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Protein

Phospholipase A2

Gene

PLA2G1B

Organism
Bos taurus (Bovine)
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.

Catalytic activityi

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

Cofactori

Ca2+3 PublicationsNote: Binds 1 Ca2+ ion per subunit.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi52Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi54Calcium; via carbonyl oxygenCombined sources3 Publications1
Active sitei701 Publication1
Metal bindingi71CalciumCombined sources3 Publications1
Active sitei1211 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.1.1.4. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B
Gene namesi
Name:PLA2G1B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 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

ChEMBLiCHEMBL5710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 151 PublicationAdd BLAST15
PropeptideiPRO_000002273116 – 22Removed by trypsin1 Publication7
ChainiPRO_000002273223 – 145Phospholipase A21 PublicationAdd BLAST123

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Pyrrolidone carboxylic acid1
Disulfide bondi33 ↔ 99Combined sources4 Publications
Disulfide bondi49 ↔ 145Combined sources4 Publications
Disulfide bondi51 ↔ 67Combined sources4 Publications
Disulfide bondi66 ↔ 127Combined sources4 Publications
Disulfide bondi73 ↔ 120Combined sources4 Publications
Disulfide bondi83 ↔ 113Combined sources4 Publications
Disulfide bondi106 ↔ 118Combined sources4 Publications

Post-translational modificationi

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, Pyrrolidone carboxylic acid, Zymogen

Proteomic databases

PaxDbiP00593.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037960.

Structurei

Secondary structure

1145
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 34Combined sources11
Helixi40 – 43Combined sources4
Beta strandi45 – 47Combined sources3
Turni48 – 50Combined sources3
Beta strandi51 – 53Combined sources3
Helixi62 – 79Combined sources18
Helixi81 – 85Combined sources5
Beta strandi86 – 88Combined sources3
Helixi90 – 92Combined sources3
Beta strandi97 – 100Combined sources4
Beta strandi103 – 106Combined sources4
Helixi112 – 129Combined sources18
Helixi135 – 137Combined sources3
Helixi142 – 144Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BP2X-ray1.70A23-145[»]
1BPQX-ray1.80A23-145[»]
1BVMNMR-A23-145[»]
1C74X-ray1.90A23-145[»]
1CEHX-ray1.90A23-145[»]
1FDKX-ray1.91A23-145[»]
1G4IX-ray0.97A23-145[»]
1GH4X-ray1.90A23-145[»]
1IRBX-ray1.90A23-145[»]
1KVWX-ray1.95A23-145[»]
1KVXX-ray1.90A23-145[»]
1KVYX-ray1.90A23-145[»]
1MKSX-ray1.90A23-145[»]
1MKTX-ray1.72A23-145[»]
1MKUX-ray1.80A23-145[»]
1MKVX-ray1.89A23-145[»]
1O2EX-ray2.60A23-145[»]
1O3WX-ray1.85A23-145[»]
1UNEX-ray1.50A23-145[»]
1VKQX-ray1.60A23-145[»]
1VL9X-ray0.97A23-145[»]
2B96X-ray1.70A23-145[»]
2BAXX-ray1.10A23-145[»]
2BCHX-ray1.10A23-145[»]
2BD1X-ray1.90A/B23-145[»]
2BP2X-ray3.00A17-145[»]
2BPPX-ray1.80A23-145[»]
2ZP3X-ray1.90A23-145[»]
2ZP4X-ray1.90A23-145[»]
2ZP5X-ray1.90A23-145[»]
3BP2X-ray2.10A24-145[»]
4BP2X-ray1.60A16-145[»]
ProteinModelPortaliP00593.
SMRiP00593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00593.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP00593.
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.
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.

P00593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLVLAALL TVGAGQAGLN SRALWQFNGM IKCKIPSSEP LLDFNNYGCY
60 70 80 90 100
CGLGGSGTPV DDLDRCCQTH DNCYKQAKKL DSCKVLVDNP YTNNYSYSCS
110 120 130 140
NNEITCSSEN NACEAFICNC DRNAAICFSK VPYNKEHKNL DKKNC
Length:145
Mass (Da):16,002
Last modified:December 1, 2000 - v2
Checksum:i17A1E04B0C22F668
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti144N → K in CAA68303 (PubMed:3562249).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00120 mRNA. Translation: CAA68303.1.
PIRiA27508. PSBOA.
RefSeqiNP_777071.2. NM_174646.3.
XP_010812367.1. XM_010814065.2.
XP_015322603.1. XM_015467117.1.
UniGeneiBt.4439.

Genome annotation databases

GeneIDi104974671.
282457.
KEGGibta:104974671.
bta:282457.

Similar proteinsi

Entry informationi

Entry nameiPA21B_BOVIN
AccessioniPrimary (citable) accession number: P00593
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 2000
Last modified: August 30, 2017
This is version 159 of the entry and version 2 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