ENOB_MOUSE
ID ENOB_MOUSE Reviewed; 434 AA.
AC P21550;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Beta-enolase;
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P15429};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 3;
DE AltName: Full=Muscle-specific enolase;
DE Short=MSE;
DE AltName: Full=Skeletal muscle enolase;
GN Name=Eno3; Synonyms=Eno-3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ, and Swiss Webster; TISSUE=Liver, and Skeletal muscle;
RA Lamande N., Brosset S., Keller A., Lucas M., Lazar M.;
RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RX PubMed=1339335; DOI=10.1016/0012-1606(92)90201-q;
RA Peterson C.A., Cho M., Rastinejad F., Blau H.M.;
RT "Beta-enolase is a marker of human myoblast heterogeneity prior to
RT differentiation.";
RL Dev. Biol. 151:626-629(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
RX PubMed=2734297; DOI=10.1073/pnas.86.12.4445;
RA Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F.,
RA Legault-Demare L., Lazar M.;
RT "Murine muscle-specific enolase: cDNA cloning, sequence, and developmental
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989).
RN [7]
RP ACTIVATION DURING MYOGENESIS.
RX PubMed=1525038; DOI=10.1016/0925-4773(92)90037-k;
RA Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M.,
RA Lazar M.;
RT "Activation of the gene encoding the glycolytic enzyme beta-enolase during
RT early myogenesis precedes an increased expression during fetal muscle
RT development.";
RL Mech. Dev. 38:41-54(1992).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=8594891; DOI=10.1152/ajpheart.1995.269.6.h1843;
RA Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F.,
RA Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.;
RT "Differential expression of alpha- and beta-enolase genes during rat heart
RT development and hypertrophy.";
RL Am. J. Physiol. 269:H1843-H1851(1995).
RN [9]
RP INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, AND DEVELOPMENTAL STAGE.
RX PubMed=9169614; DOI=10.1042/bj3230791;
RA Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F.,
RA Lazar M., Keller A.;
RT "Biochemical characterization of the mouse muscle-specific enolase:
RT developmental changes in electrophoretic variants and selective binding to
RT other proteins.";
RL Biochem. J. 323:791-800(1997).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11229603; DOI=10.1016/s0248-4900(00)01103-5;
RA Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C.,
RA Lucas M., Chatelet F.-P.;
RT "Fibre-type distribution and subcellular localisation of alpha and beta
RT enolase in mouse striated muscle.";
RL Biol. Cell 92:527-535(2000).
RN [11]
RP EXPRESSION REGULATION.
RX PubMed=10848992; DOI=10.1046/j.1432-1327.2000.01408.x;
RA Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H.,
RA Keller A.;
RT "Differential modulation of alpha, beta and gamma enolase isoforms in
RT regenerating mouse skeletal muscle.";
RL Eur. J. Biochem. 267:3735-3743(2000).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=23446454; DOI=10.1095/biolreprod.112.107128;
RA Nakamura N., Dai Q., Williams J., Goulding E.H., Willis W.D., Brown P.R.,
RA Eddy E.M.;
RT "Disruption of a spermatogenic cell-specific mouse enolase 4 (eno4) gene
RT causes sperm structural defects and male infertility.";
RL Biol. Reprod. 88:90-90(2013).
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. Appears to have a function in
CC striated muscle development and regeneration.
CC {ECO:0000250|UniProtKB:P15429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P15429}.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
CC beta and gamma, which can form homodimers or heterodimers which are
CC cell-type and development-specific. In vitro, interacts with several
CC glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and
CC troponin, in vitro. Interacts with PNKD (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11229603}.
CC Note=Localized to the Z line. Some colocalization with CKM at M-band
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain (at protein level). The alpha/alpha homodimer
CC is expressed in embryo and in most adult tissues. The alpha/beta
CC heterodimer and the beta/beta homodimer are found in striated muscle,
CC and the alpha/gamma heterodimer and the gamma/gamma homodimer in
CC neurons. In striated muscle, the fiber-type order of ENO3 expression is
CC IIB > IIX > IIA > I. {ECO:0000269|PubMed:11229603,
CC ECO:0000269|PubMed:23446454}.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
CC alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
CC cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg
CC muscle, first expressed at 15 dpc after which, levels increase sharply
CC between 15 dpc and 17 dpc. A steep prenatal rise in expression
CC accompanies the formation of secondary myofibers and the development of
CC innervation. High levels continue throughout newborn and adult stages.
CC Beginning at postnatal day 5, a second sharp increase in expression
CC correlates with the definitive specialization of the myofibers. Later
CC in development, mainly expressed in fast-twitch fibers. In cardiac
CC muscle, first expressed in the embryo in the cardiac tube.
CC {ECO:0000269|PubMed:8594891, ECO:0000269|PubMed:9169614}.
CC -!- INDUCTION: Levels decrease in degenerating myofibers, and increase with
CC their regeneration.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; X61600; CAA43797.1; -; Genomic_DNA.
DR EMBL; X57747; CAA40913.1; -; mRNA.
DR EMBL; X62667; CAA44540.1; -; mRNA.
DR EMBL; AK002485; BAB22137.1; -; mRNA.
DR EMBL; BC013460; AAH13460.1; -; mRNA.
DR EMBL; M20745; AAA37554.1; -; mRNA.
DR CCDS; CCDS24961.1; -.
DR PIR; S17109; NOMSB.
DR RefSeq; NP_001129534.1; NM_001136062.2.
DR RefSeq; NP_001263214.1; NM_001276285.1.
DR RefSeq; NP_031959.1; NM_007933.3.
DR RefSeq; XP_006532225.1; XM_006532162.3.
DR AlphaFoldDB; P21550; -.
DR SMR; P21550; -.
DR BioGRID; 199453; 26.
DR IntAct; P21550; 14.
DR MINT; P21550; -.
DR STRING; 10090.ENSMUSP00000072620; -.
DR iPTMnet; P21550; -.
DR PhosphoSitePlus; P21550; -.
DR SWISS-2DPAGE; P21550; -.
DR UCD-2DPAGE; P21550; -.
DR CPTAC; non-CPTAC-3791; -.
DR CPTAC; non-CPTAC-3792; -.
DR EPD; P21550; -.
DR jPOST; P21550; -.
DR PaxDb; P21550; -.
DR PeptideAtlas; P21550; -.
DR PRIDE; P21550; -.
DR ProteomicsDB; 277875; -.
DR Antibodypedia; 630; 408 antibodies from 34 providers.
DR DNASU; 13808; -.
DR Ensembl; ENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
DR Ensembl; ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
DR Ensembl; ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
DR GeneID; 13808; -.
DR KEGG; mmu:13808; -.
DR UCSC; uc007jvx.3; mouse.
DR CTD; 2027; -.
DR MGI; MGI:95395; Eno3.
DR VEuPathDB; HostDB:ENSMUSG00000060600; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P21550; -.
DR OMA; XAFNVIN; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P21550; -.
DR TreeFam; TF300391; -.
DR BRENDA; 4.2.1.11; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 13808; 6 hits in 75 CRISPR screens.
DR PRO; PR:P21550; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P21550; protein.
DR Bgee; ENSMUSG00000060600; Expressed in sternocleidomastoid and 257 other tissues.
DR ExpressionAtlas; P21550; baseline and differential.
DR Genevisible; P21550; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IGI:MGI.
DR GO; GO:0006096; P:glycolytic process; ISS:CAFA.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT CHAIN 2..434
FT /note="Beta-enolase"
FT /id="PRO_0000134108"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 234..235
FT /note="AG -> NA (in Ref. 6; AAA37554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47025 MW; A1F757D83709D2B8 CRC64;
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKARYLGK
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
AVFAGRKFRN PKAK
