[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Skeletal muscle; DOI=10.1016/0014-5793(89)80515-0; PubMed=2914621 [NCBI, ExPASy, EBI, Israel, Japan] Ohshima Y., Mitsui H., Takayama Y., Kushiya E., Sakimura K., Takahashi Y.; "cDNA cloning and nucleotide sequence of rat muscle-specific enolase (beta beta enolase)."; FEBS Lett. 242:425-430(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Heart; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. DOI=10.1016/0014-5793(90)80813-X; PubMed=2269373 [NCBI, ExPASy, EBI, Israel, Japan] Sakimura K., Kushiya E., Ohshima-Ichimura Y., Mitsui H., Takahashi Y.; "Structure and expression of rat muscle-specific enolase gene."; FEBS Lett. 277:78-82(1990).
[4]	PROTEIN SEQUENCE OF 10-28; 33-50; 106-120; 240-253; 257-262; 336-394 AND 407-412, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord; Lubec G., Afjehi-Sadat L., Kang S.U.; Submitted (JUL-2007) to UniProtKB.
[5]	DEVELOPMENTAL STAGE. PubMed=8594891 [NCBI, ExPASy, EBI, Israel, Japan] Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.; "Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."; Am. J. Physiol. 269:H1843-H1851(1995).
[6]	EFFECT OF THYROID HORMONES ON EXPRESSION. PubMed=10662718 [NCBI, ExPASy, EBI, Israel, Japan] Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L., Rappaport L., Lamande N., Lucas M.; "Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development."; Am. J. Physiol. 278:E330-E339(2000).

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. Some colocalization with CKM at 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.
INDUCTION: Thyroid hormones up-regulate expression during hindleg muscle development and down-regulate during cardiac muscle development. Decrease in ENO3 levels with aortic stenosis.
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

Y00979; CAA68788.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC083566; AAH83566.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57774; CAA40920.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S02072; S02072.

NP_037081.2; -.

3D structure databases

HSSP

Q9NDH8; 1OEP. [HSSP ENTRY / PDB]

P15429; 2-431.

PTM databases

P15429; -.

Organism-specific databases

RGD

2555; Eno3.

Gene expression databases

ArrayExpress

P15429; -.

GermOnline

ENSRNOG00000004078; Rattus norvegicus.

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

Ensembl

ENSRNOG00000004078; Rattus norvegicus. [Contig view]

GeneID

25438; -.

KEGG

rno:25438; -.

Phylogenomic databases

HOVERGEN

P15429; -.

Other

ProtoNet

P15429.

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 (By similarity).`
`CHAIN`	`2 434`	`433`	`Beta-enolase.`	`PRO_0000134110`
`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`	`63 63`		`L -> P (in Ref. 1; CAA68788).`
`CONFLICT`	`176 182`		`SSFKEAM -> KLFQGSQ (in Ref. 1; CAA68788).`
`CONFLICT`	`279 279`		`L -> P (in Ref. 1; CAA68788).`
`CONFLICT`	`355 355`		`Q -> L (in Ref. 1; CAA68788).`
`CONFLICT`	`381 381`		`I -> V (in Ref. 1; CAA68788).`

Sequence information

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

Molecular weight: 47014 Da [This is the MW of the unprocessed precursor]

CRC64: 136A5300E052D5A7 [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 PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 

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

       250        260        270        280        290        300 
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY 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

P15429 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