Beta-enolase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P15429 (ENOB_RAT)

Last modified June 16, 2009. Version 83. 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:
    Beta-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Muscle-specific enolase
      Short name=MSE
    Skeletal muscle enolase
    Enolase 3

Gene names

Name:	Eno3
Synonyms:	Eno-3

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	Appears to have a function in striated muscle development and regeneration.
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. Interacts with PNKD By similarity.
Subcellular location	Cytoplasm. Note: Localized to the Z line. Some colocalization with CKM at M-band 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. Ref.5
Induction	Thyroid hormones up-regulate expression during hindleg muscle development and down-regulate during cardiac muscle development. Decrease in ENO3 levels with aortic stenosis.
Sequence similarities	Belongs to the enolase family.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aging Inferred from expression pattern. Source: RGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from expression pattern. Source: RGD skeletal muscle regeneration Inferred from expression pattern. Source: RGD
Cellular component	membrane fraction Inferred from direct assay. Source: RGD phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.5 Inferred from direct assay. Source: RGD protein heterodimerization activity Inferred from direct assay. Source: RGD protein homodimerization activity 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

Beta-enolase

PRO_0000134110

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

Experimental info

Sequence conflict

L → P in CAA68788. Ref.1

Sequence conflict

176 – 182

SSFKEAM → KLFQGSQ in CAA68788. Ref.1

Sequence conflict

279

L → P in CAA68788. Ref.1

Sequence conflict

355

Q → L in CAA68788. Ref.1

Sequence conflict

381

I → V in CAA68788. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P15429-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 136A5300E052D5A7
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FASTA

434

47,014

        10         20         30         40         50         60 
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKSRYLGK 

        70         80         90        100        110        120 
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 

       190        200        210        220        230        240 
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 

       250        260        270        280        290        300 
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KSFIKNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AVFAGRKFRN PKAK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and nucleotide sequence of rat muscle-specific enolase (beta beta enolase)." Ohshima Y., Mitsui H., Takayama Y., Kushiya E., Sakimura K., Takahashi Y. FEBS Lett. 242:425-430(1989) [PubMed: 2914621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Skeletal muscle.
[2]	"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: Heart.
[3]	"Structure and expression of rat muscle-specific enolase gene." Sakimura K., Kushiya E., Ohshima-Ichimura Y., Mitsui H., Takahashi Y. FEBS Lett. 277:78-82(1990) [PubMed: 2269373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[4]	Lubec G., Afjehi-Sadat L., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 10-28; 33-50; 106-120; 240-253; 257-262; 336-394 AND 407-412, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Spinal cord.
[5]	"Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy." Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M. Am. J. Physiol. 269:H1843-H1851(1995) [PubMed: 8594891] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[6]	"Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development." Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L., Rappaport L., Lamande N., Lucas M. Am. J. Physiol. 278:E330-E339(2000) [PubMed: 10662718] [Abstract] Cited for: EFFECT OF THYROID HORMONES ON EXPRESSION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Y00979 mRNA. Translation: CAA68788.1. BC083566 mRNA. Translation: AAH83566.1. X57774 Genomic DNA. Translation: CAA40920.1.
IPI	IPI00231631.
PIR	S02072.
RefSeq	NP_037081.2.
UniGene	Rn.3443
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
SMR	P15429. Positions 2-431.
ModBase	Search...
PTM databases
PhosphoSite	P15429.
Genome annotation databases
Ensembl	ENSRNOG00000004078. Rattus norvegicus. [Contig view]
GeneID	25438.
KEGG	rno:25438.
Organism-specific databases
RGD	2555. Eno3.
Phylogenomic databases
HOVERGEN	P15429.
OMA	P15429. VENINNT.
Enzyme and pathway databases
BRENDA	4.2.1.11. 248.
Gene expression databases
ArrayExpress	P15429.
GermOnline	ENSRNOG00000004078. Rattus norvegicus.
Family and domain databases
InterPro	IPR000941. Enolase. [Graphical view]
PANTHER	PTHR11902. Enolase. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	606651.

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Entry information

Entry name

ENOB_RAT

Accession

Primary (citable) accession number: P15429
Secondary accession number(s): Q5XIV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 83 of the entry and version 3 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM 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