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P17182 (ENOA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 1
Non-neural enolase
Short name=NNE
Gene names
Name:Eno1
Synonyms:Eno-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses By similarity. 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. Stimulates immunoglobulin production By similarity. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium. Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subunit structure

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 By similarity. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and aldolase. Also binds troponin, in vitro. Ref.6

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form By similarity. ENO1 is localized to the M-band. Ref.7

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. In striated muscle, expression of ENO1 appears to be independent of fiber type. Ref.7

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. In embryonic muscle, ENO1 is highly expressed until E17. Decreased levels from P5. Ref.6

Post-translational modification

ISGylated. Ref.8

Sequence similarities

Belongs to the enolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Alpha-enolase HAMAP-Rule MF_00318
PRO_0000134098

Regions

Region370 – 3734Substrate binding By similarity
Region405 – 43430Required for interaction with PLG By similarity

Sites

Active site2101Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding401Magnesium 1 By similarity
Metal binding2451Magnesium 2 By similarity
Metal binding2931Magnesium 2 By similarity
Metal binding3181Magnesium 2 By similarity
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2931Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue441Phosphotyrosine Ref.9
Modified residue601N6-acetyllysine; alternate Ref.10
Modified residue601N6-succinyllysine; alternate Ref.10
Modified residue711N6-acetyllysine By similarity
Modified residue891N6-acetyllysine; alternate Ref.10
Modified residue891N6-succinyllysine; alternate Ref.10
Modified residue921N6-acetyllysine Ref.10
Modified residue1261N6-acetyllysine Ref.10
Modified residue1931N6-acetyllysine Ref.10
Modified residue1991N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine Ref.10
Modified residue2281N6-acetyllysine; alternate Ref.10
Modified residue2281N6-succinyllysine; alternate Ref.10
Modified residue2331N6-acetyllysine; alternate By similarity
Modified residue2331N6-malonyllysine; alternate By similarity
Modified residue2541Phosphoserine By similarity
Modified residue2561N6-acetyllysine Ref.10
Modified residue2631Phosphoserine By similarity
Modified residue2811N6-acetyllysine By similarity
Modified residue2871Phosphotyrosine By similarity
Modified residue3351N6-acetyllysine Ref.10
Modified residue3431N6-acetyllysine Ref.10
Modified residue4061N6-acetyllysine Ref.10
Modified residue4201N6-acetyllysine; alternate By similarity
Modified residue4201N6-malonyllysine; alternate By similarity
Modified residue4201N6-succinyllysine; alternate Ref.10

Experimental info

Sequence conflict3591L → P in CAA36605. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17182 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DBEF6270A70DE3A6

FASTA43447,141
        10         20         30         40         50         60 
MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK 

        70         80         90        100        110        120 
GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAVEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV 

       250        260        270        280        290        300 
VIGMDVAASE FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK 

       430 
AKFAGRSFRN PLAK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse brain."
Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M., Lazar M., Caput D.
Nucleic Acids Res. 18:3638-3638(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary gland and Mammary tumor.
[4]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 10-28; 33-50; 61-120; 133-179; 184-193; 203-228; 234-253; 257-262; 270-281; 307-326; 344-358; 373-394 AND 413-420, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an alpha-enolase isoform."
Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I.
Arterioscler. Thromb. 13:264-275(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-71; 100-114; 184-198 AND 246-259.
Tissue: Macrophage.
[6]"Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
[7]"Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-92; LYS-126; LYS-193; LYS-202; LYS-228; LYS-256; LYS-335; LYS-343 AND LYS-406, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-228 AND LYS-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52379 mRNA. Translation: CAA36605.1.
AK002336 mRNA. Translation: BAB22021.1.
BC003891 mRNA. Translation: AAH03891.1.
BC004017 mRNA. Translation: AAH04017.1.
BC010685 mRNA. Translation: AAH10685.1.
BC024644 mRNA. Translation: AAH24644.1.
BC085098 mRNA. Translation: AAH85098.1.
CCDSCCDS18971.1.
PIRS10246.
RefSeqNP_001020559.1. NM_001025388.1.
NP_075608.2. NM_023119.2.
UniGeneMm.372357.
Mm.372389.
Mm.70666.

3D structure databases

ProteinModelPortalP17182.
SMRP17182. Positions 2-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199451. 16 interactions.
241069. 8 interactions.
IntActP17182. 13 interactions.
MINTMINT-4996502.

PTM databases

PhosphoSiteP17182.

2D gel databases

REPRODUCTION-2DPAGEIPI00462072.
P17182.
SWISS-2DPAGEP17182.
UCD-2DPAGEP17182.

Proteomic databases

MaxQBP17182.
PaxDbP17182.
PRIDEP17182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
GeneID13806.
433182.
KEGGmmu:13806.
mmu:433182.
UCSCuc008ewh.1. mouse.

Organism-specific databases

CTD2023.
433182.
MGIMGI:95393. Eno1.

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
HOVERGENHBG000067.
InParanoidP17182.
KOK01689.
OMAVSEKSCN.
OrthoDBEOG776SQ1.
PhylomeDBP17182.
TreeFamTF300391.

Enzyme and pathway databases

BRENDA4.2.1.11. 3474.
SABIO-RKP17182.
UniPathwayUPA00109; UER00187.

Gene expression databases

ArrayExpressP17182.
BgeeP17182.
GenevestigatorP17182.

Family and domain databases

Gene3D3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
SUPFAMSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284584.
PROP17182.
SOURCESearch...

Entry information

Entry nameENOA_MOUSE
AccessionPrimary (citable) accession number: P17182
Secondary accession number(s): Q99KT7, Q9DCY7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot