Gamma-enolase - Mus musculus (Mouse)

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P17183 (ENOG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 130. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Eno2
Synonyms:	Eno-2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
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.
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.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from direct assay PubMed 9758704. Source: MGI perikaryon Inferred from direct assay PubMed 9671661. Source: MGI phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro photoreceptor inner segment Inferred from direct assay PubMed 9364238. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 434

434

Gamma-enolase

PRO_0000134113

Regions

Region

370 – 373

Substrate binding By similarity

Sites

Active site

210

Proton donor By similarity

Active site

343

Proton acceptor By similarity

Metal binding

245

Magnesium By similarity

Metal binding

293

Magnesium By similarity

Metal binding

318

Magnesium By similarity

Binding site

158

Substrate By similarity

Binding site

167

Substrate By similarity

Binding site

293

Substrate By similarity

Binding site

318

Substrate By similarity

Binding site

394

Substrate By similarity

Amino acid modifications

Modified residue

Phosphotyrosine Ref.6 Ref.7

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine Ref.6 Ref.7

Modified residue

Phosphoserine Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P17183 [UniParc].

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

434

47,297

        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' referencesShow '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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[5]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, MASS SPECTROMETRY. Tissue: Mast cell.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, MASS SPECTROMETRY. Tissue: Brain.
+	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.
IPI	IPI00331704.
PIR	S10247.
RefSeq	NP_038537.1. NM_013509.2.
UniGene	Mm.3913.
3D structure databases
ProteinModelPortal	P17183.
SMR	P17183. Positions 2-434.
ModBase	Search...
Protein-protein interaction databases
IntAct	P17183. 2 interactions.
PTM databases
PhosphoSite	P17183.
2D gel databases
UCD-2DPAGE	P17183.
Proteomic databases
PaxDb	P17183.
PRIDE	P17183.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
GeneID	13807.
KEGG	mmu:13807.
Organism-specific databases
CTD	2026.
MGI	MGI:95394. Eno2.
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HOG000072174.
HOVERGEN	HBG000067.
InParanoid	P17183.
KO	K01689.
OMA	QAVDHIN.
OrthoDB	EOG4T783B.
Enzyme and pathway databases
SABIO-RK	P17183.
UniPathway	UPA00109; UER00187.
Gene expression databases
ArrayExpress	P17183.
Bgee	P17183.
CleanEx	MM_ENO2.
Genevestigator	P17183.
GermOnline	ENSMUSG00000004267. Mus musculus.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. PTHR11902. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284588.
SOURCE	Search...

Entry information

Entry name

ENOG_MOUSE

Accession

Primary (citable) accession number: P17183

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents