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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Calcium; via carbonyl oxygenCombined sources3 Publications
Metal bindingi52 – 521Calcium; via carbonyl oxygenCombined sources3 Publications
Metal bindingi54 – 541Calcium; via carbonyl oxygenCombined sources3 Publications
Active sitei70 – 7011 Publication
Metal bindingi71 – 711CalciumCombined sources3 Publications
Active sitei121 – 12111 Publication

GO - Molecular functioni

GO - Biological processi

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. 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

  • Secreted

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 PublicationAdd
BLAST
Propeptidei16 – 227Removed by trypsin1 PublicationPRO_0000022731
Chaini23 – 145123Phospholipase A21 PublicationPRO_0000022732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acid
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

1
145
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3411Combined sources
Helixi40 – 434Combined sources
Beta strandi45 – 473Combined sources
Turni48 – 503Combined sources
Beta strandi51 – 533Combined sources
Helixi62 – 7918Combined sources
Helixi81 – 855Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 923Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi103 – 1064Combined sources
Helixi112 – 12918Combined sources
Helixi135 – 1373Combined sources
Helixi142 – 1443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 23-145.
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

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441N → K in CAA68303 (PubMed:3562249).Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 23-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037960.

Chemistry

ChEMBLiCHEMBL5710.

Proteomic databases

PaxDbiP00593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5319.

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP00593.
KOiK01047.

Enzyme and pathway databases

BRENDAi3.1.1.4. 908.

Miscellaneous databases

EvolutionaryTraceiP00593.
PROiP00593.

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. "Sequence of a cDNA coding for bovine pancreatic phospholipase A2."
    Tanaka T., Kimura S., Ota Y.
    Nucleic Acids Res. 15:3178-3178(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and properties of prophospholipase A2 from ox and sheep pancreas."
    Dutilh C.E., van Doren P.J., Verheul F.E.A.M., de Haas G.H.
    Eur. J. Biochem. 53:91-97(1975)
    Cited for: PROTEIN SEQUENCE OF 16-22.
    Tissue: Pancreas.
  3. "The primary structure of bovine pancreatic phospholipase A2."
    Fleer E.A.M., Verheij H.M., de Haas G.H.
    Eur. J. Biochem. 82:261-269(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-145.
  4. "Three-dimensional structure and disulfide bond connections in bovine pancreatic phospholipase A2."
    Dijkstra B.W., Drenth J., Kalk K.H., Vandermaelen P.J.
    J. Mol. Biol. 124:53-60(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS.
  5. "Active site and catalytic mechanism of phospholipase A2."
    Dijkstra B.W., Drenth J., Kalk K.H.
    Nature 289:604-606(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), ACTIVE SITE, CATALYTIC MECHANISM.
  6. "Structure of bovine pancreatic phospholipase A2 at 1.7A resolution."
    Dijkstra B.W., Kalk K.H., Hol W.G.J., Drenth J.
    J. Mol. Biol. 147:97-123(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 23-145 IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.
  7. "The structure of bovine pancreatic prophospholipase A2 at 3.0-A resolution."
    Dijkstra B.W., van Nes G.J.H., Kalk K.H., Brandenburg N.P., Hol W.G.J., Drenth J.
    Acta Crystallogr. B 38:793-799(1982)
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 17-145 OF PROENZYME, DISULFIDE BONDS.
  8. "Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99."
    Sekar K., Yu B.Z., Rogers J., Lutton J., Liu X., Chen X., Tsai M.-D., Jain M.K., Sundaralingam M.
    Biochemistry 36:3104-3114(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-145 IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.
  9. "Crystal structure of the complex of bovine pancreatic phospholipase A2 with the inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol."
    Sekar K., Eswaramoorthy S., Jain M.K., Sundaralingam M.
    Biochemistry 36:14186-14191(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  10. "Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2."
    Sekar K., Biswas R., Li Y., Tsai M., Sundaralingam M.
    Acta Crystallogr. D 55:443-447(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-145 OF MUTANTS IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.
  11. "Structural analysis of phospholipase A2 from functional perspective. 1. Functionally relevant solution structure and roles of the hydrogen-bonding network."
    Yuan C., Byeon I.-J.L., Li Y., Tsai M.-D.
    Biochemistry 38:2909-2918(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  12. "Structural analysis of phospholipase A2 from functional perspective. 2. Characterization of a molten globule-like state induced by site-specific mutagenesis."
    Yuan C., Byeon I.-J.L., Poi M.-J., Tsai M.-D.
    Biochemistry 38:2919-2929(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF MUTANTS.

Entry informationi

Entry nameiPA21B_BOVIN
AccessioniPrimary (citable) accession number: P00593
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 154 of the entry and version 2 of the sequence. [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

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.