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Protein

Alpha-enolase

Gene

Eno1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses (By similarity). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+Note: Binds two Mg2+ per subunit. 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 (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (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)DescriptionActionsGraphical viewLength
Metal bindingi40Magnesium 1By similarity1
Binding sitei158SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Active sitei210Proton donorBy similarity1
Metal bindingi245Magnesium 2By similarity1
Metal bindingi293Magnesium 2By similarity1
Binding sitei293SubstrateBy similarity1
Metal bindingi318Magnesium 2By similarity1
Binding sitei318SubstrateBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei394SubstrateBy similarity1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: MGI
  • GTPase binding Source: MGI
  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: MGI
  • poly(A) RNA binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • RNA binding Source: MGI

GO - Biological processi

  • glycolytic process Source: MGI
  • in utero embryonic development Source: MGI
  • positive regulation of binding Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.11. 3474.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP17182.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 1
Non-neural enolase
Short name:
NNE
Gene namesi
Name:Eno1
Synonyms:Eno-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 18, Chromosome 4

Organism-specific databases

MGIiMGI:95393. Eno1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001340982 – 434Alpha-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei44PhosphotyrosineCombined sources1
Modified residuei60N6-acetyllysine; alternateCombined sources1
Modified residuei60N6-succinyllysine; alternateCombined sources1
Modified residuei71N6-acetyllysineBy similarity1
Modified residuei89N6-acetyllysine; alternateCombined sources1
Modified residuei89N6-succinyllysine; alternateCombined sources1
Modified residuei92N6-acetyllysineCombined sources1
Modified residuei126N6-acetyllysineCombined sources1
Modified residuei193N6-acetyllysineCombined sources1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei202N6-acetyllysineCombined sources1
Modified residuei228N6-acetyllysine; alternateCombined sources1
Modified residuei228N6-succinyllysine; alternateCombined sources1
Modified residuei233N6-acetyllysine; alternateBy similarity1
Modified residuei233N6-malonyllysine; alternateBy similarity1
Modified residuei254PhosphoserineBy similarity1
Modified residuei256N6-acetyllysineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei281N6-acetyllysineBy similarity1
Modified residuei287PhosphotyrosineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei335N6-acetyllysineCombined sources1
Modified residuei343N6-acetyllysineCombined sources1
Modified residuei406N6-acetyllysineCombined sources1
Modified residuei420N6-acetyllysine; alternateBy similarity1
Modified residuei420N6-malonyllysine; alternateBy similarity1
Modified residuei420N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17182.
PaxDbiP17182.
PeptideAtlasiP17182.
PRIDEiP17182.

2D gel databases

REPRODUCTION-2DPAGEIPI00462072.
P17182.
SWISS-2DPAGEP17182.
UCD-2DPAGEP17182.

PTM databases

iPTMnetiP17182.
PhosphoSitePlusiP17182.
SwissPalmiP17182.

Expressioni

Tissue specificityi

Testis. Found in the principal piece of sperm tail (at protein level). 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, expression of ENO1 appears to be independent of fiber type.2 Publications

Developmental stagei

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 embryonic muscle, ENO1 is highly expressed until E17. Decreased levels from P5.1 Publication

Gene expression databases

BgeeiENSMUSG00000059040.
ExpressionAtlasiP17182. baseline and differential.
GenevisibleiP17182. MM.

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. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (By similarity). In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and aldolase (PubMed:9169614). Also binds troponin, in vitro (PubMed:9169614). Interacts with ENO4 and PGAM2 (PubMed:23446454).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199451. 13 interactors.
241069. 2 interactors.
IntActiP17182. 14 interactors.
MINTiMINT-4996502.
STRINGi10090.ENSMUSP00000079727.

Structurei

3D structure databases

ProteinModelPortaliP17182.
SMRiP17182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate bindingBy similarity4
Regioni405 – 434Required for interaction with PLGBy similarityAdd BLAST30

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17182.
KOiK01689.
OMAiNFRNPRI.
OrthoDBiEOG091G07NH.
PhylomeDBiP17182.
TreeFamiTF300391.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
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.

P17182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DNDKTRFMGK GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN PEVILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGASSFRE AMRIGAEVYH NLKNVIKEKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV VIGMDVAASE
260 270 280 290 300
FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD
310 320 330 340 350
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV
360 370 380 390 400
TESLQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQI LRIEEELGSK AKFAGRSFRN PLAK
Length:434
Mass (Da):47,141
Last modified:January 23, 2007 - v3
Checksum:iDBEF6270A70DE3A6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti359L → P in CAA36605 (PubMed:2362815).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52379 mRNA. Translation: CAA36605.1.
AK002336 mRNA. Translation: BAB22021.1.
BC003891 mRNA. Translation: AAH03891.1.
BC004017 mRNA. Translation: AAH04017.1.
BC010685 mRNA. Translation: AAH10685.1.
BC024644 mRNA. Translation: AAH24644.1.
BC085098 mRNA. Translation: AAH85098.1.
CCDSiCCDS18971.1.
PIRiS10246.
RefSeqiNP_001020559.1. NM_001025388.1.
NP_075608.2. NM_023119.2.
XP_006538588.2. XM_006538525.2.
UniGeneiMm.372357.
Mm.372389.
Mm.70666.

Genome annotation databases

EnsembliENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
GeneIDi13806.
433182.
KEGGimmu:13806.
mmu:433182.
UCSCiuc008ewh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52379 mRNA. Translation: CAA36605.1.
AK002336 mRNA. Translation: BAB22021.1.
BC003891 mRNA. Translation: AAH03891.1.
BC004017 mRNA. Translation: AAH04017.1.
BC010685 mRNA. Translation: AAH10685.1.
BC024644 mRNA. Translation: AAH24644.1.
BC085098 mRNA. Translation: AAH85098.1.
CCDSiCCDS18971.1.
PIRiS10246.
RefSeqiNP_001020559.1. NM_001025388.1.
NP_075608.2. NM_023119.2.
XP_006538588.2. XM_006538525.2.
UniGeneiMm.372357.
Mm.372389.
Mm.70666.

3D structure databases

ProteinModelPortaliP17182.
SMRiP17182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199451. 13 interactors.
241069. 2 interactors.
IntActiP17182. 14 interactors.
MINTiMINT-4996502.
STRINGi10090.ENSMUSP00000079727.

PTM databases

iPTMnetiP17182.
PhosphoSitePlusiP17182.
SwissPalmiP17182.

2D gel databases

REPRODUCTION-2DPAGEIPI00462072.
P17182.
SWISS-2DPAGEP17182.
UCD-2DPAGEP17182.

Proteomic databases

EPDiP17182.
PaxDbiP17182.
PeptideAtlasiP17182.
PRIDEiP17182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
GeneIDi13806.
433182.
KEGGimmu:13806.
mmu:433182.
UCSCiuc008ewh.1. mouse.

Organism-specific databases

CTDi2023.
433182.
MGIiMGI:95393. Eno1.

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17182.
KOiK01689.
OMAiNFRNPRI.
OrthoDBiEOG091G07NH.
PhylomeDBiP17182.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BRENDAi4.2.1.11. 3474.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP17182.

Miscellaneous databases

PROiP17182.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000059040.
ExpressionAtlasiP17182. baseline and differential.
GenevisibleiP17182. MM.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
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...

Entry informationi

Entry nameiENOA_MOUSE
AccessioniPrimary (citable) accession number: P17182
Secondary accession number(s): Q99KT7, Q9DCY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 179 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.