Fructose-bisphosphate aldolase C (ALDOC)

The protein contains 364 amino acids for an estimated molecular weight of 39456 Da.

 

No function (updated: March 4, 2015)

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. 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.
  3. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. 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.

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

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The reference OMIM entry for this protein is 103870

Aldolase c, fructose-bisphosphate; aldoc
Aldolase 3
Fructoaldolase c; aldc

CLONING

Rottmann et al. (1987) determined the complete amino acid sequence of aldolase C from recombinant genomic clones. The deduced polypeptide contains 363 amino acids. Aldolase C shares 81% amino acid identity with aldolase A (ALDOA; 103850) and 70% identity with aldolase B (ALDOB; 612724). For additional background information, see 103850.

GENE STRUCTURE

Rottmann et al. (1987) determined that the gene structure of ALDOC is the same as that in other aldolase genes in birds and mammals, having 9 exons separated by 8 introns, all in precisely the same positions, with only the intron sizes being different. One of the exons is noncoding. The entire gene is approximately 4 kb long. Buono et al. (1988) presented the complete nucleotide sequence of ALDOC.

MAPPING

Tolan et al. (1987) reported the mapping of ALDOC to chromosome 17 by spot-blot analysis of sorted chromosomes. Rocchi et al. (1989) also mapped the gene and narrowed the assignment to 17cen-q21 by in situ hybridization. In addition, they corroborated the assignment of ALDOA to chromosome 16, and of ALDOB to chromosome 9. ... More on the omim web site

Subscribe to this protein entry history

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 103870 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

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