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UniProtKB/Swiss-Prot entry P17182


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

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Entry information
Entry name ENOA_MOUSE
Primary accession number P17182
Secondary accession numbers Q99KT7 Q9DCY7
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 99)
Name and origin of the protein
Protein name Alpha-enolase
Synonyms EC 4.2.1.11
2-phospho-D-glycerate hydro-lyase
Non-neural enolase
NNE
Enolase 1
Gene name
Name: Eno1
Synonyms: Eno-1
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=Brain;
DOI=10.1093/nar/18.12.3638; PubMed=2362815 [NCBI, ExPASy, EBI, Israel, Japan]
Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M., Lazar M., Caput D.;
"Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse brain.";
Nucleic Acids Res. 18:3638-3638(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney;
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].
STRAIN=Czech II, and FVB/N;
TISSUE=Mammary gland, and Mammary tumor;
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]
PROTEIN SEQUENCE OF 16-28; 33-50; 72-80; 90-120; 133-179; 184-193; 203-228; 234-253; 257-262; 270-281; 307-326; 344-358 AND 373-394, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 60-71; 100-114; 184-198 AND 246-259.
TISSUE=Macrophage;
PubMed=8427861 [NCBI, ExPASy, EBI, Israel, Japan]
Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I.;
"Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an alpha-enolase isoform.";
Arterioscler. Thromb. 13:264-275(1993).
[6]
PROTEIN SEQUENCE OF 106-120; 133-179; 234-253; 270-281 AND 307-326, AND MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[7]
INTERACTION WITH PKM2; PGM; CKM; ALDO AND TROPONIN, AND DEVELOPMENTAL STAGE.
PubMed=9169614 [NCBI, ExPASy, EBI, Israel, Japan]
Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.;
"Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.";
Biochem. J. 323:791-800(1997).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0248-4900(00)01103-5; PubMed=11229603 [NCBI, ExPASy, EBI, Israel, Japan]
Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.;
"Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle.";
Biol. Cell 92:527-535(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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).
Comments
  • FUNCTION: Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses (By similarity). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (By similarity).
  • CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
  • COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
  • PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
  • SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (By similarity). In vitro, interacts with several glycolytic enzymes including PKM2, PGM, CKM and aldolase. Also binds troponin, in vitro.
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By similarity). ENO1 is localized to the M-band.
  • TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, expression of ENO1 appears to be independent of fiber type.
  • DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In embryonic muscle, ENO1 is highly expressed until E17. Decreased levels from P5.
  • SIMILARITY: Belongs to the enolase family.
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
X52379; CAA36605.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002336; BAB22021.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003891; AAH03891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004017; AAH04017.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010685; AAH10685.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024644; AAH24644.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC085098; AAH85098.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S10246; S10246.
RefSeq NP_001020559.1; -.
NP_075608.2; -.
XP_001471566.1; -.
UniGene Mm.372357
3D structure databases
HSSP P56252; 1PDZ. [HSSP ENTRY / PDB]
SMR P17182; 2-431.
ModBase P17182.
Protein-protein interaction databases
IntAct P17182; -.
PTM databases
PhosphoSite P17182; -.
2D gel databases
SWISS-2DPAGE P17182; -.
REPRODUCTION-2DPAGE P17182; -.
Organism-specific databases
MGI MGI:95393; Eno1.
Gene expression databases
GermOnline ENSMUSG00000059040; Mus musculus.
ENSMUSG00000063524; Mus musculus.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS P17182.
Genome annotation databases
Ensembl ENSMUSG00000059040; Mus musculus. [Contig view]
ENSMUSG00000063524; Mus musculus. [Contig view]
GeneID 100044223; -.
13806; -.
433182; -.
KEGG mmu:100044223; -.
mmu:13806; -.
mmu:433182; -.
Phylogenomic databases
HOGENOM P17182; -.
HOVERGEN P17182; -.
Other
SOURCE Eno1; Mus musculus.
ProtoNet P17182.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   434  433     Alpha-enolase. PRO_0000134098
REGION   370   373  4     Substrate binding (By similarity). 
REGION   405   434  30     Required for interaction with PLG (By similarity). 
ACT_SITE   210   210        Proton donor (By similarity). 
ACT_SITE   343   343        Proton acceptor (By similarity). 
METAL   245   245        Magnesium (By similarity). 
METAL   293   293        Magnesium (By similarity). 
METAL   318   318        Magnesium (By similarity). 
BINDING   158   158        Substrate (By similarity). 
BINDING   167   167        Substrate (By similarity). 
BINDING   293   293        Substrate (By similarity). 
BINDING   318   318        Substrate (By similarity). 
BINDING   394   394        Substrate (By similarity). 
MOD_RES   44    44        Phosphotyrosine. 
MOD_RES   63    63        Phosphoserine (By similarity). 
MOD_RES   71    71        N6-acetyllysine (By similarity). 
MOD_RES   72    72        Phosphothreonine (By similarity). 
MOD_RES   263   263        Phosphoserine. 
MOD_RES   287   287        Phosphotyrosine (By similarity). 
CONFLICT   359   359        L -> P (in Ref. 1; CAA36605). 
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 47141 Da [This is the MW of the unprocessed precursor] CRC64: DBEF6270A70DE3A6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK 

        70         80         90        100        110        120 
GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAVEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV 

       250        260        270        280        290        300 
VIGMDVAASE FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK 

       430 
AKFAGRSFRN PLAK 

P17182 in FASTA format

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