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P04764

- ENOA_RAT

UniProt

P04764 - ENOA_RAT

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Protein
Alpha-enolase
Gene
Eno1, Eno-1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.UniRule annotation

Catalytic activityi

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

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 1 By similarity
Binding sitei158 – 1581Substrate By similarity
Binding sitei167 – 1671Substrate By similarity
Active sitei210 – 2101Proton donor By similarity
Metal bindingi245 – 2451Magnesium 2 By similarity
Metal bindingi293 – 2931Magnesium 2 By similarity
Binding sitei293 – 2931Substrate By similarity
Metal bindingi318 – 3181Magnesium 2 By similarity
Binding sitei318 – 3181Substrate By similarity
Active sitei343 – 3431Proton acceptor By similarity
Binding sitei394 – 3941Substrate By 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
Complete GO annotation...

GO - Biological processi

  1. glycolytic process Source: RGD
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 434433Alpha-enolaseUniRule annotation
PRO_0000134099Add
BLAST

Amino acid modifications

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

Post-translational modificationi

ISGylated By similarity.UniRule annotation

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.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP04764.
SMRiP04764. Positions 2-434.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate binding By similarity
Regioni405 – 43430Required for interaction with PLGUniRule annotation
Add
BLAST

Sequence similaritiesi

Belongs to the enolase family.

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

« Hide

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.

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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