ENOA_BOVIN
ID ENOA_BOVIN Reviewed; 434 AA.
AC Q9XSJ4; Q3SYW4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 1;
DE AltName: Full=HAP47;
DE AltName: Full=Non-neural enolase;
DE Short=NNE;
DE AltName: Full=Phosphopyruvate hydratase;
GN Name=ENO1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chapman K.L., Newman B., Hillaby M.C., Freemont A.J., Grant M.E.,
RA Boot-Handford R., Wallis G.A.;
RT "Alpha enolase is upregulated in proliferative chondrocytes in the
RT epiphyseal growth plate and in human osteoarthritic tissue.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 270-281 AND 373-394, AND FUNCTION AS AN ENDOTHELIAL
RP HYPOXIC STRESS PROTEIN.
RX PubMed=7499243; DOI=10.1074/jbc.270.46.27752;
RA Aaronson R.M., Graven K.K., Tucci M., McDonald R.J., Farber H.W.;
RT "Non-neuronal enolase is an endothelial hypoxic stress protein.";
RL J. Biol. Chem. 270:27752-27757(1995).
CC -!- FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to
CC glycolysis, involved in various processes such as growth control,
CC hypoxia tolerance and allergic responses (PubMed:7499243). May also
CC function in the intravascular and pericellular fibrinolytic system due
CC to its ability to serve as a receptor and activator of plasminogen on
CC the cell surface of several cell-types such as leukocytes and neurons
CC (By similarity). Stimulates immunoglobulin production (By similarity).
CC {ECO:0000250|UniProtKB:P06733, ECO:0000269|PubMed:7499243}.
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:P06733};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06733};
CC Note=Binds two Mg(2+) per subunit. Required for catalysis and for
CC stabilizing the dimer. {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. ENO1 interacts with PLG in the
CC neuronal plasma membrane and promotes its activation. The C-terminal
CC lysine is required for this binding. Interacts with ENO4 and PGAM2 (By
CC similarity). Interacts with CMTM6 (By similarity).
CC {ECO:0000250|UniProtKB:P06733, ECO:0000250|UniProtKB:P17182}.
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. ENO1
CC is localized to the 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, and to the alpha/gamma heterodimer in nerve cells.
CC -!- INDUCTION: Expression increased up to 3-fold by hypoxic stress in
CC vascular endothelial cells.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P06733}.
CC -!- PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the
CC phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}.
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; AF149256; AAD33073.1; -; mRNA.
DR EMBL; BC103354; AAI03355.1; -; mRNA.
DR RefSeq; NP_776474.2; NM_174049.2.
DR AlphaFoldDB; Q9XSJ4; -.
DR SMR; Q9XSJ4; -.
DR STRING; 9913.ENSBTAP00000017839; -.
DR Allergome; 11909; Bos d Enolase.
DR PaxDb; Q9XSJ4; -.
DR PeptideAtlas; Q9XSJ4; -.
DR PRIDE; Q9XSJ4; -.
DR GeneID; 281141; -.
DR KEGG; bta:281141; -.
DR CTD; 2023; -.
DR eggNOG; KOG2670; Eukaryota.
DR InParanoid; Q9XSJ4; -.
DR OrthoDB; 773373at2759; -.
DR SABIO-RK; Q9XSJ4; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; ISS:UniProtKB.
DR GO; GO:0061621; P:canonical glycolysis; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Plasminogen activation; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT CHAIN 2..434
FT /note="Alpha-enolase"
FT /id="PRO_0000134096"
FT REGION 405..434
FT /note="Required for interaction with PLG"
FT /evidence="ECO:0000250"
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 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="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="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 44
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
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 71
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 92
FT /note="N6-acetyllysine"
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 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 228
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
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-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 233
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 254
FT /note="Phosphoserine"
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:P06733"
FT MOD_RES 281
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 281
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
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 MOD_RES 420
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 420
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 420
FT /note="N6-succinyllysine; alternate"
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"
FT CONFLICT 82
FT /note="L -> S (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="N -> K (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="N -> T (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="R -> T (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 331..333
FT /note="AVS -> GVN (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="I -> N (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> G (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..362
FT /note="QS -> HA (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="E -> D (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> E (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..397
FT /note="TVA -> NGP (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="S -> T (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="S -> N (in Ref. 1; AAD33073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47326 MW; 91E2A06F073C5121 CRC64;
MSILKVHARE IFDSRGNPTV EVDLFTAKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK
GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK
AGAVEKGVPL YRHIADLAGN AEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAENFRE
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKNA IGKAGYSDKV
VIGMDVAASE FYRSGKYDLD FKSPDDPSRY ITPDELANLY KSFIRDYPVV SIEDPFDQDD
WEAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVSEKSCNCL LLKVNQIGSV TESLQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTVAPCR SERLAKYNQI LRIEEELGSK
AKFAGRSFRN PLAK
