PROTEIN SEQUENCE.
TISSUE=Venom;
PubMed=6667925 [NCBI, ExPASy, EBI, Israel, Japan]
Joubert F.J., Townshend G.S., Botes D.P.;
"Snake Venoms. Purification, some properties of two phospholipases A2 (CM-I and CM-II) and the amino-acid sequence of CM-II and Bitis nasicornis (horned adder) venom.";
Hoppe-Seyler's Z. Physiol. Chem. 364:1717-1726(1983).

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).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Six disulfide bonds are present.
MISCELLANEOUS: Two very similar relatively nontoxic phospholipases were isolated from the venom, CM-II (shown here) and CM-I. The amino acid composition of CM-I differed from that of CM-II in having 1 more Thr and Ala and one fewer Ser and Lys.
SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.

Copyright

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Cross-references

Sequence databases
PIR	A00761; PSBG2H.
3D structure databases
HSSP	P81458; 1VIP. [HSSP ENTRY / PDB]
ModBase	P00621.
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	P00621.
Phylogenomic databases
HOVERGEN	P00621; -.
Other
ProtoNet	P00621.
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`	`1 119`	`119`	`Phospholipase A2 isozyme CM-II.`	`PRO_0000161616`
`ACT_SITE`	`45 45`		`By similarity.`
`ACT_SITE`	`87 87`		`By similarity.`
`METAL`	`25 25`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`27 27`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`29 29`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`46 46`		`Calcium (By similarity).`

Sequence information

Length: 119 AA [This is the length of the unprocessed precursor]

Molecular weight: 13665 Da [This is the MW of the unprocessed precursor]

CRC64: E625A8F304770181 [This is a checksum on the sequence]

        10         20         30         40         50         60 
DLTQFGNMIN KMGQSVFDYI YYGCYCGWGG QGKPRDATDR CCFVHDCCYG KMGTYDTKWT 

        70         80         90        100        110 
SYKYEFQDGD IICGDKDPQK KELCECDRVA AICFANSRNT YNSKYFGYSS SKCTETEQC

P00621 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