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UniProtKB/Swiss-Prot entry P05063


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

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Entry information
Entry name ALDOC_MOUSE
Primary accession number P05063
Secondary accession numbers Q64011 Q8CA91 Q99K96 Q9DBA4 Q9JK32
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 95)
Name and origin of the protein
Protein name Fructose-bisphosphate aldolase C
Synonyms EC 4.1.2.13
Brain-type aldolase
Aldolase 3
Zebrin II
Scrapie-responsive protein 2
Gene name
Name: Aldoc
Synonyms: Aldo3, Scrg2
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J;
TISSUE=Cerebellum;
PubMed=7925012 [NCBI, ExPASy, EBI, Israel, Japan]
Ahn A.H., Dziennis S., Hawkes R., Herrup K.;
"The cloning of zebrin II reveals its identity with aldolase C.";
Development 120:2081-2090(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, and Spinal cord;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-227.
DOI=10.1111/j.1432-1033.1986.tb09572.x; PubMed=3009179 [NCBI, ExPASy, EBI, Israel, Japan]
Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.;
"Structure and expression of mouse aldolase genes. Brain-specific aldolase C amino acid sequence is closely related to aldolase A.";
Eur. J. Biochem. 156:229-235(1986).
[5]
PROTEIN SEQUENCE OF 2-13; 29-57; 61-69; 154-200; 244-258; 260-289; 305-315; 319-330 AND 343-363, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 73-87; 112-134; 158-173 AND 260-289, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, AND TISSUE SPECIFICITY.
STRAIN=BALB/c;
TISSUE=Brain;
DOI=10.1016/S0169-328X(00)00028-0; PubMed=10719228 [NCBI, ExPASy, EBI, Israel, Japan]
Dandoy-Dron F.C., Benboudjema L., Guillo F., Jaegly A., Jasmin C., Dormont D., Tovey M.G., Dron M.;
"Enhanced levels of scrapie responsive gene mRNA in BSE-infected mouse brain.";
Brain Res. Mol. Brain Res. 76:173-179(2000).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS SPECTROMETRY.
TISSUE=Brain cortex;
DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan]
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119, AND MASS SPECTROMETRY.
TISSUE=Brain;
Lubec G., Kang S.;
Submitted (APR-2007) to UniProtKB.
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
S72537; AAB32064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005077; BAB23801.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK039267; BAC30300.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004802; AAH04802.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008184; AAH08184.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03796; CAA27422.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ132391; CAB77178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25388; ADMSC.
I53145; I53145.
RefSeq NP_033787.2; -.
UniGene Mm.7729
3D structure databases
HSSP P00883; 6ALD. [HSSP ENTRY / PDB]
SMR P05063; 3-344.
ModBase P05063.
Protein-protein interaction databases
IntAct P05063; -.
PTM databases
PhosphoSite P05063; -.
Organism-specific databases
MGI MGI:101863; Aldoc.
Gene expression databases
ArrayExpress P05063; -.
CleanEx MM_ALDOC; -.
GermOnline ENSMUSG00000017390; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0004332; Molecular function: fructose-bisphosphate aldolase activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR11627; Aldolase_I; 1.
Pfam PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.
ProDom PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00158; ALDOLASE_CLASS_I; 1.
BLOCKS P05063.
ProtoNet P05063.
Genome annotation databases
Ensembl ENSMUSG00000017390; Mus musculus. [Contig view]
GeneID 11676; -.
KEGG mmu:11676; -.
Phylogenomic databases
HOGENOM P05063; -.
HOVERGEN P05063; -.
Other
NextBio 279307; -.
SOURCE Aldoc; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein; Schiff base.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   363  362     Fructose-bisphosphate aldolase C. PRO_0000216949
ACT_SITE   188   188        Proton acceptor (By similarity). 
ACT_SITE   230   230        Schiff-base intermediate with dihydroxyacetone-P. 
BINDING   56    56        Substrate. 
BINDING   147   147        Substrate. 
SITE   363   363  1     Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate. 
MOD_RES   39    39        Phosphoserine. 
MOD_RES   119   119        Phosphothreonine. 
MOD_RES   147   147        N6-acetyllysine (By similarity). 
CONFLICT   25    25        T -> A (in Ref. 3; AAH04802/AAH08184). 
CONFLICT   46    46        Q -> E (in Ref. 2; BAC30300). 
CONFLICT   62    62        V -> A (in Ref. 4; CAA27422). 
CONFLICT   113   113        V -> L (in Ref. 4; CAA27422). 
CONFLICT   201   201        R -> H (in Ref. 3; AAH04802/AAH08184). 
CONFLICT   280   280        A -> V (in Ref. 1; AAB32064). 
CONFLICT   358   358        I -> V (in Ref. 3; AAH04802/AAH08184). 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 39395 Da [This is the MW of the unprocessed precursor] CRC64: 085C58AF163581C6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPHSYPALSA EQKKELSDIA LRIVTPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGILVGIKVD KGVVPLAGTD 

       130        140        150        160        170        180 
GETTTQGLDG LLERCAQYKK DGADFAKWRC VLKISDRTPS ALAILENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
PIKYSPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEMNGLAAQ GRYEGSGDGG AAAQSLYIAN 


HAY 

P05063 in FASTA format

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