ENOG_MOUSE
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 03-AUG-2022, entry version 201.
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; 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: Has neurotrophic and neuroprotective properties on a broad
CC spectrum of central nervous system (CNS) neurons. Binds, in a calcium-
CC dependent manner, to cultured neocortical neurons and promotes cell
CC survival (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
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.
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}.
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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_001302642.1.
DR RefSeq; NP_038537.1; NM_013509.3.
DR RefSeq; XP_006505566.1; XM_006505503.3.
DR RefSeq; XP_006505567.1; XM_006505504.2.
DR AlphaFoldDB; P17183; -.
DR SMR; P17183; -.
DR BioGRID; 199452; 22.
DR IntAct; P17183; 4.
DR MINT; P17183; -.
DR STRING; 10090.ENSMUSP00000004378; -.
DR iPTMnet; P17183; -.
DR PhosphoSitePlus; P17183; -.
DR SwissPalm; P17183; -.
DR UCD-2DPAGE; P17183; -.
DR CPTAC; non-CPTAC-3313; -.
DR EPD; P17183; -.
DR jPOST; P17183; -.
DR PaxDb; P17183; -.
DR PeptideAtlas; P17183; -.
DR PRIDE; P17183; -.
DR ProteomicsDB; 277876; -.
DR Antibodypedia; 3514; 2106 antibodies from 52 providers.
DR DNASU; 13807; -.
DR Ensembl; ENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
DR GeneID; 13807; -.
DR KEGG; mmu:13807; -.
DR UCSC; uc009drs.2; mouse.
DR CTD; 2026; -.
DR MGI; MGI:95394; Eno2.
DR VEuPathDB; HostDB:ENSMUSG00000004267; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P17183; -.
DR OMA; QHLGGAF; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P17183; -.
DR TreeFam; TF300391; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR SABIO-RK; P17183; -.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 13807; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Eno2; mouse.
DR PRO; PR:P17183; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P17183; protein.
DR Bgee; ENSMUSG00000004267; Expressed in motor neuron and 206 other tissues.
DR ExpressionAtlas; P17183; baseline and differential.
DR Genevisible; P17183; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
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:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; ISO:MGI.
DR GO; GO:0006094; P:gluconeogenesis; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 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; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
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
