Alpha-enolase (ENO1)

The protein contains 434 amino acids for an estimated molecular weight of 47169 Da.

 

Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:29775581, PubMed:1369209). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:2005901, PubMed:10802057, PubMed:12666133, PubMed:29775581). 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 (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209).', 'MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. (updated: Nov. 13, 2019)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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VariantDescription
dbSNP:rs11544513
dbSNP:rs11544514

The reference OMIM entry for this protein is 172430

Enolase 1; eno1
Enolase, alpha
Phosphopyruvate hydratase; pph crystallin, tau, included
Enolase, nonneuronal, included; nne, included

DESCRIPTION

Enolase is a glycolytic enzyme (2-phospho-D-glycerate hydrolyase; EC 4.2.1.11). Each of the 3 ENO isoenzymes is a homodimer composed of 2 alpha (ENO1), 2 gamma (ENO2; 131360), or 2 beta (ENO3; 131370) subunits. Isoenzyme alpha (ENO1) is present in most tissues, whereas the beta form (ENO3) is localized to muscle and the gamma form (ENO2) is found only in nervous tissue (summary by Giallongo et al., 1986).

CLONING

Giallongo et al. (1986) cloned and sequenced a full-length cDNA for human alpha-enolase. Its coding region was found to be 1,299 bases long. The 433-amino acid protein shows 67% homology to yeast enolase and 94% homology to rat nonneural enolase. Wistow et al. (1988) presented evidence for the remarkable conclusion that alpha-enolase is encoded by the same gene that encodes tau-crystallin, a lens structural protein.

GENE STRUCTURE

Giallongo et al. (1990) determined that the ENO1 gene contains 12 exons.

MAPPING

Giblett et al. (1974) observed an electrophoretic variant of red cell PPH among Cree Indians. Linkage was found with the Rhesus locus. Since the Rh locus has been assigned to chromosome 1 and since cell hybridization studies assign the PPH locus to chromosome 1, the new data are consistent. The Goss-Harris method of mapping combines features of recombinational study in families and synteny tests in hybrid cells. As applied to chromosome 1, the method shows that AK2 and UMPK are distal to PGM1 and that the order of the loci is PGM1: UMPK: (AK2, alpha-FUC): ENO1 (Goss and Harris, 1977). Comings (1972) and Ohno (1973) suggested that during vertebrate evolution tetraploidization occurred 2-3 hundred million years ago and that chromosomal events that tend to preserve ancestral linkage groups, such as Robertsonian fusions, inversions and gene duplications, have been favored. Demonstration of linkage of homologous genes supports this hypothesis. D'Ancona et al. (1977) regionalized ENO1 to 1pter-p36.13. Lalley et al. (1978) demonstrated synteny of enolase, PGD (172200), PGM1 (171900), and AK2 (103020) on chromosome 4 of the mouse; they are on 1p of man. - Pseudogene Feo et al. (1990) concluded that there is a single alpha-enolase pseudogene in the human genome. This intronless, processed pseudogene was mapped to chromosome 1 by Southern blot analysis of rodent-human hybrid cell DNAs; thus, it is on the same chromosome as the functional gene. Ribaudo et al. (1996) confirmed the assignment of ENO1P to chromosome 1. By fluorescence in situ hybridization, they found that it is located on 1q41-q42, whereas the functional gene is located on the short arm of that chromosome.

GENE FUNCTION

Lachant et al. (1986) and Lachant and Tanaka (1987) reported 4 generations of a Caucasian family with hereditary red cell enolase deficiency. Partial deficiency in this kindred behaved as an autosomal dominant and was associated with a spherocytic phenotype, although a normal acidified glycerol lysis test suggested that the spherocytes of enolase deficiency are different from those of hereditary spherocytosis (see 182900). Clinical expression of enolase deficiency varied in this family. Some had slightly low hematocrit with elevated reticulocytes, while others had no evidence of anemia or hemolysis. To identify the autoantigens related to Hashimoto encephalopathy, a rare autoimmune disease associated with Hashimoto thyroiditis (140300), Ochi et al. (2002) developed a human brain proteom ... More on the omim web site

Subscribe to this protein entry history

Dec. 2, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 172430 was added.

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed