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Protein

Phospholipase A2, major isoenzyme

Gene

PLA2G1B

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Calcium; via carbonyl oxygen
Metal bindingi52 – 521Calcium; via carbonyl oxygen
Metal bindingi54 – 541Calcium; via carbonyl oxygen
Active sitei70 – 7011 Publication
Metal bindingi71 – 711Calcium
Active sitei121 – 12111 Publication

GO - Molecular functioni

  • bile acid binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • phospholipase A2 activity Source: BHF-UCL
  • receptor binding Source: UniProtKB

GO - Biological processi

  • activation of MAPK activity Source: BHF-UCL
  • cellular response to insulin stimulus Source: BHF-UCL
  • fatty acid biosynthetic process Source: BHF-UCL
  • glucose transport Source: BHF-UCL
  • interleukin-8 production Source: BHF-UCL
  • intracellular signal transduction Source: BHF-UCL
  • leukotriene biosynthetic process Source: BHF-UCL
  • lipid catabolic process Source: UniProtKB-KW
  • neutrophil chemotaxis Source: BHF-UCL
  • neutrophil mediated immunity Source: BHF-UCL
  • positive regulation of calcium ion transport into cytosol Source: BHF-UCL
  • positive regulation of DNA replication Source: BHF-UCL
  • positive regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of immune response Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 6170.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2, major isoenzyme (EC:3.1.1.4)
Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B
Gene namesi
Name:PLA2G1B
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Secreted

  • Note: secreted from pancreatic acinar cells in its inactive form.By similarity

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular region Source: UniProtKB-SubCell
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 PublicationAdd
BLAST
Propeptidei16 – 227Activation peptidePRO_0000022743
Chaini23 – 146124Phospholipase A2, major isoenzymePRO_0000022744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acid
Disulfide bondi33 ↔ 991 Publication
Disulfide bondi49 ↔ 1461 Publication
Disulfide bondi51 ↔ 671 Publication
Disulfide bondi66 ↔ 1271 Publication
Disulfide bondi73 ↔ 1201 Publication
Lipidationi78 – 781N6-palmitoyl lysine1 Publication
Disulfide bondi83 ↔ 1131 Publication
Disulfide bondi106 ↔ 1181 Publication

Post-translational modificationi

Acylation causes dimerization.
Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Lipoprotein, Palmitate, Pyrrolidone carboxylic acid, Zymogen

Proteomic databases

PaxDbiP00592.

Interactioni

Subunit structurei

Monomer or homodimer. The inactive pro-form is a homotrimer (By similarity).By similarity

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028002.

Chemistry

BindingDBiP00592.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3414Combined sources
Beta strandi35 – 373Combined sources
Helixi40 – 445Combined sources
Beta strandi45 – 473Combined sources
Turni48 – 503Combined sources
Beta strandi51 – 544Combined sources
Helixi62 – 7817Combined sources
Helixi81 – 877Combined sources
Helixi90 – 923Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi108 – 1103Combined sources
Helixi112 – 13019Combined sources
Helixi135 – 1373Combined sources
Helixi142 – 1454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX9X-ray2.00A/B23-146[»]
1FXFX-ray1.85A/B23-146[»]
1HN4X-ray1.50A/B16-146[»]
1L8SX-ray1.55A/B23-146[»]
1P2PX-ray2.60A23-146[»]
1PIRNMR-A23-146[»]
1PISNMR-A23-146[»]
1SFVNMR-A23-146[»]
1SFWNMR-A23-146[»]
1Y6OX-ray2.00A/B23-146[»]
1Y6PX-ray2.25A/B23-146[»]
2AZYX-ray1.90A23-146[»]
2AZZX-ray2.20A23-146[»]
2B00X-ray1.85A23-146[»]
2B01X-ray2.20A23-146[»]
2B03X-ray2.30A23-146[»]
2B04X-ray2.50A23-146[»]
2PHIX-ray2.20A/B23-146[»]
3FVIX-ray2.70A/B/C/D23-146[»]
3FVJX-ray2.30A23-146[»]
3HSWX-ray2.50A23-146[»]
3L30X-ray2.40A23-146[»]
3O4MX-ray2.50A23-146[»]
3P2PX-ray2.10A/B23-146[»]
3QLMX-ray2.50A23-146[»]
4DBKX-ray2.30A23-146[»]
4G5IX-ray2.40A23-146[»]
4O1YX-ray2.50A23-146[»]
4P2PX-ray2.40A23-146[»]
5P2PX-ray2.40A/B23-146[»]
ProteinModelPortaliP00592.
SMRiP00592. Positions 18-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00592.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
HOVERGENiHBG008137.
InParanoidiP00592.
KOiK01047.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00592-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLVLAVLL TVGAAQEGIS SRALWQFRSM IKCAIPGSHP LMDFNNYGCY
60 70 80 90 100
CGLGGSGTPV DELDRCCETH DNCYRDAKNL DSCKFLVDNP YTESYSYSCS
110 120 130 140
NTEITCNSKN NACEAFICNC DRNAAICFSK APYNKEHKNL DTKKYC
Length:146
Mass (Da):16,279
Last modified:January 1, 1988 - v1
Checksum:iDE87674C9476FA36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00146 mRNA. Translation: CAA68341.1.
M21055 mRNA. Translation: AAA31101.1.
PIRiB25793. PSPGA.
RefSeqiNP_001004037.1. NM_001004037.1.
UniGeneiSsc.16207.

Genome annotation databases

GeneIDi445525.
KEGGissc:445525.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00146 mRNA. Translation: CAA68341.1.
M21055 mRNA. Translation: AAA31101.1.
PIRiB25793. PSPGA.
RefSeqiNP_001004037.1. NM_001004037.1.
UniGeneiSsc.16207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX9X-ray2.00A/B23-146[»]
1FXFX-ray1.85A/B23-146[»]
1HN4X-ray1.50A/B16-146[»]
1L8SX-ray1.55A/B23-146[»]
1P2PX-ray2.60A23-146[»]
1PIRNMR-A23-146[»]
1PISNMR-A23-146[»]
1SFVNMR-A23-146[»]
1SFWNMR-A23-146[»]
1Y6OX-ray2.00A/B23-146[»]
1Y6PX-ray2.25A/B23-146[»]
2AZYX-ray1.90A23-146[»]
2AZZX-ray2.20A23-146[»]
2B00X-ray1.85A23-146[»]
2B01X-ray2.20A23-146[»]
2B03X-ray2.30A23-146[»]
2B04X-ray2.50A23-146[»]
2PHIX-ray2.20A/B23-146[»]
3FVIX-ray2.70A/B/C/D23-146[»]
3FVJX-ray2.30A23-146[»]
3HSWX-ray2.50A23-146[»]
3L30X-ray2.40A23-146[»]
3O4MX-ray2.50A23-146[»]
3P2PX-ray2.10A/B23-146[»]
3QLMX-ray2.50A23-146[»]
4DBKX-ray2.30A23-146[»]
4G5IX-ray2.40A23-146[»]
4O1YX-ray2.50A23-146[»]
4P2PX-ray2.40A23-146[»]
5P2PX-ray2.40A/B23-146[»]
ProteinModelPortaliP00592.
SMRiP00592. Positions 18-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028002.

Chemistry

BindingDBiP00592.
ChEMBLiCHEMBL2366566.

Proteomic databases

PaxDbiP00592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi445525.
KEGGissc:445525.

Organism-specific databases

CTDi5319.

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
HOVERGENiHBG008137.
InParanoidiP00592.
KOiK01047.

Enzyme and pathway databases

BRENDAi3.1.1.4. 6170.

Miscellaneous databases

EvolutionaryTraceiP00592.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), ACTIVE SITE, 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiPA21B_PIG
AccessioniPrimary (citable) accession number: P00592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Loss of activity upon alkylation of His-70 with p-bromo phenacyl bromide; Ca2+ and Ba2+ protect against inactivation.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.