Unconventional myosin-XVIIIa (MYO18A)
The protein contains 2054 amino acids for an estimated molecular weight of 233115 Da.
May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). (updated: Nov. 22, 2017)
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.
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:rs8076604 |
Biological Process
Actomyosin structure organization
Asymmetric Golgi ribbon formation
Cell migration
DNA metabolic process
Golgi organization
Golgi ribbon formation
Golgi vesicle budding
Microtubule-based movement
Negative regulation of apoptotic process
Positive regulation of opsonization
Positive regulation of protein secretion
Regulation of macrophage activation
The reference OMIM entry for this protein is 609517
Tgfb1-induced antiapoptotic factor 1; tiaf1
Myosin containing pdz domain; myspdz
Molecule associated with jak3 n terminus; majn
Kiaa0216
CLONING
By sequencing clones obtained from a size-fractionated immature myeloid cell line cDNA library, Nagase et al. (1996) cloned TIAF1, which they designated KIAA0216. The deduced 1,581-amino acid protein shares significant similarity with rat myosin heavy chain, and it contains an ATP/GTP-binding site motif A. Northern blot analysis detected TIAF1 in all tissues and cell lines examined, with highest expression in skeletal muscle. Using differential display to identify genes whose expression correlated with the ability of mouse stromal cells to support hematopoiesis, Furusawa et al. (2000) cloned Tiaf1, which they designated Myspdz. The deduced 2,035-amino acid protein shares 94% homology with KIAA0216, but it contains an additional 458 N-terminal amino acids. By database analysis, Furusawa et al. (2000) identified a human genomic clone containing an exon with significant similarity to nucleotides 1 to 946 of the mouse Tiaf1 gene, suggesting that human TIAF1 may also encode a longer protein. Mouse Tiaf1 contains an N-terminal KE-rich region, followed by a PDZ domain, a head region with an ATP-binding site, a neck region with an IQ motif, and a coiled-coil C-terminal domain. Northern blot analysis detected Tiaf1 in all tissues examined. A 10.5-kb transcript was detected in heart and skeletal muscle, and a 7.0-kb transcript was detected in hematopoietic tissues and cells. Western blot analysis detected Tiaf1 at an apparent molecular mass of 230 kD. Immunostaining localized Tiaf1 in a filamentous network slightly concentrated in the perinuclear region of mouse stromal cells.GENE FUNCTION
Ji et al. (2000) found that the C-terminal myosin tail motif of TIAF1 interacts with the N terminus of JAK3 (600173). Schultz et al. (2004) showed that TIAF1 and p53 (TP53; 191170) induced apoptosis in human U937 myocytoma cells in both synergistic and antagonistic manners. At optimal levels, both TIAF1 and p53 mediated apoptosis cooperatively. Both proteins also suppressed adherence-independent growth in a mouse fibroblast cell line. In contrast, initiation of apoptosis by overexpressed TIAF1 was blocked by low doses of p53, and vice versa. Ectopic p53 blocked apoptosis in U937 cells stably expressing TIAF1. TIAF1 and p53 did not appear to physically interact; however, nuclear translocation of phosphorylated p53 was significantly reduced in TIAF1-silenced cells. Schultz et al. (2004) concluded that TIAF1 likely participates in the nuclear translocation of activated p53.GENE STRUCTURE
The TIAF1 gene resides within the 3-prime untranslated region of the MYO18A gene (610067) (Scott, 2006).MAPPING
By radiation and somatic cell hybrid analyses, Nagase et al. (1996) mapped the TIAF1 gene to chromosome 17. ... More on the omim web site
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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609517 was added.