Alpha-enolase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P04764 (ENOA_RAT)

Last modified November 3, 2009. Version 106. 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

Gene names

Name:	Eno1
Synonyms:	Eno-1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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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. Stimulates immunoglobulin production.
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. 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	Cytoplasm. Cell membrane. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. Ref.1 Ref.9
Tissue specificity	Expressed in flagella of epididymal sperm. 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. Ref.10
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. In brain, levels of ENO1 decrease around 10 dpc and then gradually increase to adult age. In embryonic heart, ENO1 levels decrease rapidly during cardiac development. Ref.1 Ref.7
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)
Biological process	glycolysis Traceable author statement. Source: RGD
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.9 Inferred from direct assay. Source: RGD synaptosome Ref.9 Inferred from direct assay. Source: RGD
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.9 Inferred from direct assay. Source: RGD protein heterodimerization activity Ref.9 Inferred from direct assay. Source: RGD protein homodimerization activity Ref.9 Inferred from direct assay. Source: RGD serine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
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 By similarity

Chain

2 – 434

433

Alpha-enolase

PRO_0000134099

Regions

Region

370 – 373

Substrate binding By similarity

Region

405 – 434

Required for interaction with PLG

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

N-acetylserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

126

N6-acetyllysine By similarity

Modified residue

193

N6-acetyllysine By similarity

Modified residue

199

N6-acetyllysine By similarity

Modified residue

228

N6-acetyllysine By similarity

Modified residue

233

N6-acetyllysine By similarity

Modified residue

256

N6-acetyllysine By similarity

Modified residue

263

Phosphoserine By similarity

Modified residue

281

N6-acetyllysine By similarity

Modified residue

285

N6-acetyllysine By similarity

Modified residue

287

Phosphotyrosine By similarity

Modified residue

406

N6-acetyllysine By similarity

Modified residue

420

N6-acetyllysine By similarity

Experimental info

Sequence conflict

E → Q AA sequence Ref.5

Sequence conflict

93 – 96

LMIE → DQIK in AAK01319. Ref.6

Sequence conflict

125

E → G in CAA26456. Ref.1

Sequence conflict

144

I → T in CAA26456. Ref.1

Sequence conflict

151

N → D in AAK01319. Ref.6

Sequence conflict

250

E → Q AA sequence Ref.5

Sequence conflict

374

G → E in CAA26456. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P04764-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 736660B2D5E936DC
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FASTA

434

47,128

        10         20         30         40         50         60 
MSILKIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK 

        70         80         90        100        110        120 
GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DQLMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAVEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKSA IAKAGYTDQV 

       250        260        270        280        290        300 
VIGMDVAASE FYRAGKYDLD FKSPDDASRY ITPDQLADLY KSFIKDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WDAWQKFTAT AGIQVVGDDL TVTNPKRIAK AAGEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK 

       430 
AKFAGRSFRN PLAK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and the nucleotide sequence of cDNA to mRNA for non-neuronal enolase (alpha alpha enolase) of rat brain and liver." Sakimura K., Kushiya E., Obinata M., Takahashi Y. Nucleic Acids Res. 13:4365-4378(1985) [PubMed: 2989793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Tissue: Brain and Liver.
[2]	Takahashi Y. Submitted (JAN-1986) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"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]. Tissue: Heart, Pituitary and Testis.
[4]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 10-28; 33-50; 72-103; 106-120; 163-179; 184-193; 203-228; 234-262; 270-281; 307-326; 336-394 AND 407-420, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[5]	"Plasminogen binds specifically to alpha-enolase on rat neuronal plasma membrane." Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K., Kohsaka S. J. Neurochem. 63:2048-2057(1994) [PubMed: 7964722] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-57; 97-109; 245-262 AND 369-382, INTERACTION WITH PLG. Tissue: Embryonic brain.
[6]	"Rat cDNA encoding alpha enolase (2-phospho-D-glycerate hydro-lyase) (non-neural enolase) (NNE)." Bole-Feysot C., Kelly P.A. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-153. Tissue: Lymphoma.
[7]	"Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy." Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M. Am. J. Physiol. 269:H1843-H1851(1995) [PubMed: 8594891] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[8]	"Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development." Merkulova T., Keller A., Oliviero P., Marotte F., Samuel J.L., Rappaport L., Lamande N., Lucas M. Am. J. Physiol. 278:E330-E339(2000) [PubMed: 10662718] [Abstract] Cited for: INDUCTION.
[9]	"Localization of enolase in synaptic plasma membrane as an alphagamma heterodimer in rat brain." Ueta H., Nagasawa H., Oyabu-Manabe Y., Toida K., Ishimura K., Hori H. Neurosci. Res. 48:379-386(2004) [PubMed: 15041191] [Abstract] Cited for: SUBCELLULAR LOCATION OF ALPHA/GAMMA HETERODIMER.
[10]	"Identification of novel immunodominant epididymal sperm proteins using combinatorial approach." Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V. Reproduction 138:81-93(2009) [PubMed: 19423663] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X02610 mRNA. Translation: CAA26456.1. BC063174 mRNA. Translation: AAH63174.1. Different initiation. BC078896 mRNA. Translation: AAH78896.1. BC081847 mRNA. Translation: AAH81847.2. AF241613 mRNA. Translation: AAK01319.1.
IPI	IPI00464815.
PIR	A23126.
RefSeq	NP_001103378.1. NP_036686.2.
UniGene	Rn.4236
3D structure databases
HSSP	HSSP built from PDB template 1PDZ based on UniProtKB P56252.
SMR	P04764. Positions 2-431.
ModBase	Search...
Protein-protein interaction databases
STRING	P04764.
PTM databases
PhosphoSite	P04764.
Proteomic databases
PRIDE	P04764.
Genome annotation databases
Ensembl	ENSRNOT00000024106; ENSRNOP00000024106; ENSRNOG00000017895; Rattus norvegicus. [Genome view]
GeneID	24333.
KEGG	rno:24333.
UCSC	NM_012554. rat.
Organism-specific databases
CTD	24333.
RGD	2553. Eno1.
Phylogenomic databases
HOVERGEN	P04764.
OMA	SDSSKWL.
Enzyme and pathway databases
BRENDA	4.2.1.11. 248.
Gene expression databases
ArrayExpress	P04764.
Genevestigator	P04764.
GermOnline	ENSRNOG00000017895. Rattus norvegicus.
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	603015.

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Entry information

Entry name

ENOA_RAT

Accession

Primary (citable) accession number: P04764
Secondary accession number(s): Q66HI3, Q6AYV3, Q6P504

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 106 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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents