PROTEIN SEQUENCE.
TISSUE=Venom;
DOI=10.1021/bi00363a020; PubMed=3530322 [NCBI, ExPASy, EBI, Israel, Japan]
Forst S., Weiss J., Blackburn P., Frangione B., Goni F., Elsbach P.;
"Amino acid sequence of a basic Agkistrodon halys blomhoffii phospholipase A2. Possible role of NH2-terminal lysines in action on phospholipids of Escherichia coli.";
Biochemistry 25:4309-4314(1986).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: In contrast to the pancreatic enzymes, the molecules of venom phospholipases A2 are dimers of identical chains; the monomers appear to be inactive.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.

Copyright

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Cross-references

Sequence databases
PIR	A00766; PSABA.
3D structure databases
ModBase	P04417.
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	P04417.
Phylogenomic databases
HOVERGEN	P04417; -.
Other
ProtoNet	P04417.
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`	`1 122`	`122`	`Phospholipase A2, basic.`	`PRO_0000161595`
`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`	`26 115`		`By similarity.`
`DISULFID`	`28 44`		`By similarity.`
`DISULFID`	`43 95`		`By similarity.`
`DISULFID`	`49 122`		`By similarity.`
`DISULFID`	`50 88`		`By similarity.`
`DISULFID`	`57 81`		`By similarity.`
`DISULFID`	`75 86`		`By similarity.`
`UNSURE`	`74 74`

Sequence information

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

Molecular weight: 13982 Da [This is the MW of the unprocessed precursor]

CRC64: EA2C5EE5EEF44488 [This is a checksum on the sequence]

        10         20         30         40         50         60 
HLLQFRKMIK KMTGKEPVIS YAFYGCYCGS GGRGKPKDAT DRCCFVHDCC YEKVTGCKPK 

        70         80         90        100        110        120 
WDDYTYSWKN GDIVCGGDDP CKKEICECDR AAAICFRDNL KTYKKRYMAY PDILCSSKSE 


KC

P04417 in FASTA format

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View entry in raw text format (no links)
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	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