Ras-related protein Rab-10 (RAB10)
The protein contains 200 amino acids for an estimated molecular weight of 22541 Da.
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21248164). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:21248164). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (PubMed:21248164). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Plays also a specific role in asymmetric protein transport to the plasma membrane (PubMed:16641372). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (By similarity). In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (PubMed:16641372). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (PubMed:23263280). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis ( (updated: July 31, 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.
- 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 annotated as membranous in Gene Ontology.
(right-click above to access to more options from the contextual menu)
Biological Process
Antigen processing and presentation
Axonogenesis
Basolateral protein localization
Cellular response to insulin stimulus
Endoplasmic reticulum tubular network organization
Endosomal transport
Establishment of neuroblast polarity
Establishment of protein localization to endoplasmic reticulum membrane
Establishment of protein localization to membrane
Golgi to plasma membrane protein transport
Golgi to plasma membrane transport
Intracellular protein transport
Membrane organization
Metabolic process
Neutrophil degranulation
Polarized epithelial cell differentiation
Protein localization to basolateral plasma membrane
Protein localization to plasma membrane
Protein secretion
Rab protein signal transduction
Regulated exocytosis
Regulation of exocytosis
Vesicle docking involved in exocytosis
Vesicle-mediated transport
Cellular Component
Adherens junction
Cell-cell adherens junction
Cilium
Cytoplasmic vesicle membrane
Cytoskeleton
Cytosol
Endomembrane system
Endoplasmic reticulum membrane
Endoplasmic reticulum tubular network
Endosome
Endosome membrane
Exocytic vesicle
Extracellular exosome
Focal adhesion
Golgi apparatus
Golgi membrane
Insulin-responsive compartment
Perinuclear region of cytoplasm
Phagocytic vesicle membrane
Plasma membrane
Primary cilium
Recycling endosome
Recycling endosome membrane
Secretory granule membrane
Synaptic vesicle
Trans-Golgi network
The reference OMIM entry for this protein is 612672
Ras-associated protein rab10; rab10
DESCRIPTION
RAB10 belongs to the RAS (see HRAS; 190020) superfamily of small GTPases. RAB proteins localize to exocytic and endocytic compartments and regulate intracellular vesicle trafficking (Bao et al., 1998).CLONING
Using degenerate oligonucleotide primers to amplify RAB family members from human skeletal muscle total RNA, Bao et al. (1998) obtained a partial RAB10 clone. The deduced 49-amino acid sequence includes the first 2 GTP-binding regions and effector domain residues that are conserved in RAB proteins. Bao et al. (1998) stated that RAB10 protein localizes to the distal Golgi complex. By searching databases for RAS family members, followed by PCR, He et al. (2002) cloned RAB10. The deduced 200-amino acid RAB10 protein contains 4 highly conserved GTPase motifs and a C-terminal geranylgeranylation motif. Northern blot analysis detected a major transcript of about 4 kb and a smaller minor transcript. Highest expression was detected in heart and skeletal muscle, followed by brain, placenta, lung, liver, kidney, pancreas, testis, and spleen. Low expression was detected in ovary, prostate, and colon, and little to no expression was detected in thymus, small intestine, and leukocytes.GENE FUNCTION
In muscle and fat cells, insulin (INS; 176730) stimulation activates a signaling cascade that causes intracellular vesicles containing glucose transporter-4 (GLUT4, or SLC2A4; 138190) to translocate to and fuse with the plasma membrane. Using mass spectrometry, Larance et al. (2005) identified Rab10, Rab11 (see RAB11A; 605570), and Rab14 (612673) on Glut4 vesicles from cultured mouse adipocytes. These vesicles also contained the RAB GTPase-activating protein (GAP) As160 (TBC1D4; 612465), suggesting that the RAB proteins may be AS160 substrates. Miinea et al. (2005) found that the purified recombinant GAP domain of human AS160 showed GAP activity with RAB2A (RAB2; 179509), RAB8A (165040), RAB10, and RAB14, but not with 14 other RABs. Immunoblot analysis showed that these RABs associated with Glut4-positive vesicles in mouse adipocytes. Miinea et al. (2005) concluded that AK160 functions as a RAB GAP and that RABs may participate in GLUT4 translocation.GENE STRUCTURE
He et al. (2002) determined that the RAB10 gene contains 5 exons and spans over 36.7 kb.MAPPING
By radiation hybrid analysis, He et al. (2002) mapped the RAB10 gene to chromosome 2p23.1-p22.3. Hartz (2009) mapped the RAB10 gene to chromosome 2p23.3 based on an alignment of the RAB10 sequence (GENBANK GenBank AF106681) with the genomic sequence (build 36.1). ... More on the omim web site
Aug. 20, 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612672 was added.