[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; Tsai I.-H.; "Cloning and sequencing of an phospholipase A2 from Taiwan habu."; Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
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

EMBL

X77088; CAA54363.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S46979; S46979.

3D structure databases

HSSP

P51972; 1VAP. [HSSP ENTRY / PDB]

SMR

Q91506; 1-122.

ModBase

Q91506.

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

Q91506.

Phylogenomic databases

HOVERGEN

Q91506; -.

Other

ProtoNet

Q91506.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 122`	`122`	`Phospholipase A2 1.`	`PRO_0000161705`
`ACT_SITE`	`47 47`		`By similarity.`
`ACT_SITE`	`88 88`		`By similarity.`
`METAL`	`27 27`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`29 29`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`31 31`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`48 48`		`Calcium (By similarity).`
`DISULFID`	`26 115`		`By similarity.`
`DISULFID`	`28 44`		`By similarity.`
`DISULFID`	`43 94`		`By similarity.`
`DISULFID`	`49 122`		`By similarity.`
`DISULFID`	`50 87`		`By similarity.`
`DISULFID`	`57 81`		`By similarity.`
`DISULFID`	`75 85`		`By similarity.`

Sequence information

Length: 122 AA [This is the length of the unprocessed precursor]

Molecular weight: 13615 Da [This is the MW of the unprocessed precursor]

CRC64: CA62DAAE5D284626 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NLWQFENMIM KVAKKSGILS YSAYGCYCGW GGRGTPKDAT DRCCFVHDCC YGKVTGCNPK 

        70         80         90        100        110        120 
LGKYTYSSEN GDIICGGDGP CKEVCECDRA AAICFRDNLD TYDRKTYWKY PASNCQEDSE 


PC

Q91506 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