P59071 (PA28_DABRR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 VRV-PL-VIIIa EC=3.1.1.4 Alternative name(s): DPLA2 P1 Phosphatidylcholine 2-acylhydrolase Phospholipase A2 4 Short name=PLA24
Organism	Daboia russelli russelli (Indian Russell's viper) (Vipera russelli russelli)
Taxonomic identifier	31159 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Daboia

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
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. This toxin shows neurotoxic symptoms and damages vital organs such as lung, liver and kidney. Displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. Ref.2
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion.
Subunit structure	Monomer. Ref.1
Subcellular location	Secreted Ref.3.
Tissue specificity	Expressed by the venom gland. Ref.3
Toxic dose	LD50 is between 5.3 and 5.5 mg/kg by intravenous injection into mice. Ref.2 Ref.4
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 Neurotoxin Presynaptic neurotoxin 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	other organism presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
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

Chain

1 – 121

121

Phospholipase A2 VRV-PL-VIIIa

PRO_0000161717

Sites

Active site

47

1

Active site

89

1

Metal binding

27

1

Calcium; via carbonyl oxygen

Metal binding

29

1

Calcium; via carbonyl oxygen

Metal binding

31

1

Calcium; via carbonyl oxygen

Metal binding

48

1

Calcium

Amino acid modifications

Disulfide bond

26 ↔ 115

Disulfide bond

28 ↔ 44

Disulfide bond

43 ↔ 95

Disulfide bond

49 ↔ 121

Disulfide bond

50 ↔ 88

Disulfide bond

57 ↔ 81

Disulfide bond

75 ↔ 86

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

121

Helix Strand Turn

Details...

Helix

2 – 13

12

Helix

17 – 20

4

Beta strand

22 – 24

3

Turn

25 – 30

6

Helix

39 – 52

14

Turn

59 – 61

3

Beta strand

66 – 69

4

Beta strand

72 – 75

4

Helix

80 – 98

19

Helix

99 – 102

4

Helix

105 – 107

3

Helix

112 – 114

3

Sequences

	Sequence		Length	Mass (Da)
	P59071 [UniParc]. Last modified November 1, 2002. Version 1. Checksum: 5CDF82DDA7DA638E	FASTA	121	13,611
	10 20 30 40 50 60 SLLEFGKMIL EETGKLAIPS YSSYGCYCGW GGKGTPKDAT DRCCFVHDCC YGNLPDCNPK 70 80 90 100 110 120 SDRYKYKRVN GAIVCEKGTS CENRICECDK AAAICFRQNL NTYSKKYMLY PDFLCKGELK C

References

[1]	"Primary sequence determination of the most basic myonecrotic phospholipase A2 from the venom of Vipera russelli." Gowda T.V., Schmidt J., Middlebrook J.L. Toxicon 32:665-673(1994) [PubMed: 7940574] [Abstract] Cited for: PROTEIN SEQUENCE, SUBUNIT. Tissue: Venom.
[2]	"Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies." Tsai I.-H., Lu P.-J., Su J.-C. Toxicon 34:99-109(1996) [PubMed: 8835338] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-50, FUNCTION, LETHAL DOSE. Tissue: Venom.
[3]	"Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka." Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G., Athauda S.B., Moriyama A. Biomed. Res. 31:71-81(2010) [PubMed: 20203422] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Venom.
[4]	"Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom." Kasturi S., Gowda T.V. Toxicon 27:229-237(1989) [PubMed: 2718191] [Abstract] Cited for: CHARACTERIZATION, LETHAL DOSE. Tissue: Venom.
[5]	"Three-dimensional structure of a presynaptic neurotoxic phospholipase A2 from Daboia russelli pulchella at 2.4 A resolution." Chandra V., Kaur P., Srinivasan A., Singh T.P. J. Mol. Biol. 296:1117-1126(2000) [PubMed: 10686108] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[6]	"Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution." Chandra V., Kaur P., Jasti J., Betzel C., Singh T.P. Acta Crystallogr. D 57:1793-1798(2001) [PubMed: 11717491] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[7]	"Design of specific peptide inhibitors of phospholipase A2: structure of a complex formed between Russell's viper phospholipase A2 and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS)." Chandra V., Jasti J., Kaur P., Dey S., Srinivasan A., Betzel C., Singh T.P. Acta Crystallogr. D 58:1813-1819(2002) [PubMed: 12351825] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]	"Structural basis of phospholipase A2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 A crystal structure." Chandra V., Jasti J., Kaur P., Srinivasan A., Betzel C., Singh T.P. Biochemistry 41:10914-10919(2002) [PubMed: 12206661] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[9]	"Crystal structure of a complex formed between a snake venom phospholipase A(2) and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 A resolution." Chandra V., Jasti J., Kaur P., Dey S., Perbandt M., Srinivasan A., Betzel C., Singh T.P. J. Biol. Chem. 277:41079-41085(2002) [PubMed: 12186870] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CL5	X-ray	2.45	A/B	1-121	[»]
1FB2	X-ray	1.95	A/B	1-121	[»]
1FV0	X-ray	1.70	A/B	1-121	[»]
1JQ8	X-ray	2.00	A/B	1-121	[»]
1JQ9	X-ray	1.80	A/B	1-121	[»]
1KPM	X-ray	1.80	A/B	1-121	[»]
1OXL	X-ray	1.80	A/B	1-121	[»]
1OYF	X-ray	2.45	A	1-121	[»]
1SKG	X-ray	1.21	A	1-121	[»]
1SQZ	X-ray	1.20	A	1-121	[»]
1SV3	X-ray	1.35	A	1-121	[»]
1SV9	X-ray	2.71	A	1-121	[»]
1SXK	X-ray	1.21	A	1-121	[»]
1TDV	X-ray	1.70	A	1-121	[»]
1TG1	X-ray	1.25	A	1-121	[»]
1TG4	X-ray	1.70	A	1-121	[»]
1TGM	X-ray	1.86	A	1-121	[»]
1TH6	X-ray	1.23	A	1-121	[»]
1TJ9	X-ray	1.10	A	1-121	[»]
1TJK	X-ray	1.25	A	1-121	[»]
1TK4	X-ray	1.10	A	1-121	[»]
1TP2	X-ray	2.40	A/B	1-121	[»]
1Y38	X-ray	2.44	A/B	1-121	[»]
1ZR8	X-ray	2.03	A	1-121	[»]
1ZWP	X-ray	1.10	A	1-121	[»]
1ZYX	X-ray	1.95	A	1-121	[»]
2B17	X-ray	2.71	A	1-121	[»]
2DO2	X-ray	2.60	A	1-121	[»]
2DPZ	X-ray	2.10	A	1-121	[»]
2FNX	X-ray	2.70	A	1-121	[»]
2G58	X-ray	0.98	A	1-121	[»]
2GNS	X-ray	2.30	A	1-121	[»]
2O1N	X-ray	2.80	A	1-121	[»]
2OLI	X-ray	2.21	A	1-121	[»]
2OTF	X-ray	1.95	A	1-121	[»]
2OTH	X-ray	2.90	A	1-121	[»]
2OUB	X-ray	2.75	A	1-121	[»]
2OYF	X-ray	1.20	A	1-121	[»]
2PB8	X-ray	2.00	A	1-121	[»]
2PMJ	X-ray	2.40	A	1-121	[»]
2PVT	X-ray	2.10	A	1-117	[»]
2PWS	X-ray	2.21	A	1-121	[»]
2PYC	X-ray	1.50	A	1-121	[»]
2Q1P	X-ray	1.50	A	1-121	[»]
2QHW	X-ray	2.21	A	1-121	[»]
2QU9	X-ray	2.08	A	1-121	[»]
2QUE	X-ray	2.25	A	1-121	[»]
2QVD	X-ray	1.93	A	1-121	[»]
2ZBH	X-ray	2.60	A	1-121	[»]
3CBI	X-ray	3.15	A/B/C/D	1-121	[»]
3G8F	X-ray	1.25	A	1-121	[»]
3H1X	X-ray	1.40	A	1-121	[»]

ProteinModelPortal

P59071.

SMR

P59071. Positions 1-121.

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...

Other

DrugBank

DB00233. Aminosalicylic Acid.
DB00945. Aspirin.
DB00572. Atropine.
DB03585. Oxyphenbutazone.

Entry information

Entry name

PA28_DABRR

Accession

Primary (citable) accession number: P59071

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	November 1, 2002
Last modified:	December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program