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Protein

Beta-enolase

Gene

Eno3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to have a function in striated muscle development and regeneration.

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (Gapdh-ps2), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (RGD1562758)
  2. Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Alpha-enolase (Eno1), Beta-enolase (Eno3), Gamma-enolase (Eno2)
  5. Pyruvate kinase PKLR (Pklr), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (LOC100362738), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pkm)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Active sitei210 – 2101Proton donorBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi318 – 3181MagnesiumBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Active sitei343 – 3431Proton acceptorBy similarity
Binding sitei394 – 3941SubstrateBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • glycolytic process Source: UniProtKB-UniPathway
  • response to drug Source: RGD
  • skeletal muscle tissue regeneration Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name:
MSE
Skeletal muscle enolase
Gene namesi
Name:Eno3
Synonyms:Eno-3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2555. Eno3.

Subcellular locationi

  • Cytoplasm

  • Note: Localized to the Z line. Some colocalization with CKM at M-band (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 434433Beta-enolasePRO_0000134110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei44 – 441PhosphotyrosineBy similarity
Modified residuei64 – 641N6-acetyllysineBy similarity
Modified residuei71 – 711N6-acetyllysineBy similarity
Modified residuei72 – 721PhosphothreonineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei193 – 1931N6-acetyllysineBy similarity
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei205 – 2051PhosphothreonineCombined sources
Modified residuei228 – 2281N6-acetyllysineBy similarity
Modified residuei229 – 2291PhosphothreonineCombined sources
Modified residuei236 – 2361PhosphotyrosineCombined sources
Modified residuei256 – 2561N6-acetyllysineBy similarity
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei281 – 2811N6-acetyllysineBy similarity
Modified residuei285 – 2851N6-acetyllysineBy similarity
Modified residuei287 – 2871PhosphotyrosineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei420 – 4201N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP15429.
PRIDEiP15429.

PTM databases

iPTMnetiP15429.
PhosphoSiteiP15429.

Expressioni

Tissue specificityi

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 stagei

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells.1 Publication

Inductioni

Thyroid hormones up-regulate expression during hindleg muscle development and down-regulate during cardiac muscle development. Decrease in ENO3 levels with aortic stenosis.

Gene expression databases

GenevisibleiP15429. RN.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE4DIPQ5VU43-112EBI-10817548,EBI-10769071From a different organism.

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP15429. 1 interaction.
STRINGi10116.ENSRNOP00000005612.

Structurei

3D structure databases

ProteinModelPortaliP15429.
SMRiP15429. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000130007.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP15429.
KOiK01689.
OMAiGASNFHE.
OrthoDBiEOG776SQ1.
PhylomeDBiP15429.
TreeFamiTF300391.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15429-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKSRYLGK GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLVLPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE
260 270 280 290 300
FYRNGKYDLD FKSPDDPARH ISGEKLGELY KSFIKNYPVV SIEDPFDQDD
310 320 330 340 350
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV
360 370 380 390 400
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEALGDK AVFAGRKFRN PKAK
Length:434
Mass (Da):47,014
Last modified:January 23, 2007 - v3
Checksum:i136A5300E052D5A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631L → P in CAA68788 (PubMed:2914621).Curated
Sequence conflicti176 – 1827SSFKEAM → KLFQGSQ in CAA68788 (PubMed:2914621).Curated
Sequence conflicti279 – 2791L → P in CAA68788 (PubMed:2914621).Curated
Sequence conflicti355 – 3551Q → L in CAA68788 (PubMed:2914621).Curated
Sequence conflicti381 – 3811I → V in CAA68788 (PubMed:2914621).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00979 mRNA. Translation: CAA68788.1.
BC083566 mRNA. Translation: AAH83566.1.
X57774 Genomic DNA. Translation: CAA40920.1.
PIRiS02072.
RefSeqiNP_037081.2. NM_012949.2.
XP_006246661.1. XM_006246599.2.
XP_006246662.1. XM_006246600.2.
UniGeneiRn.3443.

Genome annotation databases

EnsembliENSRNOT00000005612; ENSRNOP00000005612; ENSRNOG00000004078.
GeneIDi25438.
KEGGirno:25438.
UCSCiRGD:2555. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00979 mRNA. Translation: CAA68788.1.
BC083566 mRNA. Translation: AAH83566.1.
X57774 Genomic DNA. Translation: CAA40920.1.
PIRiS02072.
RefSeqiNP_037081.2. NM_012949.2.
XP_006246661.1. XM_006246599.2.
XP_006246662.1. XM_006246600.2.
UniGeneiRn.3443.

3D structure databases

ProteinModelPortaliP15429.
SMRiP15429. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15429. 1 interaction.
STRINGi10116.ENSRNOP00000005612.

PTM databases

iPTMnetiP15429.
PhosphoSiteiP15429.

Proteomic databases

PaxDbiP15429.
PRIDEiP15429.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005612; ENSRNOP00000005612; ENSRNOG00000004078.
GeneIDi25438.
KEGGirno:25438.
UCSCiRGD:2555. rat.

Organism-specific databases

CTDi2027.
RGDi2555. Eno3.

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000130007.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP15429.
KOiK01689.
OMAiGASNFHE.
OrthoDBiEOG776SQ1.
PhylomeDBiP15429.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
ReactomeiR-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.

Miscellaneous databases

PROiP15429.

Gene expression databases

GenevisibleiP15429. RN.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and nucleotide sequence of rat muscle-specific enolase (beta beta enolase)."
    Ohshima Y., Mitsui H., Takayama Y., Kushiya E., Sakimura K., Takahashi Y.
    FEBS Lett. 242:425-430(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Skeletal muscle.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  3. "Structure and expression of rat muscle-specific enolase gene."
    Sakimura K., Kushiya E., Ohshima-Ichimura Y., Mitsui H., Takahashi Y.
    FEBS Lett. 277:78-82(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  4. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 10-28; 33-50; 106-120; 240-253; 257-262; 336-394 AND 407-412, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  5. "Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."
    Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.
    Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  6. "Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development."
    Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L., Rappaport L., Lamande N., Lucas M.
    Am. J. Physiol. 278:E330-E339(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECT OF THYROID HORMONES ON EXPRESSION.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-83; SER-157; THR-205; THR-229; TYR-236 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENOB_RAT
AccessioniPrimary (citable) accession number: P15429
Secondary accession number(s): Q5XIV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.