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UniProtKB/Swiss-Prot entry Q9Z0Y2


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

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Entry information
Entry name PA21B_MOUSE
Primary accession number Q9Z0Y2
Secondary accession numbers Q9D7E2 Q9D884
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 77)
Name and origin of the protein
Protein name Phospholipase A2 [Precursor]
Synonyms EC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase
Group IB phospholipase A2
PLA2-Ib
Gene name
Name: Pla2g1b
Synonyms: Pla2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=129/SvJ;
Mandal A.K., Zhang Z., Mukherjee A.B.;
"Isolation, characterization and chromosomal localization of mouse sPLA2-Ib gene.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.274.11.7043; PubMed=10066760 [NCBI, ExPASy, EBI, Israel, Japan]
Cupillard L., Mulherkar R., Gomez N., Kadam S., Valentin E., Lazdunski M., Lambeau G.;
"Both group IB and group IIA secreted phospholipases A2 are natural ligands of the mouse 180-kDa M-type receptor.";
J. Biol. Chem. 274:7043-7051(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Lung;
DOI=10.1074/jbc.274.44.31476; PubMed=10531350 [NCBI, ExPASy, EBI, Israel, Japan]
Bingham C.O. III, Fijneman R.J.A., Friend D.S., Goddeau R.P., Rogers R.A., Austen K.F., Arm J.P.;
"Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells.";
J. Biol. Chem. 274:31476-31484(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0378-1119(00)00006-8; PubMed=10689188 [NCBI, ExPASy, EBI, Israel, Japan]
Richmond B.L., Hui D.Y.;
"Molecular structure and tissue-specific expression of the mouse pancreatic phospholipase A2 gene.";
Gene 244:65-72(2000).
[5]
NUCLEOTIDE SEQUENCE.
STRAIN=129/SvJ;
TISSUE=Pancreas;
Mandal A.K., Zhang Z., Popescu N., Mukherjee A.B.;
"Role of sPLA2-I in colorectal tumorigenesis.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Pancreas, Small intestine, Stomach, and Tongue;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
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
AF094611; AAF02298.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097637; AAD19896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162712; AAD45806.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF187852; AAF44297.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF094610; AAG27064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK028104; BAC25749.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK028134; BAC25763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008936; BAB25978.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK007730; BAB25218.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK007797; BAB25263.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008664; BAB25819.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008668; BAB25822.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008841; BAB25922.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008934; BAB25976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008331; BAB25608.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK009314; BAB26212.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_035237.1; -.
UniGene Mm.20190
3D structure databases
HSSP P00593; 1GH4. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR Q9Z0Y2; 19-141.
ModBase Q9Z0Y2.
PTM databases
PhosphoSite Q9Z0Y2; -.
Organism-specific databases
MGI MGI:101842; Pla2g1b.
Gene expression databases
ArrayExpress Q9Z0Y2; -.
CleanEx MM_PLA2G1B; -.
GermOnline ENSMUSG00000029522; Mus musculus.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from direct assay from MGI).
GO:0004623; Molecular function: phospholipase A2 activity (inferred from direct assay from MGI).
GO:0005102; Molecular function: receptor binding (inferred from direct assay from MGI).
GO:0008283; Biological process: cell proliferation (traceable author statement from MGI).
GO:0009395; Biological process: phospholipid catabolic process (traceable author statement from MGI).
GO:0006950; Biological process: response to stress (traceable author statement from MGI).
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 Q9Z0Y2.
Genome annotation databases
Ensembl ENSMUSG00000029522; Mus musculus. [Contig view]
GeneID 18778; -.
KEGG mmu:18778; -.
Phylogenomic databases
HOGENOM Q9Z0Y2; -.
HOVERGEN Q9Z0Y2; -.
Other
SOURCE Pla2g1b; Mus musculus.
ProtoNet Q9Z0Y2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15     By similarity. 
PROPEP   16    22  7     Activation peptide (By similarity). PRO_0000022741
CHAIN   23   146  124     Phospholipase A2. PRO_0000022742
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        By similarity. 
DISULFID   49   146        By similarity. 
DISULFID   51    67        By similarity. 
DISULFID   66   127        By similarity. 
DISULFID   73   120        By similarity. 
DISULFID   83   113        By similarity. 
DISULFID   106   118        By similarity. 
CONFLICT   52    52        G -> S (in Ref. 6; BAB26212). 
CONFLICT   58    58        T -> P (in Ref. 6; BAB26212). 
CONFLICT   78    79        KK -> EN (in Ref. 6; BAB26212). 
CONFLICT   87    87        I -> R (in Ref. 6; BAB26212). 
CONFLICT   95    95        Y -> F (in Ref. 6; BAB26212). 
CONFLICT   102   102        S -> G (in Ref. 6; BAB26212). 
CONFLICT   122   122        R -> S (in Ref. 6; BAB25608). 
Sequence information
Length: 146 AA [This is the length of the unprocessed precursor] Molecular weight: 16290 Da [This is the MW of the unprocessed precursor] CRC64: 59500C68845B7C81 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLLLLAALL TAGAAAHSIS PRAVWQFRNM IKCTIPGSDP LKDYNNYGCY CGLGGWGTPV 

        70         80         90        100        110        120 
DDLDRCCQTH DHCYSQAKKL ESCKFLIDNP YTNTYSYSCS GSEITCSAKN NKCEDFICNC 

       130        140 
DREAAICFSK VPYNKEYKNL DTGKFC 

Q9Z0Y2 in FASTA format

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