SEC14-like protein 4 (SEC14L4)
The protein contains 406 amino acids for an estimated molecular weight of 46644 Da.
Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids. (updated: March 4, 2015)
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.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs9608956 | |
| dbSNP:rs9606739 | |
| dbSNP:rs17738540 | |
| dbSNP:rs17738527 |
No binding partner found
Biological Process
The reference OMIM entry for this protein is 612825
Sec14-like 4; sec14l4
Sec14, s. cerevisiae, homolog of, 4
Tocopherol-associated protein 3; tap3
CLONING
By database analysis of the region surrounding human SEC14L2 (607558), followed by RT-PCR analysis of human lung total RNA, Kempna et al. (2003) cloned SEC14L3 (612824) and SEC14L4, which they called TAP2 and TAP3, respectively. The 406-amino acid SEC14L4 protein has a conserved CRAL/TRIO domain and shares 80% similarity with SEC14L2. All 3 proteins share residues glu185 and lys216, which are predicted to play a role in phospholipid binding and transfer activity in S. cerevisiae Sec14. RT-PCR of human tissues and cell lines detected high SEC14L4 expression in all tissues examined. Immunocytochemical studies localized SEC14L4 to intracellular membranes of the cytoplasm in HeLa cells, including partial localization to the ER and Golgi, with more intense staining surrounding but not within the nucleus.GENE FUNCTION
Kempna et al. (2003) showed that in HeLa cells deletion of the C-terminal Golgi dynamics (GOLD) domain changed SEC14L4 localization with decreased staining surrounding the nucleus and a more dispersed staining throughout the cell. They suggested that the SEC14L4 GOLD domain may play a role in docking to other proteins or in intracellular transport of bound ligands. Using several assays, Kempna et al. (2003) demonstrated that SEC14L3 bound tocopherol, squalene, and phospholipids (phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol). Although SEC14L4 bound phospholipids, it failed to complement an S. cerevisiae temperature-sensitive Sec14 allele in yeast. Using immunoprecipitation assays, Kempna et al. (2003) showed that SEC14L4 may interact with and regulate phosphatidylinositol 3-kinase activity and that SEC14L4 displayed low basal GTPase activity.GENE STRUCTURE
Kempna et al. (2003) determined that the SEC14L4 gene contains 12 exons.MAPPING
By database analysis, Kempna et al. (2003) mapped the SEC14L4 gene to chromosome 22q12.1-qter, where it lies within 100 kb of the SEC14L2 and SEC14L3 genes. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for SEC14L4
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612825 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed