Neutral alpha-glucosidase AB (GANAB)
The protein contains 944 amino acids for an estimated molecular weight of 106874 Da.
Catalytic subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:10929008). Required for PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia (PubMed:27259053). (updated: June 20, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- 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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
This protein is predicted to be membranous by TOPCONS.
(right-click above to access to more options from the contextual menu)
Biological Process
Carbohydrate metabolic process
Cellular protein metabolic process
N-glycan processing
Post-translational protein modification
Protein folding
Protein N-linked glycosylation via asparagine
Viral protein processing
The reference OMIM entry for this protein is 104160
Glucosidase, alpha, neutral ab; ganab
Alpha-glucosidase, neutral, ab form
Glucosidase ii, alpha subunit
CLONING
Human tissues contain 2 isozymes of neutral alpha-glucosidase designated AB (GANAB) and C (GANC; 104180). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, the two have been shown to have other differences including those of substrate specificity. Since the AB form of mouse is not different electrophoretically from that in man, Martiniuk et al. (1982, 1983) used rocket immunoelectrophoresis to distinguish the enzymes from the 2 species. Trombetta et al. (1996) isolated enzymatically active glucosidase II from rat liver and found that it was composed of 2 subunits, alpha and beta (177060). Based on peptide sequences of the purified enzyme, they identified the corresponding human cDNAs in existing sequence databases. Trombetta et al. (1996) reported that the available sequence of the alpha subunit of human glucosidase II predicts a 912-amino acid polypeptide with homology to the catalytic domains of several other glucosidases, but without significant homology to human glucosidase I. They found that the alpha subunit of human glucosidase II is a functional homolog of a gene found on S. cerevisiae chromosome II.MAPPING
Martiniuk et al. (1982, 1983) assigned the GANAB gene to 11q13-qter by study of mouse-man hybrid cells. ... More on the omim web site
July 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: 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 104160 was added.