Alpha-enolase - Bos taurus (Bovine)

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Reviewed, UniProtKB/Swiss-Prot Q9XSJ4 (ENOA_BOVIN)

Last modified July 22, 2008. Version 67. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Alpha-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Non-neural enolase
      Short name=NNE
    Enolase 1
    Phosphopyruvate hydratase
    HAP47

Gene names

Name:

ENO1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 By similarity.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
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 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.
Subcellular location	CytoplasmBy similarity. Cell membraneBy 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.
Sequence similarities	Belongs to the enolase family.

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Ontologies

Keywords
Biological process	Glycolysis Plasminogen activation
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: AgBase
Molecular function	phosphopyruvate hydratase activity Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 434

433

Alpha-enolase

PRO_0000134096

Regions

Region

370 – 373

Substrate binding By similarity

Region

405 – 434

Required for interaction with PLG By similarity

Sites

Active site

210

Proton donor By similarity

Active site

343

Proton acceptor By similarity

Metal binding

245

Magnesium By similarity

Metal binding

293

Magnesium By similarity

Metal binding

318

Magnesium By similarity

Binding site

158

Substrate By similarity

Binding site

167

Substrate By similarity

Binding site

293

Substrate By similarity

Binding site

318

Substrate By similarity

Binding site

394

Substrate By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

263

Phosphoserine By similarity

Modified residue

287

Phosphotyrosine By similarity

Experimental info

Sequence conflict

L → S in AAD33073. Ref.1

Sequence conflict

102

N → K in AAD33073. Ref.1

Sequence conflict

324

N → T in AAD33073. Ref.1

Sequence conflict

327

R → T in AAD33073. Ref.1

Sequence conflict

331 – 333

AVS → GVN in AAD33073. Ref.1

Sequence conflict

347

I → N in AAD33073. Ref.1

Sequence conflict

356

A → G in AAD33073. Ref.1

Sequence conflict

361 – 362

QS → HA in AAD33073. Ref.1

Sequence conflict

377

E → D in AAD33073. Ref.1

Sequence conflict

383

D → E in AAD33073. Ref.1

Sequence conflict

395 – 397

TVA → NGP in AAD33073. Ref.1

Sequence conflict

401

S → T in AAD33073. Ref.1

Sequence conflict

427

S → N in AAD33073. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9XSJ4-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 91E2A06F073C5121
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FASTA

434

47,326

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alpha enolase is upregulated in proliferative chondrocytes in the epiphyseal growth plate and in human osteoarthritic tissue." Chapman K.L., Newman B., Hillaby M.C., Freemont A.J., Grant M.E., Boot-Handford R., Wallis G.A. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[3]	"Non-neuronal enolase is an endothelial hypoxic stress protein." Aaronson R.M., Graven K.K., Tucci M., McDonald R.J., Farber H.W. J. Biol. Chem. 270:27752-27757(1995) [PubMed: 7499243] [Abstract] Cited for: PROTEIN SEQUENCE OF 270-281 AND 373-394, FUNCTION AS AN ENDOTHELIAL HYPOXIC STRESS PROTEIN.

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Cross-references

Sequence databases
	AF149256 mRNA. Translation: AAD33073.1. BC103354 mRNA. Translation: AAI03355.1.
RefSeq	NP_776474.2.
UniGene	Bt.22783
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
SMR	Q9XSJ4. Positions 2-431.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000013411. Bos taurus. [Contig view]
GeneID	281141.
KEGG	bta:281141.
Phylogenomic databases
HOVERGEN	Q9XSJ4.
Family and domain databases
InterPro	IPR000941. Enolase. [Graphical view]
PANTHER	PTHR11902. Enolase. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...

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Entry information

Entry name

ENOA_BOVIN

Accession

Primary (citable) accession number: Q9XSJ4
Secondary accession number(s): Q3SYW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 67 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents