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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)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

  • 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
  • phospholipid metabolic process Source: InterPro
  • 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.

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

  • 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 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
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

  • receptor binding Source: UniProtKB

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.
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
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...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028002.

Chemistry databases

BindingDBiP00592.
ChEMBLiCHEMBL4715.
SwissLipidsiSLP:000001435.

Proteomic databases

PaxDbiP00592.
PRIDEiP00592.

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.
PROiP00592.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
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...

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: November 30, 2016
This is version 161 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.