ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00592


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PA21B_PIG
Primary accession number P00592
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 101)
Name and origin of the protein
Protein name Phospholipase A2, major isoenzyme [Precursor]
Synonyms EC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase
Group IB phospholipase A2
Gene name
Name: PLA2G1B
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
DOI=10.1093/nar/15.9.3743; PubMed=3295782 [NCBI, ExPASy, EBI, Israel, Japan]
de Geus P., van den Bergh C.J., Kuipers O., Verheij H.M., Hoekstra W.P.M., de Haas G.H.;
"Expression of porcine pancreatic phospholipase A2. Generation of active enzyme by sequence-specific cleavage of a hybrid protein from Escherichia coli.";
Nucleic Acids Res. 15:3743-3759(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=3028739 [NCBI, ExPASy, EBI, Israel, Japan]
Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K.;
"Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung.";
DNA 5:519-527(1986).
[3]
PROTEIN SEQUENCE OF 16-146.
PubMed=5528841 [NCBI, ExPASy, EBI, Israel, Japan]
de Haas G.H., Slotboom A.J., Bonsen P.P.M., van Deenen L.L.M., Maroux S., Puigserver A., Desnuelle P.;
"Studies on phospholipase A and its zymogen from porcine pancreas. I. The complete amino acid sequence.";
Biochim. Biophys. Acta 221:31-53(1970).
[4]
SEQUENCE REVISION.
DOI=10.1016/0005-2795(77)90076-9; PubMed=884127 [NCBI, ExPASy, EBI, Israel, Japan]
Puijk W.C., Verheij H.M., de Haas G.H.;
"The primary structure of phospholipase A2 from porcine pancreas. A reinvestigation.";
Biochim. Biophys. Acta 492:254-259(1977).
[5]
DISULFIDE BONDS.
PubMed=4919729 [NCBI, ExPASy, EBI, Israel, Japan]
de Haas G.H., Slotboom A.J., Bonsen P.P.M., Nieuwenhuizen W., van Deenen L.L.M., Maroux S., Dlouha V., Desnuelle P.;
"Studies on phospholipase A and its zymogen from porcine pancreas. II. The assignment of the position of the six disulfide bridges.";
Biochim. Biophys. Acta 221:54-61(1970).
[6]
PALMITOYLATION AT LYS-78.
TISSUE=Pancreas;
PubMed=2498336 [NCBI, ExPASy, EBI, Israel, Japan]
Tomasselli A.G., Hui J., Fisher J., Zuercher-Neely H., Reardon H.M., Oriaku E., Kezdy F.J., Heinrikson R.L.;
"Dimerization and activation of porcine pancreatic phospholipase A2 via substrate level acylation of lysine 56.";
J. Biol. Chem. 264:10041-10047(1989).
[7]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND ACTIVE AND BINDING SITES.
DOI=10.1016/S0022-2836(83)80328-3; PubMed=6876174 [NCBI, ExPASy, EBI, Israel, Japan]
Dijkstra B.W., Renetseder R., Kalk K.H., Hol W.G.J., Drenth J.;
"Structure of porcine pancreatic phospholipase A2 at 2.6-A resolution and comparison with bovine phospholipase A2.";
J. Mol. Biol. 168:163-179(1983).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1016/S0022-2836(05)80332-8; PubMed=2254938 [NCBI, ExPASy, EBI, Israel, Japan]
Thunnissen M.M.G.M., Kalk K.H., Drenth J., Dijkstra B.W.;
"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.";
J. Mol. Biol. 216:425-439(1990).
[9]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1038/347689a0; PubMed=2215698 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"X-ray structure of phospholipase A2 complexed with a substrate-derived inhibitor.";
Nature 347:689-691(1990).
[10]
STRUCTURE BY NMR.
DOI=10.1021/bi00226a022; PubMed=2007145 [NCBI, ExPASy, EBI, Israel, Japan]
Dekker N., Peters A.R., Slotboom A.J., Boelens R., Kaptein R., de Haas G.H.;
"Porcine pancreatic phospholipase A2: sequence-specific 1H and 15N NMR assignments and secondary structure.";
Biochemistry 30:3135-3147(1991).
[11]
STRUCTURE BY NMR.
DOI=10.1038/nsb0595-402; PubMed=7664098 [NCBI, ExPASy, EBI, Israel, Japan]
van den Berg B., Tessari M., Boelens R., Dijkman R., de Haas G.H., Kaptein R., Verheij H.M.;
"NMR structures of phospholipase A2 reveal conformational changes during interfacial activation.";
Nat. Struct. Biol. 2:402-406(1995).
[12]
STRUCTURE BY NMR.
PubMed=7556053 [NCBI, ExPASy, EBI, Israel, Japan]
van den Berg B., Tessari M., de Haas G.H., Verheij H.M., Boelens R., Kaptein R.;
"Solution structure of porcine pancreatic phospholipase A2.";
EMBO J. 14:4123-4131(1995).
[13]
STRUCTURE BY NMR.
DOI=10.1007/BF00208802; PubMed=7703697 [NCBI, ExPASy, EBI, Israel, Japan]
van den Berg B., Tessari M., Boelens R., Dijkman R., Kaptein R., de Haas G.H., Verheij H.M.;
"Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor.";
J. Biomol. NMR 5:110-121(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00146; CAA68341.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21055; AAA31101.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B25793; PSPGA.
RefSeq NP_001004037.1; -.
UniGene Ssc.16207
3D structure databases
PDB
1FX9; X-ray; 2.00 A; A/B=23-146.[ExPASy / RCSB / EBI]
1FXF; X-ray; 1.85 A; A/B=23-146.[ExPASy / RCSB / EBI]
1HN4; X-ray; 1.50 A; A/B=16-146.[ExPASy / RCSB / EBI]
1L8S; X-ray; 1.55 A; A/B=23-146.[ExPASy / RCSB / EBI]
1P2P; X-ray; 2.60 A; A=23-146.[ExPASy / RCSB / EBI]
1PIR; NMR; -; A=23-146.[ExPASy / RCSB / EBI]
1PIS; NMR; -; A=23-146.[ExPASy / RCSB / EBI]
1SFV; NMR; -; A=23-146.[ExPASy / RCSB / EBI]
1SFW; NMR; -; A=23-146.[ExPASy / RCSB / EBI]
1Y6O; X-ray; 2.00 A; A/B=23-146.[ExPASy / RCSB / EBI]
1Y6P; X-ray; 2.25 A; A/B=23-146.[ExPASy / RCSB / EBI]
2AZY; X-ray; 1.90 A; A=23-146.[ExPASy / RCSB / EBI]
2AZZ; X-ray; 2.20 A; A=23-146.[ExPASy / RCSB / EBI]
2B00; X-ray; 1.85 A; A=23-146.[ExPASy / RCSB / EBI]
2B01; X-ray; 2.20 A; A=23-146.[ExPASy / RCSB / EBI]
2B03; X-ray; 2.30 A; A=23-146.[ExPASy / RCSB / EBI]
2B04; X-ray; 2.50 A; A=23-146.[ExPASy / RCSB / EBI]
2PHI; X-ray; 2.20 A; A/B=23-146.[ExPASy / RCSB / EBI]
3P2P; X-ray; 2.10 A; A/B=23-146.[ExPASy / RCSB / EBI]
4P2P; X-ray; 2.40 A; A=23-146.[ExPASy / RCSB / EBI]
5P2P; X-ray; 2.40 A; A/B=23-146.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FX9; -.
1FXF; -.
1HN4; -.
1L8S; -.
1P2P; -.
1PIR; -.
1PIS; -.
1SFV; -.
1SFW; -.
1Y6O; -.
1Y6P; -.
2AZY; -.
2AZZ; -.
2B00; -.
2B01; -.
2B03; -.
2B04; -.
2PHI; -.
3P2P; -.
4P2P; -.
5P2P; -.
ModBase P00592.
Ontologies
GO
GO:0032052; Molecular function: bile acid binding (inferred from direct assay from UniProtKB).
GO:0043498; Molecular function: cell surface binding (inferred from direct assay from UniProtKB).
GO:0004623; Molecular function: phospholipase A2 activity (inferred from direct assay from UniProtKB).
GO:0005102; Molecular function: receptor binding (inferred from direct assay from UniProtKB).
GO:0000187; Biological process: activation of MAPK activity (inferred from direct assay from UniProtKB).
GO:0032869; Biological process: cellular response to insulin stimulus (inferred from direct assay from UniProtKB).
GO:0015758; Biological process: glucose transport (inferred from direct assay from UniProtKB).
GO:0032637; Biological process: interleukin-8 production (inferred from direct assay from UniProtKB).
GO:0019370; Biological process: leukotriene biosynthetic process (inferred from direct assay from UniProtKB).
GO:0030593; Biological process: neutrophil chemotaxis (inferred from direct assay from UniProtKB).
GO:0002446; Biological process: neutrophil mediated immunity (inferred from direct assay from UniProtKB).
GO:0010524; Biological process: positive regulation of calcium ion transport into cytosol (inferred from direct assay from UniProtKB).
GO:0045740; Biological process: positive regulation of DNA replication (inferred from direct assay from UniProtKB).
GO:0048146; Biological process: positive regulation of fibroblast proliferation (inferred from direct assay from UniProtKB).
GO:0050778; Biological process: positive regulation of immune response (inferred from direct assay from UniProtKB).
GO:0051092; Biological process: positive regulation of NF-kappaB transcription factor activity (inferred from direct assay from UniProtKB).
GO:0010552; Biological process: positive regulation of specific transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016090; Phospholipase_A2.
IPR013090; Phospholipase_A2_AS.
IPR001211; Phospholipase_A2_euk.
Graphical view of domain structure.
Gene3D G3DSA:1.20.90.10; Phospholipase_A2; 1.
PANTHER PTHR11716; Phospholipase_A2; 1.
Pfam PF00068; Phospholip_A2_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00389; PHPHLIPASEA2.
ProDom PD000303; PhospholipaseA2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00085; PA2c; 1.
SMART graphical view of domain structure.
PROSITE PS00119; PA2_ASP; 1.
PS00118; PA2_HIS; 1.
BLOCKS P00592.
Genome annotation databases
GeneID 445525; -.
KEGG ssc:445525; -.
Phylogenomic databases
HOVERGEN P00592; -.
Other
LinkHub P00592; -.
ProtoNet P00592.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Lipoprotein; Metal-binding; Palmitate; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15      
PROPEP   16    22  7     Activation peptide. PRO_0000022743
CHAIN   23   146  124     Phospholipase A2, major isoenzyme. PRO_0000022744
ACT_SITE   70    70         
ACT_SITE   121   121         
METAL   50    50        Calcium; via carbonyl oxygen. 
METAL   52    52        Calcium; via carbonyl oxygen. 
METAL   54    54        Calcium; via carbonyl oxygen. 
METAL   71    71        Calcium. 
MOD_RES   16    16        Pyrrolidone carboxylic acid. 
LIPID   78    78        N6-palmitoyl lysine. 
DISULFID   33    99         
DISULFID   49   146         
DISULFID   51    67         
DISULFID   66   127         
DISULFID   73   120         
DISULFID   83   113         
DISULFID   106   118         
HELIX   24    34  11      
HELIX   40    44  5      
TURN   48    50  3      
STRAND   51    53  3      
HELIX   62    79  18      
HELIX   81    83  3      
HELIX   90    92  3      
STRAND   97   100  4      
STRAND   103   106  4      
HELIX   112   128  17      
HELIX   135   137  3      
HELIX   142   145  4      
Sequence information
Length: 146 AA [This is the length of the unprocessed precursor] Molecular weight: 16279 Da [This is the MW of the unprocessed precursor] CRC64: DE87674C9476FA36 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKFLVLAVLL TVGAAQEGIS SRALWQFRSM IKCAIPGSHP LMDFNNYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DELDRCCETH DNCYRDAKNL DSCKFLVDNP YTESYSYSCS NTEITCNSKN NACEAFICNC 

       130        140 
DRNAAICFSK APYNKEHKNL DTKKYC 

P00592 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!