Reviewed, UniProtKB/Swiss-Prot Q5R6Y1 (ENOA_PONAB)

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

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

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

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 transcript level.

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 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 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 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.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
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	Alpha-enolase		PRO_0000290000
Regions
	Region	370 – 373	4	Substrate binding By similarity
	Region	405 – 434	30	Required for interaction with PLG
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
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	5	1	N6-acetyllysine By similarity
	Modified residue	44	1	Phosphotyrosine By similarity
	Modified residue	57	1	Phosphotyrosine By similarity
	Modified residue	60	1	N6-acetyllysine By similarity
	Modified residue	63	1	Phosphoserine By similarity
	Modified residue	64	1	N6-acetyllysine By similarity
	Modified residue	71	1	N6-acetyllysine By similarity
	Modified residue	72	1	Phosphothreonine By similarity
	Modified residue	89	1	N6-acetyllysine By similarity
	Modified residue	126	1	N6-acetyllysine By similarity
	Modified residue	193	1	N6-acetyllysine By similarity
	Modified residue	199	1	N6-acetyllysine By similarity
	Modified residue	228	1	N6-acetyllysine By similarity
	Modified residue	233	1	N6-acetyllysine By similarity
	Modified residue	254	1	Phosphoserine By similarity
	Modified residue	256	1	N6-acetyllysine By similarity
	Modified residue	263	1	Phosphoserine By similarity
	Modified residue	281	1	N6-acetyllysine By similarity
	Modified residue	285	1	N6-acetyllysine By similarity
	Modified residue	287	1	Phosphotyrosine By similarity
	Modified residue	406	1	N6-acetyllysine By similarity
	Modified residue	420	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R6Y1-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: A3DE650FFF169EA5	FASTA	434	47,197
	10 20 30 40 50 60 MSILKIHARE 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 TVTNPKRIAK AVNEKSCNCL LLKVNRIGSV TESLQACKLA 370 380 390 400 410 420 QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 430 AKFAGRNFRN PLAK

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR860345 mRNA. Translation: CAH92479.1.
RefSeq	NP_001126461.1.
UniGene	Pab.18302
3D structure databases
SMR	Q5R6Y1. Positions 2-431.
ModBase	Search...
Genome annotation databases
GeneID	100173448.
Organism-specific databases
CTD	100173448.
Phylogenomic databases
HOVERGEN	Q5R6Y1.
Enzyme and pathway databases
BRENDA	4.2.1.11. 269192.
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.
ProtoNet	Search...

Entry information

Entry name

ENOA_PONAB

Accession

Primary (citable) accession number: Q5R6Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	December 21, 2004
Last modified:	October 13, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)