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

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A00761; PSBG2H.

3D structure databases

HSSP

P81458; 1VIP. [HSSP ENTRY / PDB]

ModBase

P00621.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from InterPro).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from InterPro).
GO:0006644;	Biological process: phospholipid metabolic process (inferred from electronic annotation from InterPro).
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.

ProtoNet

P00621.

Phylogenomic databases

HOVERGEN

P00621; -.

Other

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

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