Reviewed, UniProtKB/Swiss-Prot P00621 (PA22_BITNA)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme CM-II     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Bitis nasicornis (Rhinoceros adder) (Rhinoceros viper)
Taxonomic identifier	8695 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Bitis

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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.
Post-translational modification	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.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 119	119	Phospholipase A2 isozyme CM-II		PRO_0000161616
Sites
	Active site	45	1	By similarity
	Active site	87	1	By similarity
	Metal binding	25	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	27	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	29	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	46	1	Calcium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00621-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: E625A8F304770181	FASTA	119	13,665
	10 20 30 40 50 60 DLTQFGNMIN KMGQSVFDYI YYGCYCGWGG QGKPRDATDR CCFVHDCCYG KMGTYDTKWT 70 80 90 100 110 SYKYEFQDGD IICGDKDPQK KELCECDRVA AICFANSRNT YNSKYFGYSS SKCTETEQC

References

[1]

"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." Joubert F.J., Townshend G.S., Botes D.P. Hoppe-Seyler's Z. Physiol. Chem. 364:1717-1726(1983) [PubMed: 6667925] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

Sequence databases
PIR	PSBG2H. A00761.
3D structure databases
HSSP	HSSP built from PDB template 1VIP based on UniProtKB P81458.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00621.
Enzyme and pathway databases
BRENDA	3.1.1.4. 279506.
Family and domain databases
InterPro	IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_A2_euk. [Graphical view]
Gene3D	G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHER	PTHR11716. Phospholipase_A2. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
ProDom	PD000303. PhospholipaseA2. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00085. PA2c. 1 hit. [Graphical view]
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA22_BITNA

Accession

Primary (citable) accession number: P00621

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)