By similarity.`
`DISULFID`	`69 125`		`By similarity.`
`DISULFID`	`76 118`		`By similarity.`
`DISULFID`	`86 111`		`By similarity.`
`DISULFID`	`104 116`		`By similarity.`
`VARIANT`	`18 18`	`1`	`A -> G.`
`VARIANT`	`114 114`	`1`	`T -> N.`
`VARIANT`	`124 124`	`1`	`L -> I.`

Sequence information

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

Molecular weight: 15769 Da [This is the MW of the unprocessed precursor]

CRC64: 5599DA79109D0700 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPAHLLVLL AVCVSLLAAA NIPPQSLNLL QFKNMIECAG TRTWMAYVKY GCYCGPGGTG 

        70         80         90        100        110        120 
TPLDELDRCC QTHDQCYDNA KKFGNCIPYF KTYVYTCNKP DITCTGAKGS CGRTVCDCDR 

       130        140 
AAALCFAAAP YNLANFGINK ETHCQ

Q90WA8 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