ID ENOG_MOUSE Reviewed; 434 AA. AC P17183; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 220. DE RecName: Full=Gamma-enolase; DE EC=4.2.1.11; DE AltName: Full=2-phospho-D-glycerate hydro-lyase; DE AltName: Full=Enolase 2; DE AltName: Full=Neural enolase; DE AltName: Full=Neuron-specific enolase; DE Short=NSE; GN Name=Eno2 {ECO:0000312|MGI:MGI:95394}; Synonyms=Eno-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=2362815; DOI=10.1093/nar/18.12.3638; RA Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M., RA Lazar M., Caput D.; RT "Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse RT brain."; RL Nucleic Acids Res. 18:3638-3638(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9445485; RA Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., RA Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.; RT "Comparative sequence analysis of a gene-rich cluster at human chromosome RT 12p13 and its syntenic region in mouse chromosome 6."; RL Genome Res. 8:29-40(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 16-28; 33-50; 73-89; 104-120; 163-179; 184-193; RP 203-228; 240-262; 270-285; 307-326; 336-358; 373-394 AND 413-429, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP TISSUE SPECIFICITY. RX PubMed=11229603; DOI=10.1016/s0248-4900(00)01103-5; RA Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., RA Lucas M., Chatelet F.-P.; RT "Fibre-type distribution and subcellular localisation of alpha and beta RT enolase in mouse striated muscle."; RL Biol. Cell 92:527-535(2000). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, and Liver; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP TISSUE SPECIFICITY. RX PubMed=23446454; DOI=10.1095/biolreprod.112.107128; RA Nakamura N., Dai Q., Williams J., Goulding E.H., Willis W.D., Brown P.R., RA Eddy E.M.; RT "Disruption of a spermatogenic cell-specific mouse enolase 4 (eno4) gene RT causes sperm structural defects and male infertility."; RL Biol. Reprod. 88:90-90(2013). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197 AND LYS-199, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Enolase that catalyzes the conversion of 2-phosphoglycerate CC to phosphoenolpyruvate in glycolysis and the reverse reaction in CC gluconeogenesis (By similarity). Has neurotrophic and neuroprotective CC properties on a broad spectrum of central nervous system (CNS) neurons. CC Binds, in a calcium-dependent manner, to cultured neocortical neurons CC and promotes cell survival (By similarity). CC {ECO:0000250|UniProtKB:P06733, ECO:0000250|UniProtKB:P07323}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, CC ChEBI:CHEBI:58702; EC=4.2.1.11; CC Evidence={ECO:0000250|UniProtKB:P06733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; CC Evidence={ECO:0000250|UniProtKB:P06733}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10166; CC Evidence={ECO:0000250|UniProtKB:P06733}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P07323}; CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer. CC {ECO:0000250|UniProtKB:P06733}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, CC beta and gamma, which can form homodimers or heterodimers which are CC cell-type and development-specific. {ECO:0000250|UniProtKB:P09104}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane CC {ECO:0000250}. Note=Can translocate to the plasma membrane in either CC the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Skeletal muscle (at protein level). The alpha/alpha CC homodimer is expressed in embryo and in most adult tissues. The CC alpha/beta heterodimer and the beta/beta homodimer are found in CC striated muscle, and the alpha/gamma heterodimer and the gamma/gamma CC homodimer in neurons. {ECO:0000269|PubMed:23446454, CC ECO:0000305|PubMed:11229603}. CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the CC alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle CC cells, and to the alpha/gamma heterodimer in nerve cells. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X52380; CAA36606.1; -; mRNA. DR EMBL; AC002397; AAC36002.1; -; Genomic_DNA. DR EMBL; BC031739; AAH31739.1; -; mRNA. DR CCDS; CCDS20527.1; -. DR PIR; S10247; S10247. DR RefSeq; NP_001289571.1; NM_001302642.2. DR RefSeq; NP_001342149.1; NM_001355220.2. DR RefSeq; NP_001396615.1; NM_001409686.1. DR RefSeq; NP_001396616.1; NM_001409687.1. DR RefSeq; NP_001396617.1; NM_001409688.1. DR RefSeq; NP_038537.1; NM_013509.4. DR SMR; P17183; -. DR BioGRID; 199452; 24. DR IntAct; P17183; 4. DR STRING; 10090.ENSMUSP00000004378; -. DR GlyGen; P17183; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P17183; -. DR PhosphoSitePlus; P17183; -. DR SwissPalm; P17183; -. DR MetOSite; P17183; -. DR CPTAC; non-CPTAC-3313; -. DR PaxDb; 10090-ENSMUSP00000004378; -. DR PeptideAtlas; P17183; -. DR ProteomicsDB; 277876; -. DR Pumba; P17183; -. DR jPOST; P17183; -. DR DNASU; 13807; -. DR Ensembl; ENSMPUT00000016913; ENSMPUP00000016664; ENSMPUG00000016769. DR Ensembl; ENSMUST00000004378.15; ENSMUSP00000004378.9; ENSMUSG00000004267.17. DR GeneID; 13807; -. DR KEGG; mmu:13807; -. DR UCSC; uc009drs.2; mouse. DR CTD; 2026; -. DR VEuPathDB; HostDB:ENSMUSG00000004267; -. DR AGR; MGI:95394; -. DR MGI; MGI:95394; Eno2. DR eggNOG; KOG2670; Eukaryota. DR GeneTree; ENSGT00950000182805; -. DR HOGENOM; CLU_031223_0_0_1; -. DR InParanoid; P17183; -. DR OMA; AACNMAQ; -. DR OrthoDB; 1739814at2759; -. DR PhylomeDB; P17183; -. DR Reactome; R-MMU-70171; Glycolysis. DR Reactome; R-MMU-70263; Gluconeogenesis. DR SABIO-RK; P17183; -. DR UniPathway; UPA00109; UER00187. DR PRO; PR:P17183; -. DR Bgee; ENSMUSG00000004267; Expressed in motor neuron and 209 other cell types or tissues. DR ExpressionAtlas; P17183; baseline and differential. DR CDD; cd03313; enolase; 1. DR FunFam; 3.30.390.10:FF:000001; Enolase; 1. DR FunFam; 3.20.20.120:FF:000002; Enolase 1; 1. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR PANTHER; PTHR11902; ENOLASE; 1. DR PANTHER; PTHR11902:SF10; GAMMA-ENOLASE; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SFLD; SFLDS00001; Enolase; 1. DR SFLD; SFLDF00002; enolase; 1. DR SFLD; SFLDG00178; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR NCBIfam; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. DR GO; GO:0005938; C:cell cortex; ISO:GO_Central. DR GO; GO:0009986; C:cell surface; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0030426; C:growth cone; ISO:GO_Central. DR GO; GO:0016020; C:membrane; ISO:GO_Central. DR GO; GO:0045121; C:membrane raft; ISO:GO_Central. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0043204; C:perikaryon; IDA:MGI. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; ISO:GO_Central. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central. DR GO; GO:0097060; C:synaptic membrane; ISO:GO_Central. DR GO; GO:0019899; F:enzyme binding; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0061621; P:canonical glycolysis; ISO:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; ISO:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR Proteomes; UP000000589; Chromosome 6. DR Antibodypedia; 3514; 2392 antibodies from 57 providers. DR RNAct; P17183; protein. DR BioGRID-ORCS; 13807; 0 hits in 78 CRISPR screens. DR AlphaFoldDB; P17183; -. DR CD-CODE; CE726F99; Postsynaptic density. DR FunCoup; P17183; 1149. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; KW Glycolysis; Hydroxylation; Isopeptide bond; Lyase; Magnesium; Membrane; KW Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P06733" FT CHAIN 2..434 FT /note="Gamma-enolase" FT /id="PRO_0000134113" FT ACT_SITE 210 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P00924" FT ACT_SITE 343 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00924" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P06733" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00924" FT BINDING 167 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00924" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06733" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06733" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 293 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00924" FT BINDING 318 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P06733" FT BINDING 318 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00924" FT BINDING 370..373 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00924" FT BINDING 394 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00924" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 5 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 26 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P09104" FT MOD_RES 44 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P09104" FT MOD_RES 60 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 60 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 64 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 89 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 89 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 193 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 197 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 202 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 228 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 228 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 233 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09104" FT MOD_RES 233 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 256 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09104" FT MOD_RES 287 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 291 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06733" FT MOD_RES 335 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 343 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17182" FT MOD_RES 406 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17182" FT CROSSLNK 202 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06733" SQ SEQUENCE 434 AA; 47297 MW; A5C7F189E913392E CRC64; MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK GVLKAVDHIN SRIAPALISS GISVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK AGAAERDLPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM VIGMDVAASE FYRDGKYDLD FKSPADPSRY ITGDQLGALY QDFVRNYPVV SIEDPFDQDD WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL //