Reviewed, UniProtKB/Swiss-Prot P00592 (PA21B_PIG)

Names and origin

Protein names

Recommended name:
    Phospholipase A2, major isoenzyme
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Group IB phospholipase A2

Gene names

Name:

PLA2G1B

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	146 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.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Monomer or homodimer.
Subcellular location	Secreted.
Post-translational modification	Acylation causes dimerization.
Miscellaneous	Loss of activity upon alkylation of His-70 with p-bromo phenacyl bromide; Ca2+ and Ba2+ protect against inactivation.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Lipoprotein Palmitate Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	activation of MAPK activity Inferred from direct assay. Source: UniProtKB cellular response to insulin stimulus Inferred from direct assay. Source: UniProtKB glucose transport Inferred from direct assay. Source: UniProtKB interleukin-8 production Inferred from direct assay. Source: UniProtKB leukotriene biosynthetic process Inferred from direct assay. Source: UniProtKB lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW neutrophil chemotaxis Inferred from direct assay. Source: UniProtKB neutrophil mediated immunity Inferred from direct assay. Source: UniProtKB phospholipid metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of DNA replication Inferred from direct assay. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from direct assay. Source: UniProtKB positive regulation of calcium ion transport into cytosol Inferred from direct assay. Source: UniProtKB positive regulation of fibroblast proliferation Inferred from direct assay. Source: UniProtKB positive regulation of immune response Inferred from direct assay. Source: UniProtKB positive regulation of specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	bile acid binding Inferred from direct assay. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW cell surface binding Inferred from direct assay. Source: UniProtKB phospholipase A2 activity Inferred from direct assay. Source: UniProtKB receptor binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Ref.3

Propeptide

16 – 22

7

Activation peptide

PRO_0000022743

Chain

23 – 146

124

Phospholipase A2, major isoenzyme

PRO_0000022744

Sites

Active site

70

1

Active site

121

1

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

Lipidation

78

1

N6-palmitoyl lysine

Disulfide bond

33 ↔ 99

Ref.5

Disulfide bond

49 ↔ 146

Ref.5

Disulfide bond

51 ↔ 67

Ref.5

Disulfide bond

66 ↔ 127

Ref.5

Disulfide bond

73 ↔ 120

Ref.5

Disulfide bond

83 ↔ 113

Ref.5

Disulfide bond

106 ↔ 118

Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

146

Helix Strand Turn

Details...

Helix

24 – 34

11

Helix

40 – 44

5

Turn

48 – 50

3

Beta strand

51 – 53

3

Helix

62 – 79

18

Helix

81 – 83

3

Helix

90 – 92

3

Beta strand

97 – 100

4

Beta strand

103 – 106

4

Helix

112 – 128

17

Helix

135 – 137

3

Helix

142 – 145

4

Sequences

	Sequence		Length	Mass (Da)
	P00592-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: DE87674C9476FA36	FASTA	146	16,279
	10 20 30 40 50 60 MKFLVLAVLL TVGAAQEGIS SRALWQFRSM IKCAIPGSHP LMDFNNYGCY CGLGGSGTPV 70 80 90 100 110 120 DELDRCCETH DNCYRDAKNL DSCKFLVDNP YTESYSYSCS NTEITCNSKN NACEAFICNC 130 140 DRNAAICFSK APYNKEHKNL DTKKYC

References

[1]	"Expression of porcine pancreatic phospholipase A2. Generation of active enzyme by sequence-specific cleavage of a hybrid protein from Escherichia coli." de Geus P., van den Bergh C.J., Kuipers O., Verheij H.M., Hoekstra W.P.M., de Haas G.H. Nucleic Acids Res. 15:3743-3759(1987) [PubMed: 3295782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[2]	"Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung." Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K. DNA 5:519-527(1986) [PubMed: 3028739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[3]	"Studies on phospholipase A and its zymogen from porcine pancreas. I. The complete amino acid sequence." de Haas G.H., Slotboom A.J., Bonsen P.P.M., van Deenen L.L.M., Maroux S., Puigserver A., Desnuelle P. Biochim. Biophys. Acta 221:31-53(1970) [PubMed: 5528841] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-146.
[4]	"The primary structure of phospholipase A2 from porcine pancreas. A reinvestigation." Puijk W.C., Verheij H.M., de Haas G.H. Biochim. Biophys. Acta 492:254-259(1977) [PubMed: 884127] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"Studies on phospholipase A and its zymogen from porcine pancreas. II. The assignment of the position of the six disulfide bridges." de Haas G.H., Slotboom A.J., Bonsen P.P.M., Nieuwenhuizen W., van Deenen L.L.M., Maroux S., Dlouha V., Desnuelle P. Biochim. Biophys. Acta 221:54-61(1970) [PubMed: 4919729] [Abstract] Cited for: DISULFIDE BONDS.
[6]	"Dimerization and activation of porcine pancreatic phospholipase A2 via substrate level acylation of lysine 56." Tomasselli A.G., Hui J., Fisher J., Zuercher-Neely H., Reardon H.M., Oriaku E., Kezdy F.J., Heinrikson R.L. J. Biol. Chem. 264:10041-10047(1989) [PubMed: 2498336] [Abstract] Cited for: PALMITOYLATION AT LYS-78. Tissue: Pancreas.
[7]	"Structure of porcine pancreatic phospholipase A2 at 2.6-A resolution and comparison with bovine phospholipase A2." Dijkstra B.W., Renetseder R., Kalk K.H., Hol W.G.J., Drenth J. J. Mol. Biol. 168:163-179(1983) [PubMed: 6876174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), ACTIVE AND BINDING SITES.
[8]	"Structure of an engineered porcine phospholipase A2 with enhanced activity at 2.1-A resolution. Comparison with the wild-type porcine and Crotalus atrox phospholipase A2." Thunnissen M.M.G.M., Kalk K.H., Drenth J., Dijkstra B.W. J. Mol. Biol. 216:425-439(1990) [PubMed: 2254938] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]	"X-ray structure of phospholipase A2 complexed with a substrate-derived inhibitor." Thunnissen M.M.G.M., Ab E., Kalk K.H., Drenth J., Dijkstra B.W., Kuipers O.P., Dijkman R., de Haas G.H., Verheij H.M. Nature 347:689-691(1990) [PubMed: 2215698] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[10]	"Porcine pancreatic phospholipase A2: sequence-specific 1H and 15N NMR assignments and secondary structure." Dekker N., Peters A.R., Slotboom A.J., Boelens R., Kaptein R., de Haas G.H. Biochemistry 30:3135-3147(1991) [PubMed: 2007145] [Abstract] Cited for: STRUCTURE BY NMR.
[11]	"NMR structures of phospholipase A2 reveal conformational changes during interfacial activation." van den Berg B., Tessari M., Boelens R., Dijkman R., de Haas G.H., Kaptein R., Verheij H.M. Nat. Struct. Biol. 2:402-406(1995) [PubMed: 7664098] [Abstract] Cited for: STRUCTURE BY NMR.
[12]	"Solution structure of porcine pancreatic phospholipase A2." van den Berg B., Tessari M., de Haas G.H., Verheij H.M., Boelens R., Kaptein R. EMBO J. 14:4123-4131(1995) [PubMed: 7556053] [Abstract] Cited for: STRUCTURE BY NMR.
[13]	"Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor." van den Berg B., Tessari M., Boelens R., Dijkman R., Kaptein R., de Haas G.H., Verheij H.M. J. Biomol. NMR 5:110-121(1995) [PubMed: 7703697] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00146 mRNA. Translation: CAA68341.1.
M21055 mRNA. Translation: AAA31101.1.

PIR

PSPGA. B25793.

RefSeq

NP_001004037.1.

UniGene

Ssc.16207

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FX9	X-ray	2.00	A/B	23-146	[»]
1FXF	X-ray	1.85	A/B	23-146	[»]
1HN4	X-ray	1.50	A/B	16-146	[»]
1L8S	X-ray	1.55	A/B	23-146	[»]
1P2P	X-ray	2.60	A	23-146	[»]
1PIR	NMR	-	A	23-146	[»]
1PIS	NMR	-	A	23-146	[»]
1SFV	NMR	-	A	23-146	[»]
1SFW	NMR	-	A	23-146	[»]
1Y6O	X-ray	2.00	A/B	23-146	[»]
1Y6P	X-ray	2.25	A/B	23-146	[»]
2AZY	X-ray	1.90	A	23-146	[»]
2AZZ	X-ray	2.20	A	23-146	[»]
2B00	X-ray	1.85	A	23-146	[»]
2B01	X-ray	2.20	A	23-146	[»]
2B03	X-ray	2.30	A	23-146	[»]
2B04	X-ray	2.50	A	23-146	[»]
2PHI	X-ray	2.20	A/B	23-146	[»]
3P2P	X-ray	2.10	A/B	23-146	[»]
4P2P	X-ray	2.40	A	23-146	[»]
5P2P	X-ray	2.40	A/B	23-146	[»]

ModBase

Search...

Genome annotation databases

GeneID

445525.

KEGG

ssc:445525.

Phylogenomic databases

HOVERGEN

P00592.

Enzyme and pathway databases

BRENDA

3.1.1.4. 249.

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

PA21B_PIG

Accession

Primary (citable) accession number: P00592

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)