Reviewed, UniProtKB/Swiss-Prot Q9DF52 (PA2K_BUNCE)

Names and origin

Protein names	Recommended name:     Phospholipase A2 KPA2     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Bungarus caeruleus (Indian krait)
Taxonomic identifier	132961 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	145 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. The protein shows anticoagulant and neurotoxic activities.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
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 Neurotoxin Presynaptic neurotoxin Toxin
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro synaptic transmission Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 – 19

19

Potential

Propeptide

20 – 27

8

By similarity

PRO_0000022827

Chain

28 – 145

118

Phospholipase A2 KPA2

PRO_0000022828

Sites

Active site

50

1

Active site

73

1

Active site

119

1

Metal binding

53

1

Calcium; via carbonyl oxygen By similarity

Metal binding

55

1

Calcium; via carbonyl oxygen By similarity

Metal binding

57

1

Calcium; via carbonyl oxygen By similarity

Metal binding

74

1

Calcium By similarity

Amino acid modifications

Disulfide bond

38 ↔ 97

Disulfide bond

52 ↔ 144

Disulfide bond

54 ↔ 70

Disulfide bond

69 ↔ 125

Disulfide bond

76 ↔ 118

Disulfide bond

86 ↔ 111

Disulfide bond

104 ↔ 116

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

145

Helix Strand Turn

Details...

Helix

29 – 39

11

Helix

44 – 47

4

Turn

51 – 53

3

Beta strand

54 – 57

4

Helix

65 – 80

16

Turn

88 – 90

3

Beta strand

95 – 98

4

Beta strand

101 – 104

4

Helix

110 – 128

19

Helix

133 – 135

3

Sequences

	Sequence		Length	Mass (Da)
	Q9DF52-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4CE49BD226AF3317	FASTA	145	15,765
	10 20 30 40 50 60 MYPAHLLVLV AVCVSLLGAA NIPPQPLNLI QFKNMIQCAG TRPWTAYVNY GCYCGKGGSG 70 80 90 100 110 120 TPVDELDRCC YTHDNCYNEA EKIPGCNPNI KTYSYTCTEP NLTCTDTADT CARFLCDCDR 130 140 TAAICFASAP YNSNNVMISS STNCQ

References

[1]

"Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites." Singh G., Gourinath S., Sharma S., Paramasivam M., Srinivasan A., Singh T.P. J. Mol. Biol. 307:1049-1059(2001) [PubMed: 11286555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). Tissue: Venom gland.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF297663 mRNA. Translation: AAG13412.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DPY	X-ray	2.45	A	28-145	[»]
1FE5	X-ray	2.45	A	28-145	[»]
1G2X	X-ray	2.50	A/B/C	28-139	[»]
1PO8	X-ray	2.71	A	34-137	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

Q9DF52.

Enzyme and pathway databases

BRENDA

3.1.1.4. 288873.

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

PA2K_BUNCE

Accession

Primary (citable) accession number: Q9DF52

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)