PROTEIN SEQUENCE, AND CHARACTERIZATION.
TISSUE=Venom;
DOI=10.1006/abbi.1999.1230; PubMed=10375395 [NCBI, ExPASy, EBI, Israel, Japan]
Serrano S.M.T., Reichl A.P., Mentele R., Auerswald E.A., Santoro M.L., Sampaio C.A.M., Camargo A.C.M., Assakura M.T.;
"A novel phospholipase A2, BJ-PLA2, from the venom of the snake Bothrops jararaca: purification, primary structure analysis, and its characterization as a platelet-aggregation-inhibiting factor.";
Arch. Biochem. Biophys. 367:26-32(1999).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits collagen- and ADP-induced platelet aggregation.
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

3D structure databases
HSSP	P14418; 1BK9. [HSSP ENTRY / PDB]
SMR	P81243; 2-124.
ModBase	P81243.
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	P81243.
Phylogenomic databases
HOVERGEN	P81243; -.
Other
ProtoNet	P81243.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Secreted.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 124`	`124`	`Phospholipase A2.`	`PRO_0000161621`
`ACT_SITE`	`47 47`		`By similarity.`
`ACT_SITE`	`89 89`		`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`	`26 117`		`By similarity.`
`DISULFID`	`28 44`		`By similarity.`
`DISULFID`	`43 97`		`By similarity.`
`DISULFID`	`49 124`		`By similarity.`
`DISULFID`	`50 90`		`By similarity.`
`DISULFID`	`57 83`		`By similarity.`
`DISULFID`	`77 88`		`By similarity.`

Sequence information

Length: 124 AA [This is the length of the unprocessed precursor]

Molecular weight: 14304 Da [This is the MW of the unprocessed precursor]

CRC64: 5A4E33EE7745E3EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
DLWQFGQMMN DVMREYVVFN YLYYGCYCGW GGIGKPRDAT DRCCFVHDCC YGKVTGCNPK 

        70         80         90        100        110        120 
TDSYTYTYSE ENGDVVCGGD DLCKKQICEC DRVAATCFRD NKDTYDTKYW LYGAKNCQEE 


SEPC

P81243 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