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P25704 (ENOB_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-enolase
EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name=MSE
Skeletal muscle enolase
Gene names
Name:ENO3
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 By similarity. Some colocalization with CKM at M-band. Ref.4

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.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentphosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 434433Beta-enolase
PRO_0000134109

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

Experimental info

Sequence conflict2541N → D AA sequence Ref.3
Sequence conflict299 – 30911DDWATWTSFLS → GDWGAWSRFLA AA sequence Ref.3
Sequence conflict3151I → V AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P25704 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E0DB6CE8EA2C3214

FASTA43447,069
        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 HDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE 

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

       250        260        270        280        290        300 
VIGMDVAASE FHRNGKYDLD FKSPDDPARH ITGQKLGELY 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

« Hide

References

[1]"The cDNA cloning of rabbit muscle-specific enolase gene, site directed mutagenesis (E417L) of the gene, expression of the wild-type and mutant genes in Escherichia coli."
Zheng S.-X.
Thesis (1995), Concordia University / Montreal, Canada
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
[2]Kornblatt M.J., Zheng S.-X., Lamande N., Lazar M.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 297-309 AND 315.
[3]"The primary structure of rabbit muscle enolase."
Chin C.C.Q.
J. Protein Chem. 9:427-432(1990) [PubMed: 2275753] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-434.
Tissue: Muscle.
[4]"Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase."
Foucault G., Vacher M., Merkulova T., Keller A., Arrio-Dupont M.
Biochem. J. 338:115-121(1999) [PubMed: 9931306] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF260259 mRNA. Translation: AAF71925.2.
PIRA37210.
RefSeqNP_001075554.1. NM_001082085.1.
UniGeneOcu.512.

3D structure databases

ProteinModelPortalP25704.
SMRP25704. Positions 2-431.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008769.

Organism-specific databases

CTD2027.

Phylogenomic databases

eggNOGmaNOG17235.
HOVERGENHBG000067.

Enzyme and pathway databases

BRENDA4.2.1.11. 1749.

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. Enolase. 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...

Entry information

Entry nameENOB_RABIT
AccessionPrimary (citable) accession number: P25704
Secondary accession number(s): Q9N0N6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: October 19, 2011
This is version 83 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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