[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. TISSUE=Venom gland; PubMed=7777556 [NCBI, ExPASy, EBI, Israel, Japan] Nakashima K., Nobuhisa I., Deshimaru M., Nakai M., Ogawa T., Shimohigashi Y., Fukumaki Y., Hattori M., Sakaki Y., Hattori S., Ohno M.; "Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes."; Proc. Natl. Acad. Sci. U.S.A. 92:5605-5609(1995).
[2]	PROTEIN SEQUENCE OF 17-138. TISSUE=Venom; DOI=10.1016/0041-0101(91)90100-6; PubMed=2048135 [NCBI, ExPASy, EBI, Israel, Japan] Oda N., Nakamura H., Sakamoto S., Liu S.-Y., Kihara H., Chang C.-C., Ohno M.; "Amino acid sequence of a phospholipase A2 from the venom of Trimeresurus gramineus (green habu snake)."; Toxicon 29:157-166(1991).
[3]	PROTEIN SEQUENCE OF 17-54. TISSUE=Venom; PubMed=3448089 [NCBI, ExPASy, EBI, Israel, Japan] Oda N., Sakai H., Shieh T.C., Nakamura H., Sakamoto S., Kihara H., Chang C.-C., Ohno M.; "Purification and characterization of phospholipase A2 from Trimeresurus gramineus venom."; J. Biochem. 102:1441-1449(1987).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has high lipolytic activity.
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

D31774; BAA06552.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D31780; BAA06558.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39557; A39557.

3D structure databases

HSSP

P14418; 1M8R. [HSSP ENTRY / PDB]

SMR

P20476; 18-138.

ModBase

P20476.

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

P20476.

Phylogenomic databases

HOVERGEN

P20476; -.

Other

ProtoNet

P20476.

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`	`17 138`	`122`	`Phospholipase A2 isozyme 1.`	`PRO_0000022959`
`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`	`42 131`		`By similarity.`
`DISULFID`	`44 60`		`By similarity.`
`DISULFID`	`59 111`		`By similarity.`
`DISULFID`	`65 138`		`By similarity.`
`DISULFID`	`66 104`		`By similarity.`
`DISULFID`	`73 97`		`By similarity.`
`DISULFID`	`91 102`		`By similarity.`

Sequence information

Length: 138 AA [This is the length of the unprocessed precursor]

Molecular weight: 15519 Da [This is the MW of the unprocessed precursor]

CRC64: 1D1EF551CCB155ED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRTLWIMAVL LVGVEGHLMQ FETLIMKVAG RSGVWYYGSY GCFCGAGGQG RPQDASDRCC 

        70         80         90        100        110        120 
FVHDCCYGKV NGCDPKKDFY TYSEENGAIV CGGDDPCKKE ICECDKDAAI CFRDNKDTYD 

       130 
NKYWFFPAKN CQEESEPC

P20476 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