O42187 (PA24_GLOHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 B EC=3.1.1.4 Alternative name(s): BPLA(2) Phosphatidylcholine 2-acylhydrolase
Organism	Gloydius halys (Chinese water mocassin) (Agkistrodon halys)
Taxonomic identifier	8714 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius

Protein attributes

Sequence length	138 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. This potent hemolytic and anticoagulant toxin is one of the few phospholipases A2 capable of hydrolyzing the phospholipids of E.coli membranes in the presence of a bactericidal/permeability-increasing protein (BPI) of neutrophils.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords
Biological process	Blood coagulation Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Toxin
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW 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 – 16

16

By similarity

Chain

17 – 138

122

Phospholipase A2 B

PRO_0000022776

Sites

Active site

63

1

By similarity

Active site

105

1

By similarity

Metal binding

43

1

Calcium; via carbonyl oxygen

Metal binding

45

1

Calcium; via carbonyl oxygen

Metal binding

47

1

Calcium; via carbonyl oxygen

Metal binding

64

1

Calcium

Amino acid modifications

Disulfide bond

42 ↔ 131

Ref.3

Disulfide bond

44 ↔ 60

Ref.3

Disulfide bond

59 ↔ 111

Ref.3

Disulfide bond

65 ↔ 138

Ref.3

Disulfide bond

66 ↔ 104

Ref.3

Disulfide bond

73 ↔ 97

Ref.3

Disulfide bond

91 ↔ 102

Ref.3

Secondary structure

1

.

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.

.

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.

.

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.

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138

Helix Strand Turn

Details...

Helix

18 – 29

12

Helix

33 – 37

5

Turn

41 – 43

3

Beta strand

44 – 47

4

Helix

55 – 68

14

Turn

75 – 77

3

Beta strand

82 – 85

4

Beta strand

88 – 91

4

Helix

96 – 114

19

Helix

116 – 118

3

Helix

121 – 123

3

Helix

128 – 130

3

Sequences

	Sequence		Length	Mass (Da)
	O42187 [UniParc]. Last modified December 13, 2002. Version 2. Checksum: 149D21704F4AA437	FASTA	138	15,614
	10 20 30 40 50 60 MRALWIVAVL LLGVEGSLLQ FRKMIKKMTG KEPVVSYAFY GCYCGSGGRG KPKDATDRCC 70 80 90 100 110 120 FVHDCCYEKL TGCDPKWDDY TYSWKNGTIV CGGDDPCKKE VCECDKAAAI CFRDNLKTYK 130 KRYMTYPNIL CSSKSEKC

References

[1]	"Cloning of the BPLA(2) gene from Agkistrodon halys pallas." Pan H., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Wu X.-F. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 28:579-582(1996) [PubMed: 12232583] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Diversity of cDNAs encoding phospholipase A2 from Agkistrodon halys pallas venom, and its expression in E. coli." Pan H., Liu X.-L., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Li Z.-P., Wu X.-F. Toxicon 36:1155-1163(1998) [PubMed: 9690782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[3]	"Structure of a basic phospholipase A2 from Agkistrodon halys pallas at 2.13 A resolution." Zhao K., Song S., Lin Z., Zhou Y.-C. Acta Crystallogr. D 54:510-521(1998) [PubMed: 9761847] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 18-138, METAL-BINDING SITES, DISULFIDE BONDS. Tissue: Venom.
[4]	"Structure of basic phospholipase A2 from Agkistrodon halys pallas: implications for its association, hemolytic and anticoagulant activities." Zhao K., Zhou Y.-C., Lin Z. Toxicon 38:901-916(2000) [PubMed: 10728829] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 18-138. Tissue: Venom.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF015242 mRNA. Translation: AAB71844.1.

PIR

JC1342.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B4W	X-ray	2.60	A/B/C/D	18-138	[»]
1C1J	X-ray	2.80	A/B/C/D	18-138	[»]
1JIA	X-ray	2.13	A/B	18-138	[»]

ProteinModelPortal

O42187.

SMR

O42187. Positions 18-138.

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

PA24_GLOHA

Accession

Primary (citable) accession number: O42187

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2002
Last sequence update:	December 13, 2002
Last modified:	October 19, 2011
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program