ENOB_RABIT
ID ENOB_RABIT Reviewed; 434 AA.
AC P25704; Q9N0N6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Beta-enolase;
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P15429};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 3;
DE AltName: Full=Muscle-specific enolase;
DE Short=MSE;
DE AltName: Full=Skeletal muscle enolase;
GN Name=ENO3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Zheng S.-X.;
RT "The cDNA cloning of rabbit muscle-specific enolase gene, site directed
RT mutagenesis (E417L) of the gene, expression of the wild-type and mutant
RT genes in Escherichia coli.";
RL Thesis (1995), Concordia University / Montreal, Canada.
RN [2]
RP SEQUENCE REVISION TO 297-309 AND 315.
RA Kornblatt M.J., Zheng S.-X., Lamande N., Lazar M.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-434.
RC TISSUE=Muscle;
RX PubMed=2275753; DOI=10.1007/bf01024618;
RA Chin C.C.Q.;
RT "The primary structure of rabbit muscle enolase.";
RL J. Protein Chem. 9:427-432(1990).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9931306; DOI=10.1042/bj3380115;
RA Foucault G., Vacher M., Merkulova T., Keller A., Arrio-Dupont M.;
RT "Presence of enolase in the M-band of skeletal muscle and possible indirect
RT interaction with the cytosolic muscle isoform of creatine kinase.";
RL Biochem. J. 338:115-121(1999).
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. Appears to have a function in
CC striated muscle development and regeneration.
CC {ECO:0000250|UniProtKB:P15429}.
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 Evidence={ECO:0000250|UniProtKB:P15429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000250|UniProtKB:P15429};
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. {ECO:0000250|UniProtKB:P15429}.
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. Interacts with PNKD (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9931306}.
CC Note=Localized to the Z line (By similarity). Some colocalization with
CC CKM at M-band. {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.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; AF260259; AAF71925.2; -; mRNA.
DR PIR; A37210; A37210.
DR RefSeq; NP_001075554.1; NM_001082085.1.
DR AlphaFoldDB; P25704; -.
DR SMR; P25704; -.
DR BioGRID; 1171792; 1.
DR STRING; 9986.ENSOCUP00000025169; -.
DR GeneID; 100008769; -.
DR KEGG; ocu:100008769; -.
DR CTD; 2027; -.
DR InParanoid; P25704; -.
DR OrthoDB; 773373at2759; -.
DR BRENDA; 4.2.1.11; 1749.
DR SABIO-RK; P25704; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13929,
FT ECO:0000269|PubMed:2275753"
FT CHAIN 2..434
FT /note="Beta-enolase"
FT /id="PRO_0000134109"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13929"
FT CONFLICT 254
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..309
FT /note="DDWATWTSFLS -> GDWGAWSRFLA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="I -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47069 MW; E0DB6CE8EA2C3214 CRC64;
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKSRYLGK
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGN HDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV
VIGMDVAASE FHRNGKYDLD FKSPDDPARH ITGQKLGELY KSFIKNYPVV SIEDPFDQDD
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
AVFAGRKFRN PKAK
