P17183 · ENOG_MOUSE
- ProteinGamma-enolase
- GeneEno2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids434 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
- (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
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 | 40 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 158 | substrate | ||||
Sequence: H | ||||||
Binding site | 167 | substrate | ||||
Sequence: E | ||||||
Active site | 210 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 245 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 245 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 293 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 293 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 293 | substrate | ||||
Sequence: E | ||||||
Binding site | 318 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
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 | cell cortex | |
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | growth cone | |
Cellular Component | membrane raft | |
Cellular Component | myelin sheath | |
Cellular Component | neuronal cell body | |
Cellular Component | perikaryon | |
Cellular Component | phosphopyruvate hydratase complex | |
Cellular Component | photoreceptor inner segment | |
Cellular Component | synaptic membrane | |
Molecular Function | enzyme binding | |
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 | gluconeogenesis | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGamma-enolase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP17183
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000134113 | 2-434 | Gamma-enolase | |||
Sequence: SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALISSGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL | ||||||
Modified residue | 5 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 26 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 44 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 60 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 60 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 64 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 89 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 89 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 193 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 197 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 199 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 202 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 202 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 228 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 228 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 233 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 233 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 256 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 263 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 287 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 291 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 335 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 343 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 406 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Skeletal muscle (at protein level). 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.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length434
- Mass (Da)47,297
- Last updated2007-01-23 v2
- ChecksumA5C7F189E913392E
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0N4SUW8 | A0A0N4SUW8_MOUSE | Eno2 | 37 | ||
A0A0N4SUX5 | A0A0N4SUX5_MOUSE | Eno2 | 391 | ||
A0A0N4SUI6 | A0A0N4SUI6_MOUSE | Eno2 | 58 | ||
D3Z6E4 | D3Z6E4_MOUSE | Eno2 | 315 | ||
D3YVD3 | D3YVD3_MOUSE | Eno2 | 121 | ||
D3Z2S4 | D3Z2S4_MOUSE | Eno2 | 162 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X52380 EMBL· GenBank· DDBJ | CAA36606.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002397 EMBL· GenBank· DDBJ | AAC36002.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC031739 EMBL· GenBank· DDBJ | AAH31739.1 EMBL· GenBank· DDBJ | mRNA |