Regulator of microtubule dynamics protein 3 (RMDN3)
The protein contains 470 amino acids for an estimated molecular weight of 52118 Da.
Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs11558807 |
The reference OMIM entry for this protein is 611873
Family with sequence similarity 82, member a2; fam82a2
Regulator of microtubule dynamics 3; rmd3
Protein tyrosine phosphatase-interacting protein 51: ptpip51 family with sequence similarity 82, member c, formerly; fam82c, formerly
CLONING
Stenzinger et al. (2005) obtained a partial cDNA encoding FAM82C, which they called PTPIP51, in a yeast 2-hybrid screen of a Jurkat human T-cell library using protein-tyrosine phosphatase-1B (PTPN1; 176885) and T-cell protein tyrosine phosphatase (PTPN2; 176887) as bait. They identified the full-length cDNA by database analysis. The deduced full-length protein contains 470 amino acid and has a calculated molecular mass of 52.1 kD. PTPIP51 has a putative N-terminal signal peptide, a potential DNA photolyase motif, a zinc finger motif, and N- and C-terminal tetratricopeptide repeats. Northern blot analysis of Jurkat cells detected a 3-kb PTPIP511 transcript, and Western blot analysis revealed a 52-kD protein. In situ hybridization, Western blot analysis, immunohistochemistry, and immunogold electron microscopy of human and rodent tissues showed high levels of PTPIP51 in epidermis and seminiferous epithelium, predominantly in keratinocytes and differentiating first-order spermatocytes up to spermatids. In skeletal muscle, expression of PTPIP51 was restricted to fast-twitch fibers, with predominant localization at A-bands. In surface epithelia containing ciliated cells, PTPIP51 mRNA and protein localized in a small rim beneath the adluminal cell membrane and on ciliated membrane surfaces, and electron microscopy showed PTPIP51 next to microtubules and the basal body. PTPIP51 was also expressed in hippocampal neurons, ganglion cells of the autonomic nervous system, and axons of the peripheral nervous system. By PCR, Lv et al. (2006) cloned PTPIP51 from a kidney cDNA library. They identified a transmembrane domain and mitochondrial targeting sequence near the N terminus of PTPIP51. Northern blot analysis detected a 2.4-kb transcript in all tissues examined, with minor transcripts of 4 and 8 kb in cerebellum. RT-PCR detected PTPIP51 expression in all tumor tissues and human cell lines examined. Fluorescence-tagged PTPIP51 colocalized with a mitochondria marker in transfected human HEK293T cells. By database searching, Oishi et al. (2007) identified 3 human proteins related to a family of microtubule-associated proteins in C. elegans: RMD1 (FAM82B; 611871), RMD2 (FAM82A; 611872), and RMD3. The deduced proteins in both species contain multiple coiled-coil domains and localize to spindle microtubules and spindle poles during cell division. Using protease digestion and differential solubilization, De Vos et al. (2012) showed that endogenous human PTIP51 is an outer mitochondrial membrane protein with a C-terminal domain that projects into the cytosol.GENE FUNCTION
Lv et al. (2006) showed that overexpression of PTPIP51 in HEK293T and HeLa cells resulted in apoptosis characterized by externalization of phosphatidylserine, activation of caspase-3 (CASP3; 600636), cleavage of PARP (173870), and condensation of nuclear DNA. Furthermore, PTPIP51 overexpression caused a decrease in mitochondrial membrane potential and release of cytochrome c (123970), suggesting that PTPIP51 may be involved in a mitochondria/cytochrome c-mediated apoptosis pathway. Using cosedimentation assays, Oishi et al. (2007) showed that human RMD1, RMD2, and RMD3 proteins interact with microtubules. Using yeast 2-hybrid and coimmunoprecipitation analyses, De Vos et al. (2012) found that endogenous human PTPIP51 interacted with the endoplasmic reticulum (ER) membrane protein VAPB (605704). The cytoplasmic C-terminal domain of PTPIP51 interacted with th ... More on the omim web site
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 611873 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).