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UniProtKB/Swiss-Prot entry P04054


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

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Entry information
Entry name PA21B_HUMAN
Primary accession number P04054
Secondary accession number Q3KPI1
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on February 1, 1991 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 88)
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
Synonyms: PLA2, PLA2A, PPLA2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Lung;
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04569; PubMed=16541075 [NCBI, ExPASy, EBI, Israel, Japan]
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 16-22.
TISSUE=Pancreas;
PubMed=7060561 [NCBI, ExPASy, EBI, Israel, Japan]
Grataroli R., Dijkman R., Dutilh C.E., van der Ouderaa F., de Haas G.H., Figarella C.;
"Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region.";
Eur. J. Biochem. 122:111-117(1982).
[6]
PROTEIN SEQUENCE OF 23-148.
TISSUE=Pancreas;
DOI=10.1016/0167-4838(83)90126-7; PubMed=6349696 [NCBI, ExPASy, EBI, Israel, Japan]
Verheij H.M., Westerman J., Sternby B., de Haas G.H.;
"The complete primary structure of phospholipase A2 from human pancreas.";
Biochim. Biophys. Acta 747:93-99(1983).
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
M21056; AAA60107.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22970; AAA60107.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21054; AAA36450.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY438977; AAR05441.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC003982; AAB95635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106725; AAI06726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106726; AAI06727.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C25793; PSHU.
RefSeq NP_000919.1; -.
UniGene Hs.992
3D structure databases
PDB
1YSK; Model; -; A=23-146.[ExPASy / RCSB / EBI]
PDBsum 1YSK; -.
ModBase P04054.
PTM databases
PhosphoSite P04054; -.
Polymorphism databases
NIEHS-SNPs PLA2G1B.
Organism-specific databases
H-InvDB HIX0011060; -.
HGNC HGNC:9030; PLA2G1B.
GenAtlas PLA2G1B.
MIM 172410; gene. [NCBI / EBI]
PharmGKB PA33361; -.
GeneCards P04054.
Gene expression databases
ArrayExpress P04054; -.
CleanEx HS_PLA2G1B; -.
GermOnline ENSG00000170890; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0032052; Molecular function: bile acid binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (inferred from direct assay from UniProtKB).
GO:0047498; Molecular function: calcium-dependent phospholipase A2 activity (inferred from direct assay from UniProtKB).
GO:0043498; Molecular function: cell surface binding (inferred from direct assay from UniProtKB).
GO:0005102; Molecular function: receptor binding (inferred from direct assay from UniProtKB).
GO:0007015; Biological process: actin filament organization (traceable author statement from ProtInc).
GO:0000187; Biological process: activation of MAPK activity (inferred from sequence or structural similarity from UniProtKB).
GO:0032431; Biological process: activation of phospholipase A2 (traceable author statement from UniProtKB).
GO:0050482; Biological process: arachidonic acid secretion (traceable author statement from UniProtKB).
GO:0032869; Biological process: cellular response to insulin stimulus (inferred from sequence or structural similarity from UniProtKB).
GO:0015758; Biological process: glucose transport (inferred from sequence or structural similarity from UniProtKB).
GO:0032637; Biological process: interleukin-8 production (inferred from sequence or structural similarity from UniProtKB).
GO:0019370; Biological process: leukotriene biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0044240; Biological process: multicellular organismal lipid catabolic process (inferred from direct assay from UniProtKB).
GO:0030593; Biological process: neutrophil chemotaxis (inferred from sequence or structural similarity from UniProtKB).
GO:0002446; Biological process: neutrophil mediated immunity (inferred from sequence or structural similarity from UniProtKB).
GO:0046470; Biological process: phosphatidylcholine metabolic process (inferred from direct assay from UniProtKB).
GO:0010524; Biological process: positive regulation of calcium ion transport into cytosol (inferred from sequence or structural similarity 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 by curator from UniProtKB).
GO:0050778; Biological process: positive regulation of immune response (inferred from sequence or structural similarity from UniProtKB).
GO:0051092; Biological process: positive regulation of NF-kappaB transcription factor activity (inferred from sequence or structural similarity from UniProtKB).
GO:0050714; Biological process: positive regulation of protein secretion (traceable author statement from UniProtKB).
GO:0010552; Biological process: positive regulation of specific transcription from RNA polymerase II promoter (inferred from sequence or structural similarity 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 P04054.
Genome annotation databases
Ensembl ENSG00000170890; Homo sapiens. [Contig view]
GeneID 5319; -.
KEGG hsa:5319; -.
Phylogenomic databases
HOGENOM P04054; -.
HOVERGEN P04054; -.
Other
SOURCE PLA2G1B; Homo sapiens.
ProtoNet P04054.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Polymorphism; 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_0000022739
CHAIN   23   148  126     Phospholipase A2. PRO_0000022740
ACT_SITE   70    70        By similarity. 
ACT_SITE   121   121        By similarity. 
METAL   50    50        Calcium (via carbonyl oxygen) (By similarity). 
METAL   52    52        Calcium (via carbonyl oxygen) (By similarity). 
METAL   54    54        Calcium (via carbonyl oxygen) (By similarity). 
METAL   71    71        Calcium (By similarity). 
DISULFID   33    99         
DISULFID   49   146         
DISULFID   51    67         
DISULFID   66   127         
DISULFID   73   120         
DISULFID   83   113         
DISULFID   106   118         
VARIANT   16    16  1     D -> A (in dbSNP:rs5632 [NCBI]). VAR_011911 
VARIANT   89    89  1     N -> K (in dbSNP:rs5636 [NCBI]). VAR_011913 [3D]
VARIANT   89    89  1     N -> T (in dbSNP:rs5635 [NCBI]). VAR_011912 [3D]
CONFLICT   144   144        Missing (in Ref. 6; AA sequence). 
Sequence information
Length: 148 AA [This is the length of the unprocessed precursor] Molecular weight: 16360 Da [This is the MW of the unprocessed precursor] CRC64: C8E38B2B64AEE8CB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLLVLAVLL TVAAADSGIS PRAVWQFRKM IKCVIPGSDP FLEYNNYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DELDKCCQTH DNCYDQAKKL DSCKFLLDNP YTHTYSYSCS GSAITCSSKN KECEAFICNC 

       130        140 
DRNAAICFSK APYNKAHKNL DTKKYCQS 

P04054 in FASTA format

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