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Protein

Alpha-enolase

Gene

ENO1

Organism
Bos taurus (Bovine)
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. 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 similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer.By similarity

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, testis-specific (GAPDHS)
  2. Phosphoglycerate kinase 1 (PGK1)
  3. no protein annotated in this organism
  4. Beta-enolase (ENO3), Alpha-enolase (ENO1)
  5. Pyruvate kinase (PKM2), Pyruvate kinase (PKLR), Pyruvate kinase (PKM2)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis, Plasminogen activation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKQ9XSJ4.
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
HAP47
Non-neural enolase
Short name:
NNE
Phosphopyruvate hydratase
Gene namesi
Name:ENO1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Protein family/group databases

Allergomei11909. Bos d Enolase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001340962 – 434Alpha-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei5N6-acetyllysineBy similarity1
Modified residuei44PhosphotyrosineBy similarity1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei64N6-acetyllysineBy similarity1
Modified residuei71N6-acetyllysineBy similarity1
Modified residuei89N6-acetyllysine; alternateBy similarity1
Modified residuei89N6-succinyllysine; alternateBy similarity1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei193N6-acetyllysineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei202N6-acetyllysineBy similarity1
Modified residuei228N6-acetyllysine; alternateBy similarity1
Modified residuei228N6-succinyllysine; alternateBy similarity1
Modified residuei233N6-acetyllysine; alternateBy similarity1
Modified residuei233N6-malonyllysine; alternateBy similarity1
Modified residuei254PhosphoserineBy similarity1
Modified residuei256N6-acetyllysineBy similarity1
Modified residuei263PhosphoserineBy similarity1
Modified residuei281N6-acetyllysineBy similarity1
Modified residuei287PhosphotyrosineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei335N6-acetyllysineBy similarity1
Modified residuei343N6-acetyllysineBy similarity1
Modified residuei406N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysine; alternateBy similarity1
Modified residuei420N6-malonyllysine; alternateBy similarity1
Modified residuei420N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9XSJ4.
PeptideAtlasiQ9XSJ4.
PRIDEiQ9XSJ4.

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, and to the alpha/gamma heterodimer in nerve cells.

Inductioni

Expression increased up to 3-fold by hypoxic stress in vascular endothelial cells.

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. Interacts with ENO4 and PGAM2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017839.

Structurei

3D structure databases

ProteinModelPortaliQ9XSJ4.
SMRiQ9XSJ4.
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.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiQ9XSJ4.
KOiK01689.

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.

Q9XSJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILKVHARE IFDSRGNPTV EVDLFTAKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DKLMIEMDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN AEVILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAENFRE AMRIGAEVYH NLKNVIKEKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN KEALELLKNA IGKAGYSDKV VIGMDVAASE
260 270 280 290 300
FYRSGKYDLD FKSPDDPSRY ITPDELANLY KSFIRDYPVV SIEDPFDQDD
310 320 330 340 350
WEAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVSEKSCNCL LLKVNQIGSV
360 370 380 390 400
TESLQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTVAPCR
410 420 430
SERLAKYNQI LRIEEELGSK AKFAGRSFRN PLAK
Length:434
Mass (Da):47,326
Last modified:January 23, 2007 - v4
Checksum:i91E2A06F073C5121
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82L → S in AAD33073 (Ref. 1) Curated1
Sequence conflicti102N → K in AAD33073 (Ref. 1) Curated1
Sequence conflicti324N → T in AAD33073 (Ref. 1) Curated1
Sequence conflicti327R → T in AAD33073 (Ref. 1) Curated1
Sequence conflicti331 – 333AVS → GVN in AAD33073 (Ref. 1) Curated3
Sequence conflicti347I → N in AAD33073 (Ref. 1) Curated1
Sequence conflicti356A → G in AAD33073 (Ref. 1) Curated1
Sequence conflicti361 – 362QS → HA in AAD33073 (Ref. 1) Curated2
Sequence conflicti377E → D in AAD33073 (Ref. 1) Curated1
Sequence conflicti383D → E in AAD33073 (Ref. 1) Curated1
Sequence conflicti395 – 397TVA → NGP in AAD33073 (Ref. 1) Curated3
Sequence conflicti401S → T in AAD33073 (Ref. 1) Curated1
Sequence conflicti427S → N in AAD33073 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149256 mRNA. Translation: AAD33073.1.
BC103354 mRNA. Translation: AAI03355.1.
RefSeqiNP_776474.2. NM_174049.2.
UniGeneiBt.22783.

Genome annotation databases

GeneIDi281141.
KEGGibta:281141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149256 mRNA. Translation: AAD33073.1.
BC103354 mRNA. Translation: AAI03355.1.
RefSeqiNP_776474.2. NM_174049.2.
UniGeneiBt.22783.

3D structure databases

ProteinModelPortaliQ9XSJ4.
SMRiQ9XSJ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017839.

Protein family/group databases

Allergomei11909. Bos d Enolase.

Proteomic databases

PaxDbiQ9XSJ4.
PeptideAtlasiQ9XSJ4.
PRIDEiQ9XSJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281141.
KEGGibta:281141.

Organism-specific databases

CTDi2023.

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiQ9XSJ4.
KOiK01689.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
SABIO-RKQ9XSJ4.

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_BOVIN
AccessioniPrimary (citable) accession number: Q9XSJ4
Secondary accession number(s): Q3SYW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 129 of the entry and version 4 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.