NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Liver, and Venom gland;
DOI=10.1016/0378-1119(96)00186-2; PubMed=8682315 [NCBI, ExPASy, EBI, Israel, Japan]
Nobuhisa I., Nakashima K., Deshimaru M., Ogawa T., Shimohigashi Y., Fukumaki Y., Sakaki Y., Hattori S., Kihara H., Ohno M.;
"Accelerated evolution of Trimeresurus okinavensis venom gland phospholipase A2 isozyme-encoding genes.";
Gene 172:267-272(1996).

[2]

PROTEIN SEQUENCE OF 17-139.
TISSUE=Venom;
PubMed=7275018 [NCBI, ExPASy, EBI, Israel, Japan]
Joubert F.J., Haylett T.;
"Snake venoms. Purification, some properties and amino acid sequence of a phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom.";
Hoppe-Seyler's Z. Physiol. Chem. 362:997-1006(1981).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Like most other acidic phospholipases, this protein is not neurotoxic.
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.
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

D49388; BAA08383.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D49390; BAA08385.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4874; PSTV.

3D structure databases

HSSP

P14418; 1BK9. [HSSP ENTRY / PDB]

SMR

P00625; 18-139.

ModBase

P00625.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
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.

Phylogenomic databases

HOVERGEN

P00625; -.

Other

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

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`
`CHAIN`	`17 139`	`123`	`Phospholipase A2 PLA2-01.`	`PRO_0000022966`
`ACT_SITE`	`63 63`		`By similarity.`
`ACT_SITE`	`105 105`		`By similarity.`
`METAL`	`43 43`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`45 45`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`47 47`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`64 64`		`Calcium (By similarity).`
`DISULFID`	`42 132`		`By similarity.`
`DISULFID`	`44 60`		`By similarity.`
`DISULFID`	`59 111`		`By similarity.`
`DISULFID`	`65 139`		`By similarity.`
`DISULFID`	`66 104`		`By similarity.`
`DISULFID`	`73 97`		`By similarity.`
`DISULFID`	`91 102`		`By similarity.`
`CONFLICT`	`39 41`		`Missing (in Ref. 1; BAA08385).`
`CONFLICT`	`83 83`		`S -> T (in Ref. 2; AA sequence).`
`CONFLICT`	`86 86`		`N -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`90 90`		`T -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`94 95`		`EN -> ND (in Ref. 2; AA sequence).`
`CONFLICT`	`117 117`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`120 120`		`N -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`135 136`		`ES -> SE (in Ref. 2; AA sequence).`

Sequence information

Length: 139 AA [This is the length of the unprocessed precursor]

Molecular weight: 15584 Da [This is the MW of the unprocessed precursor]

CRC64: E0FBB7B688925137 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRTLWIMAVL LLGVEGHLMQ FETLIMKIAG RSGVWWYGSY GCYCGAGGQG RPQDPSDRCC 

        70         80         90        100        110        120 
FVHDCCYGKV TGCNTKDEFY TYSEENGAIT CGGENPCLKE VCECDLAAAI CFRDNLDTYN 

       130 
SKKYWMFPAK NCLEESEPC

P00625 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