ENOG_RAT
ID ENOG_RAT Reviewed; 434 AA.
AC P07323;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 192.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2865729; DOI=10.1073/pnas.82.21.7453;
RA Sakimura K., Kushiya E., Obinata M., Odani S., Takahashi Y.;
RT "Molecular cloning and the nucleotide sequence of cDNA for neuron-specific
RT enolase messenger RNA of rat brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7453-7457(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=3746946; DOI=10.1002/jnr.490160114;
RA Forss-Petter S., Danielson P., Sutcliffe J.G.;
RT "Neuron-specific enolase: complete structure of rat mRNA, multiple
RT transcriptional start sites, and evidence suggesting post-transcriptional
RT control.";
RL J. Neurosci. Res. 16:141-156(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=2450052; DOI=10.1016/0378-1119(87)90218-6;
RA Sakimura K., Kushiya E., Takahashi Y., Suzuki Y.;
RT "The structure and expression of neuron-specific enolase gene.";
RL Gene 60:103-113(1987).
RN [5]
RP PROTEIN SEQUENCE OF 10-28; 32-50; 65-89; 106-120; 163-179; 184-193;
RP 240-262; 270-285; 307-326; 336-394 AND 407-422, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP POSSIBLE FUNCTION AS A NEUROTROPHIC FACTOR.
RX PubMed=7753500; DOI=10.1016/0168-0102(94)00849-b;
RA Hattori T., Takei N., Mizuno Y., Kato K., Kohsaka S.;
RT "Neurotrophic and neuroprotective effects of neuron-specific enolase on
RT cultured neurons from embryonic rat brain.";
RL Neurosci. Res. 21:191-198(1995).
RN [7]
RP SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
RX PubMed=15041191; DOI=10.1016/j.neures.2003.12.006;
RA Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H.;
RT "Localization of enolase in synaptic plasma membrane as an alphagamma
RT heterodimer in rat brain.";
RL Neurosci. Res. 48:379-386(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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: The alpha/alpha homodimer is expressed in embryo
CC and in most adult tissues. The alpha/beta heterodimer and the beta/beta
CC homodimer are found in striated muscle, and the alpha/gamma heterodimer
CC and the gamma/gamma homodimer in neurons.
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. ENO2 levels
CC in brain increase 10-30 days after birth. Levels continue to accumulate
CC over the following few months (protein only).
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; M11931; AAA41119.1; -; mRNA.
DR EMBL; M22770; AAA41725.1; -; Genomic_DNA.
DR EMBL; AF019973; AAB72088.1; -; mRNA.
DR EMBL; BC060310; AAH60310.1; -; mRNA.
DR EMBL; X07727; CAA30556.1; -; Genomic_DNA.
DR EMBL; X07728; CAA30556.1; JOINED; Genomic_DNA.
DR EMBL; X07729; CAA30556.1; JOINED; Genomic_DNA.
DR PIR; A24742; A24742.
DR PIR; JC1039; JC1039.
DR RefSeq; NP_647541.1; NM_139325.3.
DR RefSeq; XP_003750705.1; XM_003750657.3.
DR RefSeq; XP_006237392.1; XM_006237330.3.
DR RefSeq; XP_006244698.1; XM_006244636.3.
DR AlphaFoldDB; P07323; -.
DR SMR; P07323; -.
DR BioGRID; 246511; 1.
DR IntAct; P07323; 1.
DR MINT; P07323; -.
DR STRING; 10116.ENSRNOP00000005535; -.
DR iPTMnet; P07323; -.
DR PhosphoSitePlus; P07323; -.
DR SwissPalm; P07323; -.
DR World-2DPAGE; 0004:P07323; -.
DR jPOST; P07323; -.
DR PaxDb; P07323; -.
DR PRIDE; P07323; -.
DR Ensembl; ENSRNOT00000105821; ENSRNOP00000093168; ENSRNOG00000013141.
DR GeneID; 24334; -.
DR KEGG; rno:24334; -.
DR UCSC; RGD:2554; rat.
DR CTD; 2026; -.
DR RGD; 2554; Eno2.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P07323; -.
DR OMA; QHLGGAF; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P07323; -.
DR TreeFam; TF300391; -.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P07323; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013141; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P07323; RN.
DR GO; GO:0005938; C:cell cortex; IDA:CAFA.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:CAFA.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:CAFA.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; ISO:RGD.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0061621; P:canonical glycolysis; IDA:CAFA.
DR GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
DR GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IEP:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:CAFA.
DR GO; GO:1901214; P:regulation of neuron death; IGI:CAFA.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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_0000134114"
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 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
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:0000250|UniProtKB:P17183"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17183"
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:0007744|PubMed:22673903"
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; 47141 MW; BAFFCE2F04BCCA45 CRC64;
MSIQKIWARE ILDSRGNPTV EVDLHTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
AGAAEKDLPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM
VIGMDVAASE FYRDGKYDLD FKSPADPSRC ITGDQLGALY QDFVRNYPVV SIEDPFDQDD
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGEE
ARFAGHNFRN PSVL
