P80966 (PA21B_OPHHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2, acidic 1 EC=3.1.1.4 Alternative name(s): APLA2-1 OHV A-PLA2 Short name=OHV-APLA2 Phosphatidylcholine 2-acylhydrolase
Organism	Ophiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifier	8665 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Ophiophagus

Protein attributes

Sequence length	151 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. Exhibits cardiotoxicity, myotoxicity, antiplatelet activity, and edema-inducing activity.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit. Ref.3
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	Cardiotoxin Hydrolase Toxin
PTM	Disulfide bond
Technical term	3D-structure 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: InterPro 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_0000022942

Chain

28 – 151

124

Phospholipase A2, acidic 1

PRO_0000022943

Sites

Active site

75

1

By similarity

Active site

126

1

By similarity

Metal binding

55

1

Calcium; via carbonyl oxygen

Metal binding

57

1

Calcium; via carbonyl oxygen

Metal binding

59

1

Calcium; via carbonyl oxygen

Metal binding

76

1

Calcium

Amino acid modifications

Disulfide bond

38 ↔ 104

Ref.3

Disulfide bond

54 ↔ 151

Ref.3

Disulfide bond

56 ↔ 72

Ref.3

Disulfide bond

71 ↔ 132

Ref.3

Disulfide bond

78 ↔ 125

Ref.3

Disulfide bond

88 ↔ 118

Ref.3

Disulfide bond

111 ↔ 123

Ref.3

Secondary structure

1

.

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.

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.

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.

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151

Helix Strand Turn

Details...

Helix

29 – 39

11

Helix

46 – 49

4

Turn

53 – 55

3

Beta strand

56 – 59

4

Helix

67 – 84

18

Helix

86 – 88

3

Helix

94 – 97

4

Beta strand

102 – 105

4

Beta strand

108 – 111

4

Helix

117 – 134

18

Helix

140 – 142

3

Helix

147 – 150

4

Sequences

	Sequence		Length	Mass (Da)
	P80966 [UniParc]. Last modified August 30, 2002. Version 2. Checksum: F1E021B886BC4BEB	FASTA	151	16,444
	10 20 30 40 50 60 MNPAHLLVLS AVCVSLLGAS SIPPQPLHLI QFGNMIQCTV PGFLSWIKYA DYGCYCGAGG 70 80 90 100 110 120 SGTPVDKLDR CCQVHDNCYT QAQKLPACSS IMDSPYVKIY SYDCSERTVT CKADNDECAA 130 140 150 FICNCDRVAA HCFAASPYNN NNYNIDTTTR C

References

[1]	"Cloning and characterization of cDNAs encoding two acidic isoforms of phospholipase A2 in Guangxi King Cobra (Ophiophagus hannah)." Wang Q.Y., Shu Y.Y. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Complete amino acid sequence of an acidic, cardiotoxic phospholipase A2 from the venom of Ophiophagus hannah (King Cobra): a novel cobra venom enzyme with 'pancreatic loop'." Huang M.Z., Gopalakrishnakone P., Chung M.C.M., Kini R.M. Arch. Biochem. Biophys. 338:150-156(1997) [PubMed: 9028866] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-151. Tissue: Venom.
[3]	"Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with the 'pancreatic loop'." Zhang H.L., Xu S.J., Wang Q.Y., Song S.Y., Shu Y.Y., Lin Z.J. J. Struct. Biol. 138:207-215(2002) [PubMed: 12217659] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), COFACTOR, CALCIUM-BINDING SITES, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF302908 mRNA. Translation: AAG23964.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GP7	X-ray	2.60	A/B/C	1-151	[»]

ProteinModelPortal

P80966.

SMR

P80966. Positions 28-151.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG008137.

Family and domain databases

InterPro

IPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_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]

SUPFAM

SSF48619. PhospholipaseA2. 1 hit.

PROSITE

PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PA21B_OPHHA

Accession

Primary (citable) accession number: P80966
Secondary accession number(s): Q9DF32

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	August 30, 2002
Last modified:	October 19, 2011
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program