P62494P24410Q9JLX1RB11A_RATRas-related protein Rab-11ARab-113.6.5.224KGRab11aRab11Rattus norvegicusRatEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattusMolecular cloning and characterization of a ras p21-like GTP-binding protein (24KG) from rat liver.NUCLEOTIDE SEQUENCE [MRNA]TISSUE SPECIFICITYThe status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes.FUNCTIONINTERACTION WITH RAB11FIP5Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly.INTERACTION WITH STXBP6Protrudin induces neurite formation by directional membrane trafficking.INTERACTION WITH ZFYVE27The 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). The small Rab GTPase RAB11A regulates endocytic recycling (PubMed:11163216). Forms a functional Rab11/FIP3/dynein complex that regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endosomal recycling compartment (ERC) (By similarity). Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes (By similarity). May also play a role in melanosome transport and release from melanocytes (By similarity). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation. On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (By similarity). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-endososomal dependent export route via interaction with WDR44 (By similarity).GTP + H2O = GDP + H(+) + phosphateInteracts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4 (By similarity). Forms a complex with RAB11FIP3 and dynein intermediate chain DYNC1LI1; the interaction between RAB11A1 and RAB11FIP3 is direct; the complex regulates endocytic trafficking (By similarity). Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A (By similarity). Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39 (By similarity). Interacts with EXOC6 in a GTP-dependent manner. Interacts with RAB11FIP5 (PubMed:11163216). Interacts with STXBP6 (PubMed:12145319). Interacts (GDP-bound form) with ZFYVE27 (PubMed:17082457). Interacts with BIRC6/bruce (By similarity). May interact with TBC1D14 (By similarity). Interacts with UNC119; in a cell cycle-dependent manner (By similarity). GDP-bound and nucleotide-free forms interact with SH3BP5 (By similarity). Interacts (GDP-bound form) with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts (GDP-bound form) with RELCH (By similarity). Found in a complex composed of RELCH, OSBP1 and RAB11A (By similarity). Interacts with TBC1D12 (By similarity). Interacts with DEF6 (By similarity). Interacts with ATP9A (By similarity). Forms a heterotetramer with RAB11FIP3; the GTP-bound form is preferred for binding. Forms a complex with Rabin8/RAB3IP and RAB11FIP3, probably a heterohexamer with two of each protein subunit, where Rabin8/RAB3IP and RAB11FIP3 simultaneously bind to RAB11A; the complex promotes preciliary trafficking and cilia growth. Forms a complex containing RAB11A, ASAP1, Rabin8/RAB3IP, RAP11FIP3 and ARF4; the complex promotes preciliary trafficking; the complex binds to RHO in photoreceptor cells and promotes RHO ciliary transport. Interacts (GTP-bound form) with WDR44; the interaction prevents RAB11A-RAB3IP-RAB11FIP3 complex formation (By similarity).Cell membraneLipid-anchorEndosome membraneRecycling endosome membraneLipid-anchorCleavage furrowCytoplasmic vesiclePhagosomeCytoplasmic vesicle membraneGolgi apparatusGolgi apparatusTrans-Golgi networkLocalized to WDR44-positive endosomes and tubules. Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Localizes to the cleavage furrow. During interphase, localized in vesicles continuously moving from peripheral sorting endosomes towards the pericentrosomal ERC. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localized to rhodopsin transport carriers when interacting with RAB11AFIP3 and ASAP1 in photoreceptors.Detected in various tissues, such as brain, testis, spleen, and heart.Belongs to the small GTPase superfamily. Rab family.AcetylationCell cycleCell membraneCytoplasmic vesicleEndosomeGolgi apparatusGTP-bindingHydrolaseLipoproteinMembraneMethylationNucleotide-bindingPrenylationProtein transportReference proteomeTransportGTPGTPGTPGTPGTPMGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPIHVPPTTENKPKVQCCQNI
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