The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). 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 (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (By similarity). 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). Also plays a specific role in asymmetric protein transport to the plasma membrane (PubMed:17132146). 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:17132146). May play a role in the basolateral recycling pathway (PubMed:17132146). May also play a role in phagosome maturation (PubMed:20028485). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (By similarity). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (By similarity). When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis (By similarity). GTP + H2O = GDP + H(+) + phosphate Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP) (By similarity). That Rab is activated by the DENND4C guanine exchange factor (GEF) (Probable). That Rab is activated by the DENND4C and RABIF guanine exchange factors (GEF) (By similarity). Interacts with MYO5A; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles (By similarity). Interacts with GDI1 and with GDI2; negatively regulates RAB10 association with membranes and activation (By similarity). Interacts (GDP-bound form) with LLGL1; the interaction is direct and promotes RAB10 association with membranes and activation through competition with the Rab inhibitor GDI1 (By similarity). Interacts with EXOC4; probably associates with the exocyst (PubMed:20576682). Interacts (GTP-bound form) with MICALCL, MICAL1, MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1 two molecules of RAB10 can bind to one molecule of MICAL1 (By similarity). Interacts with TBC1D13 (By similarity). Interacts with SEC16A (By similarity). Interacts with CHM and CHML (By similarity). Interacts with LRRK2; interaction facilitates phosphorylation of Thr-73 (By similarity). Interacts with RILPL1 and RILPL2 when phosphorylated on Thr-73 (By similarity). Associates with SLC2A4/GLUT4 storage vesicles (By similarity). Localizes to the base of the cilium (PubMed:20576682). Transiently associates with phagosomes (PubMed:20028485). Phosphorylation of Thr-73 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2. Belongs to the small GTPase superfamily. Rab family.