P00593 (PA21B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospholipase A2
EC=3.1.1.4

Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B

Gene names

Name:

PLA2G1B

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Monomer or homodimer. The inactive pro-form is a homotrimer By similarity.
Subcellular location	Secreted. Note: secreted from pancreatic acinar cells in its inactive form By similarity.
Post-translational modification	Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically By similarity.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Autocatalytic cleavage Disulfide bond Pyrrolidone carboxylic acid Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	multicellular organismal lipid catabolic process Inferred from electronic annotation. Source: Compara phosphatidylcholine metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from electronic annotation. Source: Compara
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 – 15

15

Ref.2

Propeptide

16 – 22

7

Removed by trypsin Ref.2

PRO_0000022731

Chain

23 – 145

123

Phospholipase A2 Ref.3

PRO_0000022732

Sites

Active site

70

1

Ref.5

Active site

121

1

Ref.5

Metal binding

50

1

Calcium; via carbonyl oxygen

Metal binding

52

1

Calcium; via carbonyl oxygen

Metal binding

54

1

Calcium; via carbonyl oxygen

Metal binding

71

1

Calcium

Amino acid modifications

Modified residue

16

1

Pyrrolidone carboxylic acid

Disulfide bond

33 ↔ 99

Ref.4

Disulfide bond

49 ↔ 145

Ref.4

Disulfide bond

51 ↔ 67

Ref.4

Disulfide bond

66 ↔ 127

Ref.4

Disulfide bond

73 ↔ 120

Ref.4

Disulfide bond

83 ↔ 113

Ref.4

Disulfide bond

106 ↔ 118

Ref.4

Experimental info

Sequence conflict

144

1

N → K in CAA68303. Ref.1

Secondary structure

1

.

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145

Helix Strand Turn

Details...

Helix

24 – 34

11

Helix

40 – 43

4

Beta strand

45 – 47

3

Turn

48 – 50

3

Beta strand

51 – 53

3

Helix

62 – 79

18

Helix

81 – 85

5

Beta strand

86 – 88

3

Helix

90 – 92

3

Beta strand

97 – 100

4

Beta strand

103 – 106

4

Helix

112 – 129

18

Helix

135 – 137

3

Helix

142 – 144

3

Sequences

	Sequence		Length	Mass (Da)
	P00593 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 17A1E04B0C22F668	FASTA	145	16,002
	10 20 30 40 50 60 MRLLVLAALL TVGAGQAGLN SRALWQFNGM IKCKIPSSEP LLDFNNYGCY CGLGGSGTPV 70 80 90 100 110 120 DDLDRCCQTH DNCYKQAKKL DSCKVLVDNP YTNNYSYSCS NNEITCSSEN NACEAFICNC 130 140 DRNAAICFSK VPYNKEHKNL DKKNC

References

[1]	"Sequence of a cDNA coding for bovine pancreatic phospholipase A2." Tanaka T., Kimura S., Ota Y. Nucleic Acids Res. 15:3178-3178(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation and properties of prophospholipase A2 from ox and sheep pancreas." Dutilh C.E., van Doren P.J., Verheul F.E.A.M., de Haas G.H. Eur. J. Biochem. 53:91-97(1975) Cited for: PROTEIN SEQUENCE OF 16-22. Tissue: Pancreas.
[3]	"The primary structure of bovine pancreatic phospholipase A2." Fleer E.A.M., Verheij H.M., de Haas G.H. Eur. J. Biochem. 82:261-269(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-145.
[4]	"Three-dimensional structure and disulfide bond connections in bovine pancreatic phospholipase A2." Dijkstra B.W., Drenth J., Kalk K.H., Vandermaelen P.J. J. Mol. Biol. 124:53-60(1978) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS.
[5]	"Active site and catalytic mechanism of phospholipase A2." Dijkstra B.W., Drenth J., Kalk K.H. Nature 289:604-606(1981) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), ACTIVE SITE, CATALYTIC MECHANISM.
[6]	"Structure of bovine pancreatic phospholipase A2 at 1.7A resolution." Dijkstra B.W., Kalk K.H., Hol W.G.J., Drenth J. J. Mol. Biol. 147:97-123(1981) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[7]	"The structure of bovine pancreatic prophospholipase A2 at 3.0-A resolution." Dijkstra B.W., van Nes G.J.H., Kalk K.H., Brandenburg N.P., Hol W.G.J., Drenth J. Acta Crystallogr. B 38:793-799(1982) Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PROENZYME.
[8]	"Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99." Sekar K., Yu B.Z., Rogers J., Lutton J., Liu X., Chen X., Tsai M.-D., Jain M.K., Sundaralingam M. Biochemistry 36:3104-3114(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
[9]	"Crystal structure of the complex of bovine pancreatic phospholipase A2 with the inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol." Sekar K., Eswaramoorthy S., Jain M.K., Sundaralingam M. Biochemistry 36:14186-14191(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[10]	"Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2." Sekar K., Biswas R., Li Y., Tsai M., Sundaralingam M. Acta Crystallogr. D 55:443-447(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS.
[11]	"Structural analysis of phospholipase A2 from functional perspective. 1. Functionally relevant solution structure and roles of the hydrogen-bonding network." Yuan C., Byeon I.-J.L., Li Y., Tsai M.-D. Biochemistry 38:2909-2918(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[12]	"Structural analysis of phospholipase A2 from functional perspective. 2. Characterization of a molten globule-like state induced by site-specific mutagenesis." Yuan C., Byeon I.-J.L., Poi M.-J., Tsai M.-D. Biochemistry 38:2919-2929(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANTS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00120 mRNA. Translation: CAA68303.1.

IPI

IPI00706994.

PIR

PSBOA. A27508.

RefSeq

NP_777071.2. NM_174646.3.

UniGene

Bt.4439.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BP2	X-ray	1.70	A	23-145	[»]
1BPQ	X-ray	1.80	A	23-145	[»]
1BVM	NMR	-	A	23-145	[»]
1C74	X-ray	1.90	A	23-145	[»]
1CEH	X-ray	1.90	A	23-145	[»]
1FDK	X-ray	1.91	A	23-145	[»]
1G4I	X-ray	0.97	A	23-145	[»]
1GH4	X-ray	1.90	A	23-141	[»]
1IRB	X-ray	1.90	A	23-141	[»]
1KVW	X-ray	1.95	A	23-145	[»]
1KVX	X-ray	1.90	A	23-145	[»]
1KVY	X-ray	1.90	A	23-145	[»]
1MKS	X-ray	1.90	A	23-145	[»]
1MKT	X-ray	1.72	A	23-145	[»]
1MKU	X-ray	1.80	A	23-145	[»]
1MKV	X-ray	1.89	A	23-145	[»]
1O2E	X-ray	2.60	A	23-145	[»]
1O3W	X-ray	1.85	A	23-145	[»]
1UNE	X-ray	1.50	A	23-145	[»]
1VKQ	X-ray	1.60	A	23-145	[»]
1VL9	X-ray	0.97	A	23-145	[»]
2B96	X-ray	1.70	A	23-145	[»]
2BAX	X-ray	1.10	A	23-145	[»]
2BCH	X-ray	1.10	A	23-141	[»]
2BD1	X-ray	1.90	A/B	23-141	[»]
2BP2	X-ray	3.00	A	17-145	[»]
2BPP	X-ray	1.80	A	23-145	[»]
2ZP3	X-ray	1.90	A	23-145	[»]
2ZP4	X-ray	1.90	A	23-145	[»]
2ZP5	X-ray	1.90	A	23-145	[»]
3BP2	X-ray	2.10	A	24-145	[»]
4BP2	X-ray	1.60	A	16-145	[»]

ProteinModelPortal

P00593.

SMR

P00593. Positions 23-145.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000037960.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

282457.

KEGG

bta:282457.

Organism-specific databases

CTD

5319.

Phylogenomic databases

eggNOG

NOG290764.

HOGENOM

HOG000231749.

HOVERGEN

HBG008137.

InParanoid

P00593.

KO

K01047.

OrthoDB

EOG4GHZQJ.

Family and domain databases

Gene3D

1.20.90.10. 1 hit.

InterPro

IPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]

PANTHER

PTHR11716. PTHR11716. 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

ChEMBL

CHEMBL5710.

EvolutionaryTrace

P00593.

NextBio

20806224.

Entry information

Entry name

PA21B_BOVIN

Accession

Primary (citable) accession number: P00593

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program