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UniProtKB/Swiss-Prot entry P04764


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ENOA_RAT
Primary accession number P04764
Secondary accession numbers Q66HI3 Q6AYV3 Q6P504
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 94)
Name and origin of the protein
Protein name Alpha-enolase
Synonyms EC 4.2.1.11
2-phospho-D-glycerate hydro-lyase
Non-neural enolase
NNE
Enolase 1
Gene name
Name: Eno1
Synonyms: Eno-1
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Liver;
DOI=10.1093/nar/13.12.4365; PubMed=2989793 [NCBI, ExPASy, EBI, Israel, Japan]
Sakimura K., Kushiya E., Obinata M., Takahashi Y.;
"Molecular cloning and the nucleotide sequence of cDNA to mRNA for non-neuronal enolase (alpha alpha enolase) of rat brain and liver.";
Nucleic Acids Res. 13:4365-4378(1985).
[2]
SEQUENCE REVISION.
Takahashi Y.;
Submitted (JAN-1986) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart, Pituitary, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 10-28; 33-50; 72-103; 106-120; 163-179; 184-193; 203-228; 234-262; 270-281; 307-326; 336-394 AND 407-420, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 46-57; 97-109; 245-262 AND 369-382, AND INTERACTION WITH PLG.
TISSUE=Embryonic brain;
PubMed=7964722 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K., Kohsaka S.;
"Plasminogen binds specifically to alpha-enolase on rat neuronal plasma membrane.";
J. Neurochem. 63:2048-2057(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 93-153.
TISSUE=Lymphoma;
Bole-Feysot C., Kelly P.A.;
"Rat cDNA encoding alpha enolase (2-phospho-D-glycerate hydro-lyase) (non-neural enolase) (NNE).";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[7]
DEVELOPMENTAL STAGE.
PubMed=8594891 [NCBI, ExPASy, EBI, Israel, Japan]
Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.;
"Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy.";
Am. J. Physiol. 269:H1843-H1851(1995).
[8]
EFFECT OF THYROID HORMONES ON EXPRESSION.
PubMed=10662718 [NCBI, ExPASy, EBI, Israel, Japan]
Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L., Rappaport L., Lamande N., Lucas M.;
"Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development.";
Am. J. Physiol. 278:E330-E339(2000).
[9]
SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
DOI=10.1016/j.neures.2003.12.006; PubMed=15041191 [NCBI, ExPASy, EBI, Israel, Japan]
Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H.;
"Localization of enolase in synaptic plasma membrane as an alphagamma heterodimer in rat brain.";
Neurosci. Res. 48:379-386(2004).
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. 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.
  • CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
  • COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
  • 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 (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.
  • 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. In brain, levels of ENO1 decrease around 10 dpc and then gradually increase to adult age. In embryonic heart, ENO1 levels decrease rapidly during cardiac development.
  • SIMILARITY: Belongs to the enolase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X02610; CAA26456.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063174; AAH63174.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078896; AAH78896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081847; AAH81847.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF241613; AAK01319.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23126; A23126.
RefSeq NP_001103378.1; -.
NP_036686.2; -.
UniGene Rn.4236
3D structure databases
HSSP P56252; 1PDZ. [HSSP ENTRY / PDB]
SMR P04764; 2-431.
ModBase P04764.
Protein-protein interaction databases
IntAct P04764; -.
PTM databases
PhosphoSite P04764; -.
Organism-specific databases
RGD 2553; Eno1.
Gene expression databases
GermOnline ENSRNOG00000017895; Rattus norvegicus.
Family and domain databases
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS P04764.
Genome annotation databases
Ensembl ENSRNOG00000017895; Rattus norvegicus. [Contig view]
GeneID 24333; -.
KEGG rno:24333; -.
Phylogenomic databases
HOVERGEN P04764; -.
Other
ProtoNet P04764.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein; Plasminogen activation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   434  433     Alpha-enolase. PRO_0000134099
REGION   370   373  4     Substrate binding (By similarity). 
REGION   405   434  30     Required for interaction with PLG. 
ACT_SITE   210   210        Proton donor (By similarity). 
ACT_SITE   343   343        Proton acceptor (By similarity). 
METAL   245   245        Magnesium (By similarity). 
METAL   293   293        Magnesium (By similarity). 
METAL   318   318        Magnesium (By similarity). 
BINDING   158   158        Substrate (By similarity). 
BINDING   167   167        Substrate (By similarity). 
BINDING   293   293        Substrate (By similarity). 
BINDING   318   318        Substrate (By similarity). 
BINDING   394   394        Substrate (By similarity). 
MOD_RES   44    44        Phosphotyrosine (By similarity). 
MOD_RES   63    63        Phosphoserine (By similarity). 
MOD_RES   71    71        N6-acetyllysine (By similarity). 
MOD_RES   72    72        Phosphothreonine (By similarity). 
MOD_RES   263   263        Phosphoserine (By similarity). 
MOD_RES   287   287        Phosphotyrosine (By similarity). 
CONFLICT   48    48        E -> Q (in Ref. 5; AA sequence). 
CONFLICT   93    96        LMIE -> DQIK (in Ref. 6). 
CONFLICT   125   125        E -> G (in Ref. 1; CAA26456). 
CONFLICT   144   144        I -> T (in Ref. 1; CAA26456). 
CONFLICT   151   151        N -> D (in Ref. 6). 
CONFLICT   250   250        E -> Q (in Ref. 5; AA sequence). 
CONFLICT   374   374        G -> E (in Ref. 1; CAA26456). 
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 47128 Da [This is the MW of the unprocessed precursor] CRC64: 736660B2D5E936DC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSILKIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK 

        70         80         90        100        110        120 
GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DQLMIEMDGT ENKSKFGANA ILGVSLAVCK 

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

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

       250        260        270        280        290        300 
VIGMDVAASE FYRAGKYDLD FKSPDDASRY ITPDQLADLY KSFIKDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WDAWQKFTAT AGIQVVGDDL TVTNPKRIAK AAGEKSCNCL LLKVNQIGSV TESLQACKLA 

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

       430 
AKFAGRSFRN PLAK 

P04764 in FASTA format

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