ENOA_MESAU
ID ENOA_MESAU Reviewed; 223 AA.
AC P86210;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Alpha-enolase {ECO:0000250|UniProtKB:P06733};
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000250|UniProtKB:P06733};
DE AltName: Full=Enolase 1 {ECO:0000250|UniProtKB:P06733};
DE AltName: Full=Non-neural enolase {ECO:0000250|UniProtKB:P06733};
DE Short=NNE {ECO:0000250|UniProtKB:P06733};
DE Flags: Fragments;
GN Name=ENO1 {ECO:0000250|UniProtKB:P06733};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis,
CC involved in various processes such as growth control, hypoxia tolerance
CC and allergic responses. May also function in the intravascular and
CC pericellular fibrinolytic system due to its ability to serve as a
CC receptor and activator of plasminogen on the cell surface of several
CC cell-types such as leukocytes and neurons. Stimulates immunoglobulin
CC production. {ECO:0000250|UniProtKB:P06733}.
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. {ECO:0000250|UniProtKB:P06733}.
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|UniProtKB:P06733}. Cell
CC membrane {ECO:0000250|UniProtKB:P06733}. Note=Can translocate to the
CC plasma membrane in either the homodimeric (alpha/alpha) or
CC heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band.
CC {ECO:0000250|UniProtKB:P06733}.
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:0000255}.
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 AlphaFoldDB; P86210; -.
DR SMR; P86210; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
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 Gene3D; 3.20.20.120; -; 2.
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 PANTHER; PTHR11902; PTHR11902; 3.
DR Pfam; PF00113; Enolase_C; 2.
DR SMART; SM01192; Enolase_C; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Glycolysis; Lyase; Magnesium;
KW Membrane; Metal-binding; Phosphoprotein; Plasminogen activation;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN <1..223
FT /note="Alpha-enolase"
FT /id="PRO_0000394395"
FT REGION <202..223
FT /note="Required for interaction with PLG"
FT /evidence="ECO:0000250|UniProtKB:P04764"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56252"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56252"
FT BINDING 168..171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56252"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56252"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 87
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 87
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 87
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 215
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 215
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT UNSURE 111
FT /note="S or T"
FT NON_CONS 18..19
FT /evidence="ECO:0000305"
FT NON_CONS 34..35
FT /evidence="ECO:0000305"
FT NON_CONS 51..52
FT /evidence="ECO:0000305"
FT NON_CONS 87..88
FT /evidence="ECO:0000305"
FT NON_CONS 107..108
FT /evidence="ECO:0000305"
FT NON_CONS 128..129
FT /evidence="ECO:0000305"
FT NON_CONS 201..202
FT /evidence="ECO:0000305"
FT NON_CONS 215..216
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 223 AA; 23837 MW; 06EB554BA921BA8C CRC64;
AAVPSGASTG IYEALELRAV EHINKTIAPA LVSKLAMQEF MILPVGASSF RIGAEVYHNL
KDATNVGDEG GFAPNILENK EALELLKAGY TDQVVIGMDV AASEFYRFTA SAGIQVVGDD
LTVTNPKRAA SEKSCNCLLL KVNQIGSVTE SLQACKLAQS NGWGVMVSHR SGETEDTFIA
DLVVGLCTGQ IKTGAPCRSE RYNQILRIEE ELGSKSFRNP LAK
