ENOB_RAT
ID ENOB_RAT Reviewed; 434 AA.
AC P15429; Q5XIV3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Beta-enolase;
DE EC=4.2.1.11 {ECO:0000269|PubMed:8594891};
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Skeletal muscle;
RX PubMed=2914621; DOI=10.1016/0014-5793(89)80515-0;
RA Ohshima Y., Mitsui H., Takayama Y., Kushiya E., Sakimura K., Takahashi Y.;
RT "cDNA cloning and nucleotide sequence of rat muscle-specific enolase (beta
RT beta enolase).";
RL FEBS Lett. 242:425-430(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=2269373; DOI=10.1016/0014-5793(90)80813-x;
RA Sakimura K., Kushiya E., Ohshima-Ichimura Y., Mitsui H., Takahashi Y.;
RT "Structure and expression of rat muscle-specific enolase gene.";
RL FEBS Lett. 277:78-82(1990).
RN [4]
RP PROTEIN SEQUENCE OF 10-28; 33-50; 106-120; 240-253; 257-262; 336-394 AND
RP 407-412, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, AND FUNCTION.
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 [6]
RP EFFECT OF THYROID HORMONES ON EXPRESSION.
RX PubMed=10662718; DOI=10.1152/ajpendo.2000.278.2.e330;
RA Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L.,
RA Rappaport L., Lamande N., Lucas M.;
RT "Thyroid hormones differentially modulate enolase isozymes during rat
RT skeletal and cardiac muscle development.";
RL Am. J. Physiol. 278:E330-E339(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-83; SER-157; THR-205;
RP THR-229; TYR-236 AND SER-263, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:8594891}.
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:0000269|PubMed:8594891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000305|PubMed:8594891};
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:0000305|PubMed:8594891}.
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. Interacts with PNKD (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P15429; Q5VU43-11: PDE4DIP; Xeno; NbExp=2; IntAct=EBI-10817548, EBI-10769071;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some
CC colocalization with CKM at M-band (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo
CC and in most adult tissues. The alpha/beta heterodimer and the beta/beta
CC homodimer are found in striated muscle, and the alpha/gamma heterodimer
CC and the gamma/gamma homodimer in neurons.
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. {ECO:0000269|PubMed:8594891}.
CC -!- INDUCTION: Thyroid hormones up-regulate expression during hindleg
CC muscle development and down-regulate during cardiac muscle development.
CC Decrease in ENO3 levels with aortic stenosis.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; Y00979; CAA68788.1; -; mRNA.
DR EMBL; BC083566; AAH83566.1; -; mRNA.
DR EMBL; X57774; CAA40920.1; -; Genomic_DNA.
DR PIR; S02072; S02072.
DR RefSeq; NP_037081.2; NM_012949.2.
DR RefSeq; XP_006246661.1; XM_006246599.3.
DR RefSeq; XP_006246662.1; XM_006246600.3.
DR AlphaFoldDB; P15429; -.
DR SMR; P15429; -.
DR BioGRID; 247473; 2.
DR IntAct; P15429; 1.
DR STRING; 10116.ENSRNOP00000005612; -.
DR iPTMnet; P15429; -.
DR PhosphoSitePlus; P15429; -.
DR SwissPalm; P15429; -.
DR jPOST; P15429; -.
DR PaxDb; P15429; -.
DR PRIDE; P15429; -.
DR Ensembl; ENSRNOT00000005612; ENSRNOP00000005612; ENSRNOG00000004078.
DR GeneID; 25438; -.
DR KEGG; rno:25438; -.
DR UCSC; RGD:2555; rat.
DR CTD; 2027; -.
DR RGD; 2555; Eno3.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P15429; -.
DR OMA; KHADNGI; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P15429; -.
DR TreeFam; TF300391; -.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P15429; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004078; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; P15429; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0061621; P:canonical glycolysis; ISO:RGD.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
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_0000134110"
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:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 63
FT /note="L -> P (in Ref. 1; CAA68788)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..182
FT /note="SSFKEAM -> KLFQGSQ (in Ref. 1; CAA68788)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="L -> P (in Ref. 1; CAA68788)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Q -> L (in Ref. 1; CAA68788)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="I -> V (in Ref. 1; CAA68788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47014 MW; 136A5300E052D5A7 CRC64;
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKSRYLGK
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KSFIKNYPVV SIEDPFDQDD
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
AVFAGRKFRN PKAK
