[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Muscle; Zheng S.-X.; "The cDNA cloning of rabbit muscle-specific enolase gene, site directed mutagenesis (E417L) of the gene, expression of the wild-type and mutant genes in Escherichia coli."; Thesis (1995), Concordia University / Montreal, Canada.
[2]	SEQUENCE REVISION TO 297-309 AND 315. Kornblatt M.J., Zheng S.-X., Lamande N., Lazar M.; Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 2-434. TISSUE=Muscle; DOI=10.1007/BF01024618; PubMed=2275753 [NCBI, ExPASy, EBI, Israel, Japan] Chin C.C.Q.; "The primary structure of rabbit muscle enolase."; J. Protein Chem. 9:427-432(1990).
[4]	SUBCELLULAR LOCATION. DOI=10.1042/0264-6021:3380115; PubMed=9931306 [NCBI, ExPASy, EBI, Israel, Japan] Foucault G., Vacher M., Merkulova T., Keller A., Arrio-Dupont M.; "Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase."; Biochem. J. 338:115-121(1999).

Comments

FUNCTION: Appears to have a function in striated muscle development and regeneration.
CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.
COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
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. Interacts with PNKD (By similarity).
SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line (By similarity). Some colocalization with CKM at M-band.
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.
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

AF260259; AAF71925.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A37210; A37210.

NP_001075554.1; -.

3D structure databases

HSSP

P56252; 1PDZ. [HSSP ENTRY / PDB]

SMR

P25704; 2-431.

ModBase

P25704.

Ontologies

GO:0000015;	Cellular component: phosphopyruvate hydratase complex (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004634;	Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
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]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Genome annotation databases

GeneID

100008769; -.

Phylogenomic databases

HOVERGEN

P25704; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 434`	`433`	`Beta-enolase.`	`PRO_0000134109`
`REGION`	`370 373`	`4`	`Substrate binding (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).`
`CONFLICT`	`254 254`		`N -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`299 309`		`DDWATWTSFLS -> GDWGAWSRFLA (in Ref. 3; AA sequence).`
`CONFLICT`	`315 315`		`I -> V (in Ref. 3; AA sequence).`

Sequence information

Length: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 47069 Da [This is the MW of the unprocessed precursor]

CRC64: E0DB6CE8EA2C3214 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKSRYLGK 

        70         80         90        100        110        120 
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN HDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE 

       190        200        210        220        230        240 
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 

       250        260        270        280        290        300 
VIGMDVAASE FHRNGKYDLD FKSPDDPARH ITGQKLGELY KSFIKNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AVFAGRKFRN PKAK

P25704 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools