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P04764

- ENOA_RAT

UniProt

P04764 - ENOA_RAT

Protein

Alpha-enolase

Gene

Eno1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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. Stimulates immunoglobulin production.

    Catalytic activityi

    2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi40 – 401Magnesium 1By similarity
    Binding sitei158 – 1581SubstrateBy similarity
    Binding sitei167 – 1671SubstrateBy similarity
    Active sitei210 – 2101Proton donorBy similarity
    Metal bindingi245 – 2451Magnesium 2By similarity
    Metal bindingi293 – 2931Magnesium 2By similarity
    Binding sitei293 – 2931SubstrateBy similarity
    Metal bindingi318 – 3181Magnesium 2By similarity
    Binding sitei318 – 3181SubstrateBy similarity
    Active sitei343 – 3431Proton acceptorBy similarity
    Binding sitei394 – 3941SubstrateBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphopyruvate hydratase activity Source: RGD
    3. protein heterodimerization activity Source: RGD
    4. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. glycolytic process Source: RGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis, Plasminogen activation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_217998. Gluconeogenesis.
    REACT_225694. Glycolysis.
    SABIO-RKP04764.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Eno1
    Synonyms:Eno-1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 5

    Organism-specific databases

    RGDi2553. Eno1.

    Subcellular locationi

    Cytoplasm. Cell membrane
    Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.

    GO - Cellular componenti

    1. neuron projection Source: RGD
    2. phosphopyruvate hydratase complex Source: InterPro
    3. synaptic membrane Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 434433Alpha-enolasePRO_0000134099Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei5 – 51N6-acetyllysineBy similarity
    Modified residuei44 – 441PhosphotyrosineBy similarity
    Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
    Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
    Modified residuei64 – 641N6-acetyllysineBy similarity
    Modified residuei71 – 711N6-acetyllysineBy similarity
    Modified residuei89 – 891N6-acetyllysine; alternateBy similarity
    Modified residuei89 – 891N6-succinyllysine; alternateBy similarity
    Modified residuei126 – 1261N6-acetyllysineBy similarity
    Modified residuei193 – 1931N6-acetyllysineBy similarity
    Modified residuei199 – 1991N6-acetyllysineBy similarity
    Modified residuei202 – 2021N6-acetyllysineBy similarity
    Modified residuei228 – 2281N6-acetyllysine; alternateBy similarity
    Modified residuei228 – 2281N6-succinyllysine; alternateBy similarity
    Modified residuei233 – 2331N6-acetyllysine; alternateBy similarity
    Modified residuei233 – 2331N6-malonyllysine; alternateBy similarity
    Modified residuei256 – 2561N6-acetyllysineBy similarity
    Modified residuei263 – 2631PhosphoserineBy similarity
    Modified residuei281 – 2811N6-acetyllysineBy similarity
    Modified residuei285 – 2851N6-acetyllysineBy similarity
    Modified residuei287 – 2871PhosphotyrosineBy similarity
    Modified residuei335 – 3351N6-acetyllysineBy similarity
    Modified residuei343 – 3431N6-acetyllysineBy similarity
    Modified residuei406 – 4061N6-acetyllysineBy similarity
    Modified residuei420 – 4201N6-acetyllysine; alternateBy similarity
    Modified residuei420 – 4201N6-malonyllysine; alternateBy similarity
    Modified residuei420 – 4201N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    ISGylated.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP04764.
    PRIDEiP04764.

    2D gel databases

    World-2DPAGE0004:P04764.

    PTM databases

    PhosphoSiteiP04764.

    Expressioni

    Tissue specificityi

    Expressed in flagella of epididymal sperm. 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.1 Publication

    Developmental stagei

    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.2 Publications

    Gene expression databases

    GenevestigatoriP04764.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi246510. 2 interactions.
    IntActiP04764. 4 interactions.
    MINTiMINT-4575756.

    Structurei

    3D structure databases

    ProteinModelPortaliP04764.
    SMRiP04764. Positions 2-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 3734Substrate bindingBy similarity
    Regioni405 – 43430Required for interaction with PLGAdd
    BLAST

    Sequence similaritiesi

    Belongs to the enolase family.Curated

    Phylogenomic databases

    eggNOGiCOG0148.
    HOGENOMiHOG000072174.
    HOVERGENiHBG000067.
    InParanoidiP04764.
    KOiK01689.
    OMAiVSEKSCN.
    OrthoDBiEOG776SQ1.
    PhylomeDBiP04764.
    TreeFamiTF300391.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPiMF_00318. Enolase.
    InterProiIPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N_like.
    [Graphical view]
    PANTHERiPTHR11902. PTHR11902. 1 hit.
    PfamiPF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001400. Enolase. 1 hit.
    PRINTSiPR00148. ENOLASE.
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsiTIGR01060. eno. 1 hit.
    PROSITEiPS00164. ENOLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04764-1 [UniParc]FASTAAdd to Basket

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    MSILKIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR    50
    DNDKTRFMGK GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DQLMIEMDGT 100
    ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN PEVILPVPAF 150
    NVINGGSHAG NKLAMQEFMI LPVGASSFRE AMRIGAEVYH NLKNVIKEKY 200
    GKDATNVGDE GGFAPNILEN KEALELLKSA IAKAGYTDQV VIGMDVAASE 250
    FYRAGKYDLD FKSPDDASRY ITPDQLADLY KSFIKDYPVV SIEDPFDQDD 300
    WDAWQKFTAT AGIQVVGDDL TVTNPKRIAK AAGEKSCNCL LLKVNQIGSV 350
    TESLQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
    SERLAKYNQI LRIEEELGSK AKFAGRSFRN PLAK 434
    Length:434
    Mass (Da):47,128
    Last modified:January 23, 2007 - v4
    Checksum:i736660B2D5E936DC
    GO

    Sequence cautioni

    The sequence AAH63174.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481E → Q AA sequence (PubMed:7964722)Curated
    Sequence conflicti93 – 964LMIE → DQIK in AAK01319. 1 PublicationCurated
    Sequence conflicti125 – 1251E → G in CAA26456. (PubMed:2989793)Curated
    Sequence conflicti144 – 1441I → T in CAA26456. (PubMed:2989793)Curated
    Sequence conflicti151 – 1511N → D in AAK01319. 1 PublicationCurated
    Sequence conflicti250 – 2501E → Q AA sequence (PubMed:7964722)Curated
    Sequence conflicti374 – 3741G → E in CAA26456. (PubMed:2989793)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02610 mRNA. Translation: CAA26456.1.
    BC063174 mRNA. Translation: AAH63174.1. Different initiation.
    BC078896 mRNA. Translation: AAH78896.1.
    BC081847 mRNA. Translation: AAH81847.2.
    AF241613 mRNA. Translation: AAK01319.1.
    PIRiA23126.
    RefSeqiNP_001103378.1. NM_001109908.1.
    NP_036686.2. NM_012554.3.
    XP_006239505.1. XM_006239443.1.
    UniGeneiRn.117044.
    Rn.4236.

    Genome annotation databases

    EnsembliENSRNOT00000024106; ENSRNOP00000024106; ENSRNOG00000017895.
    GeneIDi24333.
    KEGGirno:24333.
    UCSCiRGD:2553. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02610 mRNA. Translation: CAA26456.1 .
    BC063174 mRNA. Translation: AAH63174.1 . Different initiation.
    BC078896 mRNA. Translation: AAH78896.1 .
    BC081847 mRNA. Translation: AAH81847.2 .
    AF241613 mRNA. Translation: AAK01319.1 .
    PIRi A23126.
    RefSeqi NP_001103378.1. NM_001109908.1.
    NP_036686.2. NM_012554.3.
    XP_006239505.1. XM_006239443.1.
    UniGenei Rn.117044.
    Rn.4236.

    3D structure databases

    ProteinModelPortali P04764.
    SMRi P04764. Positions 2-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246510. 2 interactions.
    IntActi P04764. 4 interactions.
    MINTi MINT-4575756.

    PTM databases

    PhosphoSitei P04764.

    2D gel databases

    World-2DPAGE 0004:P04764.

    Proteomic databases

    PaxDbi P04764.
    PRIDEi P04764.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000024106 ; ENSRNOP00000024106 ; ENSRNOG00000017895 .
    GeneIDi 24333.
    KEGGi rno:24333.
    UCSCi RGD:2553. rat.

    Organism-specific databases

    CTDi 2023.
    RGDi 2553. Eno1.

    Phylogenomic databases

    eggNOGi COG0148.
    HOGENOMi HOG000072174.
    HOVERGENi HBG000067.
    InParanoidi P04764.
    KOi K01689.
    OMAi VSEKSCN.
    OrthoDBi EOG776SQ1.
    PhylomeDBi P04764.
    TreeFami TF300391.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00187 .
    Reactomei REACT_217998. Gluconeogenesis.
    REACT_225694. Glycolysis.
    SABIO-RK P04764.

    Miscellaneous databases

    NextBioi 603015.
    PROi P04764.

    Gene expression databases

    Genevestigatori P04764.

    Family and domain databases

    Gene3Di 3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPi MF_00318. Enolase.
    InterProi IPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N_like.
    [Graphical view ]
    PANTHERi PTHR11902. PTHR11902. 1 hit.
    Pfami PF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001400. Enolase. 1 hit.
    PRINTSi PR00148. ENOLASE.
    SUPFAMi SSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsi TIGR01060. eno. 1 hit.
    PROSITEi PS00164. ENOLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and the nucleotide sequence of cDNA to mRNA for non-neuronal enolase (alpha alpha enolase) of rat brain and liver."
      Sakimura K., Kushiya E., Obinata M., Takahashi Y.
      Nucleic Acids Res. 13:4365-4378(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
      Tissue: Brain and Liver.
    2. Takahashi Y.
      Submitted (JAN-1986) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    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].
      Tissue: Heart, Pituitary and Testis.
    4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain, Hippocampus and Spinal cord.
    5. "Plasminogen binds specifically to alpha-enolase on rat neuronal plasma membrane."
      Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K., Kohsaka S.
      J. Neurochem. 63:2048-2057(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-57; 97-109; 245-262 AND 369-382, INTERACTION WITH PLG.
      Tissue: Embryonic brain.
    6. "Rat cDNA encoding alpha enolase (2-phospho-D-glycerate hydro-lyase) (non-neural enolase) (NNE)."
      Bole-Feysot C., Kelly P.A.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-153.
      Tissue: Lymphoma.
    7. "Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."
      Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.
      Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    8. "Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development."
      Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L., Rappaport L., Lamande N., Lucas M.
      Am. J. Physiol. 278:E330-E339(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Localization of enolase in synaptic plasma membrane as an alphagamma heterodimer in rat brain."
      Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H.
      Neurosci. Res. 48:379-386(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
    10. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
      Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
      Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiENOA_RAT
    AccessioniPrimary (citable) accession number: P04764
    Secondary accession number(s): Q66HI3, Q6AYV3, Q6P504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3