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P17183 (ENOG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 2
Neural enolase
Neuron-specific enolase
Short name=NSE
Gene names
Name:Eno2
Synonyms:Eno-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival By similarity. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subunit structure

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.

Subcellular location

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 By similarity. HAMAP-Rule MF_00318

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, and to the alpha/gamma heterodimer in nerve cells. HAMAP-Rule MF_00318

Sequence similarities

Belongs to the enolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Gamma-enolase HAMAP-Rule MF_00318
PRO_0000134113

Regions

Region370 – 3734Substrate binding By similarity

Sites

Active site2101Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2451Magnesium By similarity
Metal binding2931Magnesium By similarity
Metal binding3181Magnesium By similarity
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2931Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue261Phosphothreonine By similarity
Modified residue441Phosphotyrosine By similarity
Modified residue1971N6-acetyllysine Ref.5
Modified residue1991N6-acetyllysine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P17183 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A5C7F189E913392E

FASTA43447,297
        10         20         30         40         50         60 
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK 

        70         80         90        100        110        120 
GVLKAVDHIN SRIAPALISS GISVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAERDLPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD 

       190        200        210        220        230        240 
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM 

       250        260        270        280        290        300 
VIGMDVAASE FYRDGKYDLD FKSPADPSRY ITGDQLGALY QDFVRNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA 

       370        380        390        400        410        420 
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE 

       430 
ARFAGHNFRN PSVL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse brain."
Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M., Lazar M., Caput D.
Nucleic Acids Res. 18:3638-3638(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.
Genome Res. 8:29-40(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Retina.
[4]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 16-28; 33-50; 73-89; 104-120; 163-179; 184-193; 203-228; 240-262; 270-285; 307-326; 336-358; 373-394 AND 413-429, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197 AND LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52380 mRNA. Translation: CAA36606.1.
AC002397 Genomic DNA. Translation: AAC36002.1.
BC031739 mRNA. Translation: AAH31739.1.
PIRS10247.
RefSeqNP_038537.1. NM_013509.2.
XP_006505566.1. XM_006505503.1.
XP_006505567.1. XM_006505504.1.
UniGeneMm.3913.

3D structure databases

ProteinModelPortalP17183.
SMRP17183. Positions 2-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP17183. 3 interactions.
MINTMINT-4094426.

PTM databases

PhosphoSiteP17183.

2D gel databases

UCD-2DPAGEP17183.

Proteomic databases

PaxDbP17183.
PRIDEP17183.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
GeneID13807.
KEGGmmu:13807.
UCSCuc009drs.1. mouse.

Organism-specific databases

CTD2026.
MGIMGI:95394. Eno2.

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
HOVERGENHBG000067.
InParanoidP17183.
KOK01689.
OMAKNEGVER.
PhylomeDBP17183.
TreeFamTF300391.

Enzyme and pathway databases

SABIO-RKP17183.
UniPathwayUPA00109; UER00187.

Gene expression databases

ArrayExpressP17183.
BgeeP17183.
CleanExMM_ENO2.
GenevestigatorP17183.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284588.
PROP17183.
SOURCESearch...

Entry information

Entry nameENOG_MOUSE
AccessionPrimary (citable) accession number: P17183
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot