P15429 · ENOB_RAT
- ProteinBeta-enolase
- GeneEno3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids434 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Appears to have a function in striated muscle development and regeneration.
Catalytic activity
- (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvateThis reaction proceeds in the forward direction.
Cofactor
Note: Mg2+ is required for catalysis and for stabilizing the dimer.
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 158 | substrate | ||||
Sequence: H | ||||||
Binding site | 167 | substrate | ||||
Sequence: E | ||||||
Active site | 210 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 245 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 293 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 293 | substrate | ||||
Sequence: E | ||||||
Binding site | 318 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 318 | substrate | ||||
Sequence: D | ||||||
Active site | 343 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 370-373 | substrate | ||||
Sequence: SHRS | ||||||
Binding site | 394 | substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | phosphopyruvate hydratase complex | |
Molecular Function | identical protein binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphopyruvate hydratase activity | |
Molecular Function | protein-containing complex binding | |
Biological Process | canonical glycolysis | |
Biological Process | glycolytic process | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | skeletal muscle tissue regeneration |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-enolase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP15429
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized to the Z line. Some colocalization with CKM at M-band (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000134110 | 2-434 | Beta-enolase | |||
Sequence: AMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKSRYLGKGVLKAVEHINKTLGPALLEKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHISGEKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVDIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAVFAGRKFRNPKAK | ||||||
Modified residue | 72 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 83 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 157 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 176 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 205 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 229 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 236 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 263 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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.
Induction
Thyroid hormones up-regulate expression during hindleg muscle development and down-regulate during cardiac muscle development. Decrease in ENO3 levels with aortic stenosis.
Developmental stage
During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells.
Gene expression databases
Interaction
Subunit
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).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P15429 | PDE4DIP Q5VU43-11 | 2 | EBI-10817548, EBI-10769071 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length434
- Mass (Da)47,014
- Last updated2007-01-23 v3
- Checksum136A5300E052D5A7
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AK25 | A0A8I6AK25_RAT | Eno3 | 473 | ||
A0A8I5ZJD5 | A0A8I5ZJD5_RAT | Eno3 | 421 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 63 | in Ref. 1; CAA68788 | ||||
Sequence: L → P | ||||||
Sequence conflict | 176-182 | in Ref. 1; CAA68788 | ||||
Sequence: SSFKEAM → KLFQGSQ | ||||||
Sequence conflict | 279 | in Ref. 1; CAA68788 | ||||
Sequence: L → P | ||||||
Sequence conflict | 355 | in Ref. 1; CAA68788 | ||||
Sequence: Q → L | ||||||
Sequence conflict | 381 | in Ref. 1; CAA68788 | ||||
Sequence: I → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y00979 EMBL· GenBank· DDBJ | CAA68788.1 EMBL· GenBank· DDBJ | mRNA | ||
BC083566 EMBL· GenBank· DDBJ | AAH83566.1 EMBL· GenBank· DDBJ | mRNA | ||
X57774 EMBL· GenBank· DDBJ | CAA40920.1 EMBL· GenBank· DDBJ | Genomic DNA |