[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain cortex; International consortium for macaque cDNA sequencing and analysis; "DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."; Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.

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 (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. 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 (By similarity). Cell membrane (By similarity). Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By similarity). ENO1 is localized to the M-band (By similarity).
SIMILARITY: Belongs to the enolase family.

Copyright

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Cross-references

Sequence databases

EMBL

AB169531; BAE01613.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q4R5L2; 2-431.

ModBase

Q4R5L2.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
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.

Phylogenomic databases

HOVERGEN

Q4R5L2; -.

Other

ProtoNet

Q4R5L2.

UniRef

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

Keywords

Acetylation; Cell membrane; Cytoplasm; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 434`	`433`	`Alpha-enolase.`	`PRO_0000292944`
`REGION`	`370 373`	`4`	`Substrate binding (By similarity).`
`REGION`	`405 434`	`30`	`Required for interaction with PLG.`
`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).`
`MOD_RES`	`44 44`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`57 57`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`63 63`		`Phosphoserine (By similarity).`
`MOD_RES`	`71 71`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`72 72`		`Phosphothreonine (By similarity).`
`MOD_RES`	`263 263`		`Phosphoserine (By similarity).`
`MOD_RES`	`287 287`		`Phosphotyrosine (By similarity).`

Sequence information

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

Molecular weight: 47125 Da [This is the MW of the unprocessed precursor]

CRC64: 645959110D2CCB88 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSILKVHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK 

        70         80         90        100        110        120 
GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV 

       250        260        270        280        290        300 
VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WGAWQKFTAS AGIQVVGDDL TVANPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 

       430 
AKFAGRNFRN PLAK

Q4R5L2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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