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UniProtKB/Swiss-Prot entry Q9XSJ4


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

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Entry information
Entry name ENOA_BOVIN
Primary accession number Q9XSJ4
Secondary accession number Q3SYW4
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 67)
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
Phosphopyruvate hydratase
HAP47
Gene name
Name: ENO1
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Chapman K.L., Newman B., Hillaby M.C., Freemont A.J., Grant M.E., Boot-Handford R., Wallis G.A.;
"Alpha enolase is upregulated in proliferative chondrocytes in the epiphyseal growth plate and in human osteoarthritic tissue.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus;
TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 270-281 AND 373-394, AND FUNCTION AS AN ENDOTHELIAL HYPOXIC STRESS PROTEIN.
DOI=10.1074/jbc.270.46.27752; PubMed=7499243 [NCBI, ExPASy, EBI, Israel, Japan]
Aaronson R.M., Graven K.K., Tucci M., McDonald R.J., Farber H.W.;
"Non-neuronal enolase is an endothelial hypoxic stress protein.";
J. Biol. Chem. 270:27752-27757(1995).
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 (By similarity).
  • CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
  • COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer (By similarity).
  • 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 (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 (By similarity).
  • 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.
  • INDUCTION: Expression increased up to 3-fold by hypoxic stress in vascular endothelial cells.
  • 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
AF149256; AAD33073.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC103354; AAI03355.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_776474.2; -.
UniGene Bt.22783
3D structure databases
HSSP Q9NDH8; 1OEP. [HSSP ENTRY / PDB]
SMR Q9XSJ4; 2-431.
ModBase Q9XSJ4.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from AgBase).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (inferred from sequence or structural similarity from AgBase).
QuickGo view.
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 Q9XSJ4.
Genome annotation databases
Ensembl ENSBTAG00000013411; Bos taurus. [Contig view]
GeneID 281141; -.
KEGG bta:281141; -.
Phylogenomic databases
HOVERGEN Q9XSJ4; -.
Other
ProtoNet Q9XSJ4.
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. 
CHAIN   2   434  433     Alpha-enolase. PRO_0000134096
REGION   370   373  4     Substrate binding (By similarity). 
REGION   405   434  30     Required for interaction with PLG (By similarity). 
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   57    57        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   82    82        L -> S (in Ref. 1; AAD33073). 
CONFLICT   102   102        N -> K (in Ref. 1; AAD33073). 
CONFLICT   324   324        N -> T (in Ref. 1; AAD33073). 
CONFLICT   327   327        R -> T (in Ref. 1; AAD33073). 
CONFLICT   331   333        AVS -> GVN (in Ref. 1; AAD33073). 
CONFLICT   347   347        I -> N (in Ref. 1; AAD33073). 
CONFLICT   356   356        A -> G (in Ref. 1; AAD33073). 
CONFLICT   361   362        QS -> HA (in Ref. 1; AAD33073). 
CONFLICT   377   377        E -> D (in Ref. 1; AAD33073). 
CONFLICT   383   383        D -> E (in Ref. 1; AAD33073). 
CONFLICT   395   397        TVA -> NGP (in Ref. 1; AAD33073). 
CONFLICT   401   401        S -> T (in Ref. 1; AAD33073). 
CONFLICT   427   427        S -> N (in Ref. 1; AAD33073). 
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 47326 Da [This is the MW of the unprocessed precursor] CRC64: 91E2A06F073C5121 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSILKVHARE IFDSRGNPTV EVDLFTAKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK 

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

       130        140        150        160        170        180 
AGAVEKGVPL YRHIADLAGN AEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAENFRE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKNA IGKAGYSDKV 

       250        260        270        280        290        300 
VIGMDVAASE FYRSGKYDLD FKSPDDPSRY ITPDELANLY KSFIRDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WEAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVSEKSCNCL LLKVNQIGSV TESLQACKLA 

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

       430 
AKFAGRSFRN PLAK 

Q9XSJ4 in FASTA format

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