Gamma-enolase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P07323 (ENOG_RAT)

Last modified February 9, 2010. Version 106. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Gamma-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Neural enolase
    Neuron-specific enolase
      Short name=NSE
    Enolase 2

Gene names

Name:	Eno2
Synonyms:	Eno-2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. Ref.6
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. Ref.7
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. ENO2 levels in brain increase 10-30 days after birth. Levels continue to accumulate over the following few months (protein only).
Sequence similarities	Belongs to the enolase family.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from direct assay. Source: RGD glycolysis Inferred from direct assay. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to estradiol stimulus Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.7 Inferred from direct assay. Source: RGD synaptosome Ref.7 Inferred from direct assay. Source: RGD
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.1 Ref.7 Inferred from direct assay. Source: RGD protein heterodimerization activity Ref.7 Inferred from direct assay. Source: RGD protein homodimerization activity Ref.7 Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 434

433

Gamma-enolase

PRO_0000134114

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 By similarity

Modified residue

Phosphoserine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P07323-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BAFFCE2F04BCCA45
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FASTA

434

47,141

        10         20         30         40         50         60 
MSIQKIWARE ILDSRGNPTV EVDLHTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK 

        70         80         90        100        110        120 
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKDLPL 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 FKSPADPSRC 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 MRIEEELGEE 

       430 
ARFAGHNFRN PSVL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2865729] [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: 3746946] [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: 15489334] [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: 2450052] [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, 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: 7753500] [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: 15041191] [Abstract] Cited for: SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00326412.
PIR	A24742. JC1039.
RefSeq	NP_647541.1.
UniGene	Rn.10828
3D structure databases
SMR	P07323. Positions 2-434.
ModBase	Search...
Protein-protein interaction databases
STRING	P07323.
PTM databases
PhosphoSite	P07323.
Proteomic databases
PRIDE	P07323.
Genome annotation databases
Ensembl	ENSRNOT00000005601; ENSRNOP00000005601; ENSRNOG00000013141; Rattus norvegicus. [Genome view]
GeneID	24334.
KEGG	rno:24334.
NMPDR	fig\|10116.3.peg.22203.
UCSC	NM_139325. rat.
Organism-specific databases
CTD	24334.
RGD	2554. Eno2.
Phylogenomic databases
eggNOG	roNOG10078.
HOVERGEN	P07323.
InParanoid	P07323.
OMA	RDAMRIG.
PhylomeDB	P07323.
Enzyme and pathway databases
BRENDA	4.2.1.11. 248.
Gene expression databases
ArrayExpress	P07323.
Genevestigator	P07323.
GermOnline	ENSRNOG00000013141. Rattus norvegicus.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
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 Resources
NextBio	603019.

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Entry information

Entry name

ENOG_RAT

Accession

Primary (citable) accession number: P07323

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents