Reviewed, UniProtKB/Swiss-Prot P13929 (ENOB_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Muscle-specific enolase
      Short name=MSE
    Skeletal muscle enolase
    Enolase 3

Gene names

Name:

ENO3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.

General annotation (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 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. Interacts with PNKD. Ref.6
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, and to the alpha/gamma heterodimer in nerve cells.
Involvement in disease	Defects in ENO3 are the cause of muscle-specific enolase-beta deficiency (glycogenesis type XIII) [MIM:131370]. It is a glycogen storage myopathy which results in exercise-induced myalgias, generalized muscle weakness and fatigability. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected in patients.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.4 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 434	433	Beta-enolase		PRO_0000134107
Regions
	Region	370 – 373	4	Substrate binding By similarity
Sites
	Active site	210	1	Proton donor By similarity
	Active site	343	1	Proton acceptor By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	293	1	Magnesium By similarity
	Metal binding	318	1	Magnesium By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	318	1	Substrate By similarity
	Binding site	394	1	Substrate By similarity
Natural variations
	Natural variant	71	1	N → S: dbSNP rs238238. Ref.5		VAR_020618
	Natural variant	85	1	V → A: dbSNP rs238239. Ref.5 Ref.2		VAR_020619
	Natural variant	156	1	G → D in muscle-specific beta-enolase deficiency; when associated with E-374. Ref.8		VAR_020620
	Natural variant	374	1	G → E in muscle-specific beta-enolase deficiency; when associated with D-156. Ref.8		VAR_020621

Sequences

	Sequence		Length	Mass (Da)
	P13929-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4D9D8DCF32CF153F	FASTA	434	46,987
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 70 80 90 100 110 120 GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 130 140 150 160 170 180 AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 190 200 210 220 230 240 AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 250 260 270 280 290 300 VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD 310 320 330 340 350 360 WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 370 380 390 400 410 420 QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 430 AIFAGRKFRN PKAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone." Peshavaria M., Hinks L.J., Day I.N.M. Nucleic Acids Res. 17:8862-8862(1989) [PubMed: 2587223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)." Cali L., Feo S., Oliva D., Giallongo A. Nucleic Acids Res. 18:1893-1893(1990) [PubMed: 2336366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-85.
[3]	"Molecular structure of the human muscle-specific enolase gene (ENO3)." Peshavaria M., Day I.N.M. Biochem. J. 275:427-433(1991) [PubMed: 1840492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA." Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S. Eur. J. Biochem. 214:367-374(1993) [PubMed: 8513787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-71 AND ALA-85. Tissue: Muscle.
[6]	"Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle." Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., Gong L.-M. Acta Biochim. Biophys. Sin. 36:412-418(2004) [PubMed: 15188056] [Abstract] Cited for: INTERACTION WITH PNKD.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis." Comi G.P., Fortunato F., Lucchiari S., Bordoni A., Prelle A., Jann S., Keller A., Ciscato P., Galbiati S., Chiveri L., Torrente Y., Scarlato G., Bresolin N. Ann. Neurol. 50:202-207(2001) [PubMed: 11506403] [Abstract] Cited for: VARIANTS MUSCLE-SPECIFIC BETA-ENOLASE DEFICIENCY ASP-156 AND GLU-374.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X16504 mRNA. Translation: CAA34513.1. X51957 mRNA. Translation: CAA36216.1. X55976 Genomic DNA. Translation: CAA39446.1. X56832 Genomic DNA. Translation: CAA40163.1. BC017249 mRNA. Translation: AAH17249.1.
IPI	IPI00218474.
PIR	S06756.
RefSeq	NP_001967.2. NP_443739.2.
UniGene	Hs.224171
3D structure databases
HSSP	HSSP built from PDB template 1PDZ based on UniProtKB P56252.
SMR	P13929. Positions 2-431.
ModBase	Search...
PTM databases
PhosphoSite	P13929.
Proteomic databases
PRIDE	P13929.
Genome annotation databases
Ensembl	ENSG00000108515. Homo sapiens. [Contig view]
GeneID	2027.
KEGG	hsa:2027.
Organism-specific databases
GeneCards	GC17P004795.
HGNC	HGNC:3354. ENO3.
HPA	HPA000793.
MIM	131370. gene+phenotype.
Orphanet	299. Enolase deficiency.
PharmGKB	PA27789.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P13929.
HOVERGEN	P13929.
Enzyme and pathway databases
BRENDA	4.2.1.11. 247.
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P13929.
Bgee	P13929.
CleanEx	HS_ENO3.
GermOnline	ENSG00000108515. Homo sapiens.
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]
ProtoNet	Search...
Other Resources
NextBio	8207.
SOURCE	Search...

Entry information

Entry name

ENOB_HUMAN

Accession

Primary (citable) accession number: P13929
Secondary accession number(s): Q96AE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)