Reviewed, UniProtKB/Swiss-Prot P00596 (PA21_NAJKA)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme 1     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase     NnkPLA-I     CM-II
Organism	Naja kaouthia (Monocled cobra) (Naja siamensis)
Taxonomic identifier	8649 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Toxic dose	LD50 is 10 mg/kg by intravenous injection.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
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
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 27	6			PRO_0000022920
	Chain	28 – 146	119	Phospholipase A2 isozyme 1		PRO_0000022921
Sites
	Active site	74	1	By similarity
	Active site	120	1	By similarity
	Metal binding	54	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	56	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	58	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	75	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	38 ↔ 98		By similarity
	Disulfide bond	53 ↔ 145		By similarity
	Disulfide bond	55 ↔ 71		By similarity
	Disulfide bond	70 ↔ 126		By similarity
	Disulfide bond	77 ↔ 119		By similarity
	Disulfide bond	87 ↔ 112		By similarity
	Disulfide bond	105 ↔ 117		By similarity
Experimental info
	Sequence conflict	79	1	N → D AA sequence Ref.2
	Sequence conflict	107 – 110	4	GDND → NGNN AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00596-1 [UniParc]. Last modified November 1, 2002. Version 2. Checksum: F3FBB7172A829588	FASTA	146	16,271
	10 20 30 40 50 60 MNPAHLLILA AVCVSPLGAF SNRPMPLNLY QFKNMIQCTV PNRSWWDFAD YGCYCGRGGS 70 80 90 100 110 120 GTPVDDLDRC CQVHDNCYNE AEKISRCWPY FKTYSYECSQ GTLTCKGDND ACAAAVCDCD 130 140 RLAAICFAGA PYNNNNYNID LKARCQ

References

[1]	"Regional and accelerated molecular evolution in group I snake venom gland phospholipase A2 isozymes." Chuman Y., Nobuhisa I., Ogawa T., Deshimaru M., Chijiwa T., Tan N.-T., Fukumaki Y., Shimohigashi Y., Ducancel F., Boulain J.-C., Menez A., Ohno M. Toxicon 38:449-462(2000) [PubMed: 10669032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Purification, some properties and amino-acid sequences of two phospholipases A (CM-II and CM-III) from Naja naja kaouthia venom." Joubert F.J., Taljaard N. Eur. J. Biochem. 112:493-499(1980) [PubMed: 7460933] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-146. Tissue: Venom.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011388 mRNA. Translation: BAA36403.1.
3D structure databases
SMR	P00596. Positions 28-146.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00596.
Enzyme and pathway databases
BRENDA	3.1.1.4. 274888.
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.
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

PA21_NAJKA

Accession

Primary (citable) accession number: P00596
Secondary accession number(s): Q9PWS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 2002
Last modified:	November 24, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)