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P04764 (ENOA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. 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. 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. Ref.5

Subcellular location

Cytoplasm. Cell membrane. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. Ref.1 Ref.9

Tissue specificity

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. Ref.10

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. Ref.1 Ref.7

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_00318

Sequence similarities

Belongs to the enolase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Alpha-enolase HAMAP-Rule MF_00318
PRO_0000134099

Regions

Region370 – 3734Substrate binding By similarity
Region405 – 43430Required for interaction with PLG HAMAP-Rule MF_00318

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 residue51N6-acetyllysine By similarity
Modified residue441Phosphotyrosine By similarity
Modified residue601N6-acetyllysine; alternate By similarity
Modified residue601N6-succinyllysine; alternate By similarity
Modified residue641N6-acetyllysine By similarity
Modified residue711N6-acetyllysine By similarity
Modified residue891N6-acetyllysine; alternate By similarity
Modified residue891N6-succinyllysine; alternate By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue1931N6-acetyllysine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine; alternate By similarity
Modified residue2281N6-succinyllysine; alternate By similarity
Modified residue2331N6-acetyllysine; alternate By similarity
Modified residue2331N6-malonyllysine; alternate By similarity
Modified residue2561N6-acetyllysine By similarity
Modified residue2631Phosphoserine By similarity
Modified residue2811N6-acetyllysine By similarity
Modified residue2851N6-acetyllysine By similarity
Modified residue2871Phosphotyrosine By similarity
Modified residue3351N6-acetyllysine By similarity
Modified residue3431N6-acetyllysine By similarity
Modified residue4061N6-acetyllysine By similarity
Modified residue4201N6-acetyllysine; alternate By similarity
Modified residue4201N6-malonyllysine; alternate By similarity
Modified residue4201N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict481E → Q AA sequence Ref.5
Sequence conflict93 – 964LMIE → DQIK in AAK01319. Ref.6
Sequence conflict1251E → G in CAA26456. Ref.1
Sequence conflict1441I → T in CAA26456. Ref.1
Sequence conflict1511N → D in AAK01319. Ref.6
Sequence conflict2501E → Q AA sequence Ref.5
Sequence conflict3741G → E in CAA26456. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04764 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 736660B2D5E936DC

FASTA43447,128
        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 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA23126.
RefSeqNP_001103378.1. NM_001109908.1.
NP_036686.2. NM_012554.3.
XP_006239505.1. XM_006239443.1.
UniGeneRn.117044.
Rn.4236.

3D structure databases

ProteinModelPortalP04764.
SMRP04764. Positions 2-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246510. 2 interactions.
IntActP04764. 4 interactions.
MINTMINT-4575756.

PTM databases

PhosphoSiteP04764.

2D gel databases

World-2DPAGE0004:P04764.

Proteomic databases

PaxDbP04764.
PRIDEP04764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024106; ENSRNOP00000024106; ENSRNOG00000017895.
GeneID24333.
KEGGrno:24333.
UCSCRGD:2553. rat.

Organism-specific databases

CTD2023.
RGD2553. Eno1.

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
HOVERGENHBG000067.
InParanoidP04764.
KOK01689.
OMAVSEKSCN.
OrthoDBEOG776SQ1.
PhylomeDBP04764.
TreeFamTF300391.

Enzyme and pathway databases

SABIO-RKP04764.
UniPathwayUPA00109; UER00187.

Gene expression databases

GenevestigatorP04764.

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

NextBio603015.
PROP04764.

Entry information

Entry nameENOA_RAT
AccessionPrimary (citable) accession number: P04764
Secondary accession number(s): Q66HI3, Q6AYV3, Q6P504
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 143 of the entry and version 4 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