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UniProtKB/Swiss-Prot entry P21550


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

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Entry information
Entry name ENOB_MOUSE
Primary accession number P21550
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 92)
Name and origin of the protein
Protein name Beta-enolase
Synonyms EC 4.2.1.11
2-phospho-D-glycerate hydro-lyase
Muscle-specific enolase
MSE
Skeletal muscle enolase
Enolase 3
Gene name
Name: Eno3
Synonyms: Eno-3
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 [GENOMIC DNA / MRNA].
STRAIN=BALB/c, and Swiss Webster;
TISSUE=Liver, and Skeletal muscle;
Lamande N., Brosset S., Keller A., Lucas M., Lazar M.;
Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H;
DOI=10.1016/0012-1606(92)90201-Q; PubMed=1339335 [NCBI, ExPASy, EBI, Israel, Japan]
Peterson C.A., Cho M., Rastinejad F., Blau H.M.;
"Beta-enolase is a marker of human myoblast heterogeneity prior to differentiation.";
Dev. Biol. 151:626-629(1992).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
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 33-50; 104-120; 257-262; 336-358 AND 373-394, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
PubMed=2734297 [NCBI, ExPASy, EBI, Israel, Japan]
Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F., Legault-Demare L., Lazar M.;
"Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression.";
Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989).
[7]
PROTEIN SEQUENCE OF 106-120.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[8]
ACTIVATION DURING MYOGENESIS.
DOI=10.1016/0925-4773(92)90037-K; PubMed=1525038 [NCBI, ExPASy, EBI, Israel, Japan]
Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M., Lazar M.;
"Activation of the gene encoding the glycolytic enzyme beta-enolase during early myogenesis precedes an increased expression during fetal muscle development.";
Mech. Dev. 38:41-54(1992).
[9]
DEVELOPMENTAL STAGE.
PubMed=8594891 [NCBI, ExPASy, EBI, Israel, Japan]
Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.;
"Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy.";
Am. J. Physiol. 269:H1843-H1851(1995).
[10]
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).
[11]
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).
[12]
EXPRESSION REGULATION.
PubMed=10848992 [NCBI, ExPASy, EBI, Israel, Japan]
Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H., Keller A.;
"Differential modulation of alpha, beta and gamma enolase isoforms in regenerating mouse skeletal muscle.";
Eur. J. Biochem. 267:3735-3743(2000).
Comments
  • FUNCTION: Appears to have a function in striated muscle development and regeneration.
  • 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. In vitro, interacts with several glycolytic enzymes including PKM2, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity).
  • 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, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I.
  • 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 hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube.
  • INDUCTION: Levels decrease in degenerating myofibers, and increase with their regeneration.
  • 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
X61600; CAA43797.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57747; CAA40913.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X62667; CAA44540.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002485; BAB22137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013460; AAH13460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20745; AAA37554.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17109; NOMSB.
RefSeq NP_031959.1; -.
UniGene Mm.251322
3D structure databases
HSSP P56252; 1PDZ. [HSSP ENTRY / PDB]
SMR P21550; 2-431.
ModBase P21550.
PTM databases
PhosphoSite P21550; -.
2D gel databases
SWISS-2DPAGE P21550; -.
Organism-specific databases
MGI MGI:95395; Eno3.
Gene expression databases
ArrayExpress P21550; -.
CleanEx MM_ENO3; -.
GermOnline ENSMUSG00000060600; Mus musculus.
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 P21550.
Genome annotation databases
Ensembl ENSMUSG00000060600; Mus musculus. [Contig view]
GeneID 13808; -.
KEGG mmu:13808; -.
Phylogenomic databases
HOGENOM P21550; -.
HOVERGEN P21550; -.
Other
LinkHub P21550; -.
SOURCE Eno3; Mus musculus.
ProtoNet P21550.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   434  433     Beta-enolase. PRO_0000134108
REGION   370   373  4     Substrate binding (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). 
CONFLICT   234   235        AG -> NA (in Ref. 6; AAA37554). 
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 47025 Da [This is the MW of the unprocessed precursor] CRC64: A1F757D83709D2B8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKARYLGK 

        70         80         90        100        110        120 
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 

       190        200        210        220        230        240 
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 

       250        260        270        280        290        300 
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AVFAGRKFRN PKAK 

P21550 in FASTA format

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