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UniProtKB/Swiss-Prot entry P00593


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

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Entry information
Entry name PA21B_BOVIN
Primary accession number P00593
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 90)
Name and origin of the protein
Protein name Phospholipase A2 [Precursor]
Synonyms EC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase
Group IB phospholipase A2
Gene name
Name: PLA2G1B
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/15.7.3178; PubMed=3562249 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T., Kimura S., Ota Y.;
"Sequence of a cDNA coding for bovine pancreatic phospholipase A2.";
Nucleic Acids Res. 15:3178-3178(1987).
[2]
PROTEIN SEQUENCE OF 16-22.
TISSUE=Pancreas;
Dutilh C.E., van Doren P.J., Verheul F.E.A.M., de Haas G.H.;
"Isolation and properties of prophospholipase A2 from ox and sheep pancreas.";
Eur. J. Biochem. 53:91-97(1975).
[3]
PROTEIN SEQUENCE OF 23-145.
PubMed=620674 [NCBI, ExPASy, EBI, Israel, Japan]
Fleer E.A.M., Verheij H.M., de Haas G.H.;
"The primary structure of bovine pancreatic phospholipase A2.";
Eur. J. Biochem. 82:261-269(1978).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
DOI=10.1016/0022-2836(78)90146-8; PubMed=712836 [NCBI, ExPASy, EBI, Israel, Japan]
Dijkstra B.W., Drenth J., Kalk K.H., Vandermaelen P.J.;
"Three-dimensional structure and disulfide bond connections in bovine pancreatic phospholipase A2.";
J. Mol. Biol. 124:53-60(1978).
[5]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), ACTIVE SITE, AND CATALYTIC MECHANISM.
DOI=10.1038/289604a0; PubMed=7464926 [NCBI, ExPASy, EBI, Israel, Japan]
Dijkstra B.W., Drenth J., Kalk K.H.;
"Active site and catalytic mechanism of phospholipase A2.";
Nature 289:604-606(1981).
[6]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1016/0022-2836(81)90081-4; PubMed=7265241 [NCBI, ExPASy, EBI, Israel, Japan]
Dijkstra B.W., Kalk K.H., Hol W.G.J., Drenth J.;
"Structure of bovine pancreatic phospholipase A2 at 1.7A resolution.";
J. Mol. Biol. 147:97-123(1981).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PROENZYME.
Dijkstra B.W., van Nes G.J.H., Kalk K.H., Brandenburg N.P., Hol W.G.J., Drenth J.;
"The structure of bovine pancreatic prophospholipase A2 at 3.0-A resolution.";
Acta Crystallogr. B 38:793-799(1982).
[8]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
DOI=10.1021/bi961576x; PubMed=9115986 [NCBI, ExPASy, EBI, Israel, Japan]
Sekar K., Yu B.Z., Rogers J., Lutton J., Liu X., Chen X., Tsai M.-D., Jain M.K., Sundaralingam M.;
"Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99.";
Biochemistry 36:3104-3114(1997).
[9]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
DOI=10.1021/bi971370b; PubMed=9369492 [NCBI, ExPASy, EBI, Israel, Japan]
Sekar K., Eswaramoorthy S., Jain M.K., Sundaralingam M.;
"Crystal structure of the complex of bovine pancreatic phospholipase A2 with the inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol.";
Biochemistry 36:14186-14191(1997).
[10]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS.
DOI=10.1107/S0907444998013699; PubMed=10089353 [NCBI, ExPASy, EBI, Israel, Japan]
Sekar K., Biswas R., Li Y., Tsai M., Sundaralingam M.;
"Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.";
Acta Crystallogr. D 55:443-447(1999).
[11]
STRUCTURE BY NMR.
DOI=10.1021/bi982211a; PubMed=10074343 [NCBI, ExPASy, EBI, Israel, Japan]
Yuan C., Byeon I.-J.L., Li Y., Tsai M.-D.;
"Structural analysis of phospholipase A2 from functional perspective. 1. Functionally relevant solution structure and roles of the hydrogen-bonding network.";
Biochemistry 38:2909-2918(1999).
[12]
STRUCTURE BY NMR OF MUTANTS.
DOI=10.1021/bi9822123; PubMed=10074344 [NCBI, ExPASy, EBI, Israel, Japan]
Yuan C., Byeon I.-J.L., Poi M.-J., Tsai M.-D.;
"Structural analysis of phospholipase A2 from functional perspective. 2. Characterization of a molten globule-like state induced by site-specific mutagenesis.";
Biochemistry 38:2919-2929(1999).
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
Y00120; CAA68303.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A27508; PSBOA.
RefSeq NP_777071.1; -.
UniGene Bt.4439
3D structure databases
PDB
1BP2; X-ray; 1.70 A; A=23-145.[ExPASy / RCSB / EBI]
1BPQ; X-ray; 1.80 A; A=23-145.[ExPASy / RCSB / EBI]
1BVM; NMR; -; A=23-145.[ExPASy / RCSB / EBI]
1C74; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1CEH; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1FDK; X-ray; 1.91 A; A=23-145.[ExPASy / RCSB / EBI]
1G4I; X-ray; 0.97 A; A=23-145.[ExPASy / RCSB / EBI]
1GH4; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1IRB; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1KVW; X-ray; 1.95 A; A=23-145.[ExPASy / RCSB / EBI]
1KVX; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1KVY; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1MKS; X-ray; 1.90 A; A=23-145.[ExPASy / RCSB / EBI]
1MKT; X-ray; 1.72 A; A=23-145.[ExPASy / RCSB / EBI]
1MKU; X-ray; 1.80 A; A=23-145.[ExPASy / RCSB / EBI]
1MKV; X-ray; 1.89 A; A=23-145.[ExPASy / RCSB / EBI]
1O2E; X-ray; 2.60 A; A=23-145.[ExPASy / RCSB / EBI]
1O3W; X-ray; 1.85 A; A=23-145.[ExPASy / RCSB / EBI]
1UNE; X-ray; 1.50 A; A=23-145.[ExPASy / RCSB / EBI]
1VKQ; X-ray; 1.60 A; A=23-145.[ExPASy / RCSB / EBI]
1VL9; X-ray; 0.97 A; A=23-145.[ExPASy / RCSB / EBI]
2B96; X-ray; 1.70 A; A=23-145.[ExPASy / RCSB / EBI]
2BAX; X-ray; 1.10 A; A=23-145.[ExPASy / RCSB / EBI]
2BCH; X-ray; 1.10 A; A=23-145.[ExPASy / RCSB / EBI]
2BD1; X-ray; 1.90 A; A/B=23-145.[ExPASy / RCSB / EBI]
2BP2; X-ray; 3.00 A; A=17-145.[ExPASy / RCSB / EBI]
2BPP; X-ray; 1.80 A; A=23-145.[ExPASy / RCSB / EBI]
3BP2; X-ray; 2.10 A; A=24-145.[ExPASy / RCSB / EBI]
4BP2; X-ray; 1.60 A; A=16-145.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BP2; -.
1BPQ; -.
1BVM; -.
1C74; -.
1CEH; -.
1FDK; -.
1G4I; -.
1GH4; -.
1IRB; -.
1KVW; -.
1KVX; -.
1KVY; -.
1MKS; -.
1MKT; -.
1MKU; -.
1MKV; -.
1O2E; -.
1O3W; -.
1UNE; -.
1VKQ; -.
1VL9; -.
2B96; -.
2BAX; -.
2BCH; -.
2BD1; -.
2BP2; -.
2BPP; -.
3BP2; -.
4BP2; -.
ModBase P00593.
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 P00593.
Other
SWISS-3DIMAGE P00593.
Genome annotation databases
Ensembl ENSBTAG00000026732; Bos taurus. [Contig view]
GeneID 282457; -.
KEGG bta:282457; -.
Phylogenomic databases
HOVERGEN P00593; -.
Other
LinkHub P00593; -.
ProtoNet P00593.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; 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     Removed by trypsin. PRO_0000022731
CHAIN   23   145  123     Phospholipase A2. PRO_0000022732
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. 
DISULFID   33    99         
DISULFID   49   145         
DISULFID   51    67         
DISULFID   66   127         
DISULFID   73   120         
DISULFID   83   113         
DISULFID   106   118         
CONFLICT   144   144        N -> K (in Ref. 1; CAA68303). 
HELIX   24    34  11      
HELIX   40    43  4      
STRAND   45    47  3      
TURN   48    50  3      
STRAND   51    53  3      
HELIX   62    79  18      
HELIX   81    85  5      
HELIX   90    92  3      
STRAND   97   100  4      
STRAND   103   106  4      
HELIX   112   129  18      
HELIX   135   137  3      
HELIX   142   144  3      
Sequence information
Length: 145 AA [This is the length of the unprocessed precursor] Molecular weight: 16002 Da [This is the MW of the unprocessed precursor] CRC64: 17A1E04B0C22F668 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLLVLAALL TVGAGQAGLN SRALWQFNGM IKCKIPSSEP LLDFNNYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DDLDRCCQTH DNCYKQAKKL DSCKVLVDNP YTNNYSYSCS NNEITCSSEN NACEAFICNC 

       130        140 
DRNAAICFSK VPYNKEHKNL DKKNC 

P00593 in FASTA format

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View entry in raw text format (no links)
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