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Protein

Gamma-enolase

Gene

Eno2

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

Functioni

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.

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

  • gluconeogenesis Source: RGD
  • glycolytic process Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to organic cyclic compound 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:
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 namesi
Name:Eno2
Synonyms:Eno-2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componentsi: Chromosome 4, Chromosome 9

Organism-specific databases

RGDi2554. Eno2.

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.By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • neuron projection Source: RGD
  • phosphopyruvate hydratase complex Source: InterPro
  • synaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 434433Gamma-enolasePRO_0000134114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei44 – 441PhosphotyrosineBy similarity
Modified residuei72 – 721PhosphothreonineBy similarity
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei157 – 1571PhosphoserineBy similarity
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei205 – 2051PhosphothreonineBy similarity
Modified residuei236 – 2361PhosphotyrosineBy similarity
Modified residuei263 – 2631PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07323.
PRIDEiP07323.

2D gel databases

World-2DPAGE0004:P07323.

PTM databases

iPTMnetiP07323.
PhosphoSiteiP07323.

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. ENO2 levels in brain increase 10-30 days after birth. Levels continue to accumulate over the following few months (protein only).

Gene expression databases

GenevisibleiP07323. 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.

GO - Molecular functioni

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005601.

Structurei

3D structure databases

ProteinModelPortaliP07323.
SMRiP07323. Positions 2-434.
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.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP07323.
KOiK01689.
OMAiEAYAGNQ.
OrthoDBiEOG776SQ1.
PhylomeDBiP07323.
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.

P07323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIQKIWARE ILDSRGNPTV EVDLHTAKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKDLPL YRHIAQLAGN SDLILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM VIGMDVAASE
260 270 280 290 300
FYRDGKYDLD FKSPADPSRC ITGDQLGALY QDFVRNYPVV SIEDPFDQDD
310 320 330 340 350
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV
360 370 380 390 400
TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEELGEE ARFAGHNFRN PSVL
Length:434
Mass (Da):47,141
Last modified:January 23, 2007 - v2
Checksum:iBAFFCE2F04BCCA45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11931 mRNA. Translation: AAA41119.1.
M22770 Genomic DNA. Translation: AAA41725.1.
AF019973 mRNA. Translation: AAB72088.1.
BC060310 mRNA. Translation: AAH60310.1.
X07727, X07728, X07729 Genomic DNA. Translation: CAA30556.1.
PIRiA24742.
JC1039.
RefSeqiNP_647541.1. NM_139325.3.
XP_003750705.1. XM_003750657.3.
XP_006237392.1. XM_006237330.2.
XP_006244698.1. XM_006244636.2.
UniGeneiRn.10828.

Genome annotation databases

EnsembliENSRNOT00000005535; ENSRNOP00000005535; ENSRNOG00000048365.
ENSRNOT00000005601; ENSRNOP00000005601; ENSRNOG00000013141.
GeneIDi100911625.
24334.
KEGGirno:100911625.
rno:24334.
UCSCiRGD:2554. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11931 mRNA. Translation: AAA41119.1.
M22770 Genomic DNA. Translation: AAA41725.1.
AF019973 mRNA. Translation: AAB72088.1.
BC060310 mRNA. Translation: AAH60310.1.
X07727, X07728, X07729 Genomic DNA. Translation: CAA30556.1.
PIRiA24742.
JC1039.
RefSeqiNP_647541.1. NM_139325.3.
XP_003750705.1. XM_003750657.3.
XP_006237392.1. XM_006237330.2.
XP_006244698.1. XM_006244636.2.
UniGeneiRn.10828.

3D structure databases

ProteinModelPortaliP07323.
SMRiP07323. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005601.

PTM databases

iPTMnetiP07323.
PhosphoSiteiP07323.

2D gel databases

World-2DPAGE0004:P07323.

Proteomic databases

PaxDbiP07323.
PRIDEiP07323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005535; ENSRNOP00000005535; ENSRNOG00000048365.
ENSRNOT00000005601; ENSRNOP00000005601; ENSRNOG00000013141.
GeneIDi100911625.
24334.
KEGGirno:100911625.
rno:24334.
UCSCiRGD:2554. rat.

Organism-specific databases

CTDi2026.
RGDi2554. Eno2.

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP07323.
KOiK01689.
OMAiEAYAGNQ.
OrthoDBiEOG776SQ1.
PhylomeDBiP07323.
TreeFamiTF300391.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP07323.

Gene expression databases

GenevisibleiP07323. 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. "Molecular cloning and the nucleotide sequence of cDNA for neuron-specific enolase messenger RNA of rat brain."
    Sakimura K., Kushiya E., Obinata M., Odani S., Takahashi Y.
    Proc. Natl. Acad. Sci. U.S.A. 82:7453-7457(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Neuron-specific enolase: complete structure of rat mRNA, multiple transcriptional start sites, and evidence suggesting post-transcriptional control."
    Forss-Petter S., Danielson P., Sutcliffe J.G.
    J. Neurosci. Res. 16:141-156(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  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: Pituitary.
  4. "The structure and expression of neuron-specific enolase gene."
    Sakimura K., Kushiya E., Takahashi Y., Suzuki Y.
    Gene 60:103-113(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 10-28; 32-50; 65-89; 106-120; 163-179; 184-193; 240-262; 270-285; 307-326; 336-394 AND 407-422, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  6. "Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat brain."
    Hattori T., Takei N., Mizuno Y., Kato K., Kohsaka S.
    Neurosci. Res. 21:191-198(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION AS A NEUROTROPHIC FACTOR.
  7. "Localization of enolase in synaptic plasma membrane as an alphagamma heterodimer in rat brain."
    Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H.
    Neurosci. Res. 48:379-386(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
  8. "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 SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENOG_RAT
AccessioniPrimary (citable) accession number: P07323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 157 of the entry and version 2 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.