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Beta-enolase (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)

 ENOB_RAT                Reviewed;         434 AA.
P15429; Q5XIV3;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
26-FEB-2020, entry version 169.
RecName: Full=Beta-enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=Enolase 3;
AltName: Full=Muscle-specific enolase;
Short=MSE;
AltName: Full=Skeletal muscle enolase;
Name=Eno3; Synonyms=Eno-3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Skeletal muscle;
PubMed=2914621; DOI=10.1016/0014-5793(89)80515-0;
Ohshima Y., Mitsui H., Takayama Y., Kushiya E., Sakimura K., Takahashi Y.;
"cDNA cloning and nucleotide sequence of rat muscle-specific enolase (beta
beta enolase).";
FEBS Lett. 242:425-430(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
PubMed=2269373; DOI=10.1016/0014-5793(90)80813-x;
Sakimura K., Kushiya E., Ohshima-Ichimura Y., Mitsui H., Takahashi Y.;
"Structure and expression of rat muscle-specific enolase gene.";
FEBS Lett. 277:78-82(1990).
[4]
PROTEIN SEQUENCE OF 10-28; 33-50; 106-120; 240-253; 257-262; 336-394 AND
407-412, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[5]
DEVELOPMENTAL STAGE.
PubMed=8594891; DOI=10.1152/ajpheart.1995.269.6.h1843;
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).
[6]
EFFECT OF THYROID HORMONES ON EXPRESSION.
PubMed=10662718; DOI=10.1152/ajpendo.2000.278.2.e330;
Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L.,
Rappaport L., Lamande N., Lucas M.;
"Thyroid hormones differentially modulate enolase isozymes during rat
skeletal and cardiac muscle development.";
Am. J. Physiol. 278:E330-E339(2000).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-83; SER-157; THR-205;
THR-229; TYR-236 AND SER-263, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Appears to have a function in striated muscle development and
regeneration.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Mg(2+) is 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. Interacts with PNKD (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q5VU43-11:PDE4DIP (xeno); NbExp=2; IntAct=EBI-10817548, EBI-10769071;
-!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some
colocalization with CKM at M-band (By similarity). {ECO:0000250}.
-!- 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.
-!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
cells. {ECO:0000269|PubMed:8594891}.
-!- INDUCTION: Thyroid hormones up-regulate expression during hindleg
muscle development and down-regulate during cardiac muscle development.
Decrease in ENO3 levels with aortic stenosis.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
---------------------------------------------------------------------------
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---------------------------------------------------------------------------
EMBL; Y00979; CAA68788.1; -; mRNA.
EMBL; BC083566; AAH83566.1; -; mRNA.
EMBL; X57774; CAA40920.1; -; Genomic_DNA.
PIR; S02072; S02072.
RefSeq; NP_037081.2; NM_012949.2.
RefSeq; XP_006246661.1; XM_006246599.3.
RefSeq; XP_006246662.1; XM_006246600.3.
SMR; P15429; -.
BioGrid; 247473; 1.
IntAct; P15429; 1.
STRING; 10116.ENSRNOP00000005612; -.
iPTMnet; P15429; -.
PhosphoSitePlus; P15429; -.
SwissPalm; P15429; -.
jPOST; P15429; -.
PaxDb; P15429; -.
PRIDE; P15429; -.
Ensembl; ENSRNOT00000005612; ENSRNOP00000005612; ENSRNOG00000004078.
GeneID; 25438; -.
KEGG; rno:25438; -.
UCSC; RGD:2555; rat.
CTD; 2027; -.
RGD; 2555; Eno3.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
GeneTree; ENSGT00950000182805; -.
HOGENOM; CLU_031223_0_0_1; -.
InParanoid; P15429; -.
KO; K01689; -.
OMA; QEFLVVP; -.
OrthoDB; 773373at2759; -.
PhylomeDB; P15429; -.
TreeFam; TF300391; -.
Reactome; R-RNO-70171; Glycolysis.
Reactome; R-RNO-70263; Gluconeogenesis.
UniPathway; UPA00109; UER00187.
PRO; PR:P15429; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000004078; Expressed in skeletal muscle tissue and 8 other tissues.
Genevisible; P15429; RN.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:RGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P13929"
CHAIN 2..434
/note="Beta-enolase"
/id="PRO_0000134110"
REGION 370..373
/note="Substrate binding"
/evidence="ECO:0000250"
ACT_SITE 210
/note="Proton donor"
/evidence="ECO:0000250"
ACT_SITE 343
/note="Proton acceptor"
/evidence="ECO:0000250"
METAL 245
/note="Magnesium"
/evidence="ECO:0000250"
METAL 293
/note="Magnesium"
/evidence="ECO:0000250"
METAL 318
/note="Magnesium"
/evidence="ECO:0000250"
BINDING 158
/note="Substrate"
/evidence="ECO:0000250"
BINDING 167
/note="Substrate"
/evidence="ECO:0000250"
BINDING 293
/note="Substrate"
/evidence="ECO:0000250"
BINDING 318
/note="Substrate"
/evidence="ECO:0000250"
BINDING 394
/note="Substrate"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000250|UniProtKB:P13929"
MOD_RES 72
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 83
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 157
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 176
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P13929"
MOD_RES 205
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 229
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 236
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 263
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:22673903"
CONFLICT 63
/note="L -> P (in Ref. 1; CAA68788)"
/evidence="ECO:0000305"
CONFLICT 176..182
/note="SSFKEAM -> KLFQGSQ (in Ref. 1; CAA68788)"
/evidence="ECO:0000305"
CONFLICT 279
/note="L -> P (in Ref. 1; CAA68788)"
/evidence="ECO:0000305"
CONFLICT 355
/note="Q -> L (in Ref. 1; CAA68788)"
/evidence="ECO:0000305"
CONFLICT 381
/note="I -> V (in Ref. 1; CAA68788)"
/evidence="ECO:0000305"
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


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