MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Alpha-enolase {ECO:0000250|UniProtKB:P06733}; EC=4.2.1.11; AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000250|UniProtKB:P06733}; AltName: Full=Enolase 1 {ECO:0000250|UniProtKB:P06733}; AltName: Full=Non-neural enolase {ECO:0000250|UniProtKB:P06733}; Short=NNE {ECO:0000250|UniProtKB:P06733}; Flags: Fragments; |
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| MyHits synonyms | ENOA_MESAU , P86210 , 06EB554BA921BA8C |
 Legends: 1, ACT_SITE Proton donor. {ECO:0000250|UniProtKB:P06733}; 2, ACT_SITE Proton acceptor. {ECO:0000250|UniProtKB:P06733}; 3, Magnesium 1. {ECO:0000250}; 4, Magnesium 2. {ECO:0000250}; 5, BINDING Substrate. {ECO:0000250|UniProtKB:P56252}; 6, Phosphotyrosine. {ECO:0000250|UniProtKB:P06733}; 7, N6-acetyllysine. {ECO:0000250|UniProtKB:P06733}; 8, N6-acetyllysine; alternate. {ECO:0000250|UniProtKB:P06733}; 9, N6-malonyllysine; alternate. {ECO:0000250}; 10, N6-succinyllysine; alternate. {ECO:0000250|UniProtKB:P17182}; 11, N6-acetyllysine. {ECO:0000250|UniProtKB:P17182}; 12, REGION Substrate binding. {ECO:0000250|UniProtKB:P56252}; 13, NON_CONS {ECO:0000305}; 14, ipat:ENOLASE [T].
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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 30-NOV-2016, entry version 28.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; 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.,
RA Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection
RT antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Multifunctional enzyme that, as well as its role in
CC glycolysis, plays a part in various processes such as growth
CC control, hypoxia tolerance and allergic responses. May also
CC function in the intravascular and pericellular fibrinolytic system
CC due to its ability to serve as a receptor and activator of
CC plasminogen on the cell surface of several cell-types such as
CC leukocytes and neurons. Stimulates immunoglobulin production (By
CC similarity). {ECO:0000250|UniProtKB:P06733}.
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC H(2)O. {ECO:0000250|UniProtKB:P06733}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds two Mg(2+) per subunit. Required for catalysis and for
CC stabilizing the dimer. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC {ECO:0000250|UniProtKB:P06733}.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
CC alpha, beta and gamma, which can form homodimers or heterodimers
CC which are cell-type and development-specific. ENO1 interacts with
CC PLG in the neuronal plasma membrane and promotes its activation.
CC The C-terminal lysine is required for this binding. Interacts with
CC ENO4 and PGAM2 (By similarity). {ECO:0000250|UniProtKB:P06733,
CC ECO:0000250|UniProtKB:P17182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06733}.
CC Cell membrane {ECO:0000250|UniProtKB:P06733}. Note=Can translocate
CC to the 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}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255}.
DR ProteinModelPortal; P86210; -.
DR PRIDE; P86210; -.
DR UniPathway; UPA00109; UER00187.
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; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.120; -; 2.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR029017; Enolase_N-like.
DR PANTHER; PTHR11902; PTHR11902; 1.
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 Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN <1 223 Alpha-enolase.
FT /FTId=PRO_0000394395.
FT REGION 168 171 Substrate binding.
FT {ECO:0000250|UniProtKB:P56252}.
FT REGION <202 223 Required for interaction with PLG.
FT {ECO:0000250|UniProtKB:P04764}.
FT ACT_SITE 69 69 Proton donor.
FT {ECO:0000250|UniProtKB:P06733}.
FT ACT_SITE 141 141 Proton acceptor.
FT {ECO:0000250|UniProtKB:P06733}.
FT METAL 8 8 Magnesium 1. {ECO:0000250}.
FT METAL 99 99 Magnesium 2. {ECO:0000250}.
FT METAL 119 119 Magnesium 2. {ECO:0000250}.
FT BINDING 39 39 Substrate.
FT {ECO:0000250|UniProtKB:P56252}.
FT BINDING 119 119 Substrate.
FT {ECO:0000250|UniProtKB:P56252}.
FT BINDING 192 192 Substrate.
FT {ECO:0000250|UniProtKB:P56252}.
FT MOD_RES 12 12 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:P06733}.
FT MOD_RES 25 25 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P06733}.
FT MOD_RES 61 61 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P06733}.
FT MOD_RES 87 87 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P06733}.
FT MOD_RES 87 87 N6-malonyllysine; alternate.
FT {ECO:0000250}.
FT MOD_RES 87 87 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 133 133 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 141 141 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 215 215 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P06733}.
FT MOD_RES 215 215 N6-malonyllysine; alternate.
FT {ECO:0000250}.
FT MOD_RES 215 215 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT UNSURE 111 111 S or T.
FT NON_CONS 18 19 {ECO:0000305}.
FT NON_CONS 34 35 {ECO:0000305}.
FT NON_CONS 51 52 {ECO:0000305}.
FT NON_CONS 87 88 {ECO:0000305}.
FT NON_CONS 107 108 {ECO:0000305}.
FT NON_CONS 128 129 {ECO:0000305}.
FT NON_CONS 201 202 {ECO:0000305}.
FT NON_CONS 215 216 {ECO:0000305}.
FT NON_TER 1 1
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 33 107 ipfam:Enolase_C [T]
FT MYHIT 110 216 ipfam:Enolase_C [T]
FT MYHIT 138 151 ipat:ENOLASE [T]
FT MYHIT 24 220 ismart:Enolase_C [T]
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
//
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