Solute carrier family 2, facilitated glucose transporter member 14 (SLC2A14)
The protein contains 520 amino acids for an estimated molecular weight of 56320 Da.
Hexose transporter that can mediate the transport of glucose and dehydroascorbate across the cell membrane. (updated: July 3, 2019)
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.
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 annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs10845981 |
The reference OMIM entry for this protein is 611039
Solute carrier family 2 (facilitated glucose transporter), member 14; slc2a14
Glucose transporter 14; glut14
DESCRIPTION
Members of the glucose transporter (GLUT) family, including SLC2A14, are highly conserved integral membrane proteins that transport hexoses such as glucose and fructose into all mammalian cells. GLUTs show tissue and cell-type specific expression (Wu and Freeze, 2002).CLONING
By database analysis, followed by PCR of a human testis cDNA library, Wu and Freeze (2002) cloned SLC2A14. They identified 2 alternatively spliced forms. The short isoform has 10 exons and encodes a 497-amino acid protein that shares 94.5% identity with SLC2A3 (138170). The long isoform has 11 exons and encodes a 520-amino acid protein that differs from the short isoform by inclusion of exon 1b. SLC2A14 contains 12 transmembrane domains, a putative glycosylation site, and sugar transporter signature motifs. RT-PCR analysis showed that both isoforms were expressed in testis only.GENE STRUCTURE
Wu and Freeze (2002) determined that the SLC2A14 gene contains 11 exons. Exon 1b of the long isoform disrupts the reading frame, but a secondary ATG codon within exon 1b allows synthesis of a functional protein.MAPPING
By genomic sequence analysis, Wu and Freeze (2002) mapped the SLC2A14 gene to chromosome 12p13.3, about 10 Mb upstream of SLC2A3.EVOLUTION
Wu and Freeze (2002) performed sequence comparison of SLC2A14 and SLC2A3 and concluded that SLC2A14 likely resulted from gene duplication of SLC2A3. ... More on the omim web site
July 4, 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
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for SLC2A14
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 611039 was added.