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Protein

Phospholipase A2, major isoenzyme

Gene

PLA2G1B

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Calcium; via carbonyl oxygen1
Metal bindingi52Calcium; via carbonyl oxygen1
Metal bindingi54Calcium; via carbonyl oxygen1
Active sitei701 Publication1
Metal bindingi71Calcium1
Active sitei1211 Publication1

GO - Molecular functioni

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
  • 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
  • phospholipid metabolic process Source: InterPro
  • positive regulation of calcium ion transport into cytosol Source: BHF-UCL
  • positive regulation of cell proliferation 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 by RNA polymerase II Source: BHF-UCL
  • regulation of glucose import Source: BHF-UCL

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4 6170

Chemistry databases

SwissLipidsiSLP:000001435

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4715

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 151 PublicationAdd BLAST15
PropeptideiPRO_000002274316 – 22Activation peptide7
ChainiPRO_000002274423 – 146Phospholipase A2, major isoenzymeAdd BLAST124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi33 ↔ 991 Publication
Disulfide bondi49 ↔ 1461 Publication
Disulfide bondi51 ↔ 671 Publication
Disulfide bondi66 ↔ 1271 Publication
Disulfide bondi73 ↔ 1201 Publication
Lipidationi78N6-palmitoyl lysine1 Publication1
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
PRIDEiP00592

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • signaling receptor binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028002

Chemistry databases

BindingDBiP00592

Structurei

Secondary structure

1146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 34Combined sources14
Beta strandi35 – 37Combined sources3
Helixi40 – 44Combined sources5
Beta strandi45 – 47Combined sources3
Turni48 – 50Combined sources3
Beta strandi51 – 54Combined sources4
Helixi62 – 78Combined sources17
Helixi81 – 87Combined sources7
Helixi90 – 92Combined sources3
Beta strandi97 – 100Combined sources4
Beta strandi103 – 106Combined sources4
Beta strandi108 – 110Combined sources3
Helixi112 – 130Combined sources19
Helixi135 – 137Combined sources3
Helixi142 – 145Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
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

CDDicd00125 PLA2c, 1 hit
Gene3Di1.20.90.10, 1 hit
InterProiView protein in InterPro
IPR001211 PLipase_A2
IPR033112 PLipase_A2_Asp_AS
IPR016090 PLipase_A2_dom
IPR036444 PLipase_A2_dom_sf
IPR033113 PLipase_A2_His_AS
PANTHERiPTHR11716 PTHR11716, 1 hit
PfamiView protein in Pfam
PF00068 Phospholip_A2_1, 1 hit
PRINTSiPR00389 PHPHLIPASEA2
SMARTiView protein in SMART
SM00085 PA2c, 1 hit
SUPFAMiSSF48619 SSF48619, 1 hit
PROSITEiView protein in PROSITE
PS00119 PA2_ASP, 1 hit
PS00118 PA2_HIS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPA21B_PIG
AccessioniPrimary (citable) accession number: P00592
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: May 23, 2018
This is version 166 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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