[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skeletal muscle; Wu J., Deng C.Y., Xiong Y.Z.; "Molecular characterization and expression pattern of the porcine enolase 3 (beta, muscle) (ENO3) gene."; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Wu J., Deng C.Y., Xiong Y.Z.; "Molecular characterization, expression pattern and polymorphism of the porcine ENO3 gene."; Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Appears to have a function in striated muscle development and regeneration (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. Interacts with PNKD (By similarity).
SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity).
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

DQ355513; ABC75829.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ676935; ABG73136.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001037992.1; -.

UniGene

Ssc.10942

3D structure databases

SMR

Q1KYT0; 2-431.

ModBase

Q1KYT0.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
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

692156; -.

KEGG

ssc:692156; -.

Phylogenomic databases

HOVERGEN

Q1KYT0; -.

Other

UniRef

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

Keywords

Cytoplasm; 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_0000273972`
`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).`

Sequence information

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

Molecular weight: 47130 Da [This is the MW of the unprocessed precursor]

CRC64: 30C4D01FE35B4210 [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 LPVGASSFRE 

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

       250        260        270        280        290        300 
VIGMDVAASE FYRNGKYDLD FKSPDDPSRH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WKTWTSFLSG VNIQIVGDDL TVTNLKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 

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

       430 
AVFAGRKFRN PKAK

Q1KYT0 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