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Alpha-enolase (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (HAP47) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase)

 ENOA_BOVIN              Reviewed;         434 AA.
Q9XSJ4; Q3SYW4;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
26-FEB-2020, entry version 142.
RecName: Full=Alpha-enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=Enolase 1;
AltName: Full=HAP47;
AltName: Full=Non-neural enolase;
Short=NNE;
AltName: Full=Phosphopyruvate hydratase;
Name=ENO1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Chapman K.L., Newman B., Hillaby M.C., Freemont A.J., Grant M.E.,
Boot-Handford R., Wallis G.A.;
"Alpha enolase is upregulated in proliferative chondrocytes in the
epiphyseal growth plate and in human osteoarthritic tissue.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 270-281 AND 373-394, AND FUNCTION AS AN ENDOTHELIAL
HYPOXIC STRESS PROTEIN.
PubMed=7499243; DOI=10.1074/jbc.270.46.27752;
Aaronson R.M., Graven K.K., Tucci M., McDonald R.J., Farber H.W.;
"Non-neuronal enolase is an endothelial hypoxic stress protein.";
J. Biol. Chem. 270:27752-27757(1995).
-!- FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-
phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to
glycolysis, involved in various processes such as growth control,
hypoxia tolerance and allergic responses (PubMed:7499243). May also
function in the intravascular and pericellular fibrinolytic system due
to its ability to serve as a receptor and activator of plasminogen on
the cell surface of several cell-types such as leukocytes and neurons
(By similarity). Stimulates immunoglobulin production (By similarity).
{ECO:0000250|UniProtKB:P06733, ECO:0000269|PubMed:7499243}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11;
Evidence={ECO:0000250|UniProtKB:P06733};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P06733};
Note=Binds two Mg(2+) per subunit. Required for catalysis and for
stabilizing the dimer. {ECO:0000250|UniProtKB:P06733};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
beta and gamma, which can form homodimers or heterodimers which are
cell-type and development-specific. ENO1 interacts with PLG in the
neuronal plasma membrane and promotes its activation. The C-terminal
lysine is required for this binding. Interacts with ENO4 and PGAM2 (By
similarity). Interacts with CMTM6 (By similarity).
{ECO:0000250|UniProtKB:P06733, ECO:0000250|UniProtKB:P17182}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Can translocate to the plasma membrane in either
the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1
is localized to the M-band. {ECO:0000250}.
-!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo
and in most adult tissues. The alpha/beta heterodimer and the beta/beta
homodimer are found in striated muscle, and the alpha/gamma heterodimer
and the gamma/gamma homodimer in neurons.
-!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
cells, and to the alpha/gamma heterodimer in nerve cells.
-!- INDUCTION: Expression increased up to 3-fold by hypoxic stress in
vascular endothelial cells.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P06733}.
-!- PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the
phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AF149256; AAD33073.1; -; mRNA.
EMBL; BC103354; AAI03355.1; -; mRNA.
RefSeq; NP_776474.2; NM_174049.2.
SMR; Q9XSJ4; -.
STRING; 9913.ENSBTAP00000017839; -.
Allergome; 11909; Bos d Enolase.
PaxDb; Q9XSJ4; -.
PeptideAtlas; Q9XSJ4; -.
PRIDE; Q9XSJ4; -.
GeneID; 281141; -.
KEGG; bta:281141; -.
CTD; 2023; -.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
InParanoid; Q9XSJ4; -.
KO; K01689; -.
OrthoDB; 773373at2759; -.
SABIO-RK; Q9XSJ4; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:AgBase.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; ISS:UniProtKB.
GO; GO:0061621; P:canonical glycolysis; ISS:UniProtKB.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
Glycolysis; Hydroxylation; Isopeptide bond; Lyase; Magnesium; Membrane;
Metal-binding; Phosphoprotein; Plasminogen activation; Reference proteome;
Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P06733"
CHAIN 2..434
/note="Alpha-enolase"
/id="PRO_0000134096"
REGION 370..373
/note="Substrate binding"
/evidence="ECO:0000250|UniProtKB:P00924"
REGION 405..434
/note="Required for interaction with PLG"
/evidence="ECO:0000250"
ACT_SITE 210
/note="Proton donor"
/evidence="ECO:0000250|UniProtKB:P00924"
ACT_SITE 343
/note="Proton acceptor"
/evidence="ECO:0000250|UniProtKB:P00924"
METAL 40
/note="Magnesium 1"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 245
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 293
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 318
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
BINDING 158
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 167
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 293
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 318
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 394
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 5
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 44
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 60
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 60
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 64
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 71
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 89
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 89
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 92
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 126
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 193
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 199
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 202
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 228
/note="N6-(2-hydroxyisobutyryl)lysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 228
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 228
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 233
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 233
/note="N6-malonyllysine; alternate"
/evidence="ECO:0000250"
MOD_RES 254
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 256
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 263
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 281
/note="N6-(2-hydroxyisobutyryl)lysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 281
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 287
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 291
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 335
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 343
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 406
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 420
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 420
/note="N6-malonyllysine; alternate"
/evidence="ECO:0000250"
MOD_RES 420
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
CROSSLNK 202
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
CONFLICT 82
/note="L -> S (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 102
/note="N -> K (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 324
/note="N -> T (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 327
/note="R -> T (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 331..333
/note="AVS -> GVN (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 347
/note="I -> N (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 356
/note="A -> G (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 361..362
/note="QS -> HA (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 377
/note="E -> D (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 383
/note="D -> E (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 395..397
/note="TVA -> NGP (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 401
/note="S -> T (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
CONFLICT 427
/note="S -> N (in Ref. 1; AAD33073)"
/evidence="ECO:0000305"
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


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