ID RB11A_RAT Reviewed; 216 AA. AC P62494; P24410; Q9JLX1; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 169. DE RecName: Full=Ras-related protein Rab-11A {ECO:0000250|UniProtKB:P62492}; DE Short=Rab-11 {ECO:0000250|UniProtKB:P62492}; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62491}; DE AltName: Full=24KG; DE Flags: Precursor; GN Name=Rab11a {ECO:0000312|RGD:619762}; GN Synonyms=Rab11 {ECO:0000250|UniProtKB:P62492}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=1711847; DOI=10.1016/0006-291x(91)90672-t; RA Sakurada K., Uchida K., Yamaguchi K., Aisaka K., Ito S., Ohmori T., RA Takeyama Y., Ueda T., Hori Y., Ohyanagi H., Saitoh Y., Kaibuchi K., RA Takai Y.; RT "Molecular cloning and characterization of a ras p21-like GTP-binding RT protein (24KG) from rat liver."; RL Biochem. Biophys. Res. Commun. 177:1224-1232(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND INTERACTION WITH RAB11FIP5. RX PubMed=11163216; DOI=10.1016/s1097-2765(00)00140-4; RA Prekeris R., Klumperman J., Scheller R.H.; RT "A Rab11/Rip11 protein complex regulates apical membrane trafficking via RT recycling endosomes."; RL Mol. Cell 6:1437-1448(2000). RN [4] RP INTERACTION WITH STXBP6. RX PubMed=12145319; DOI=10.1074/jbc.m204929200; RA Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.; RT "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex RT assembly."; RL J. Biol. Chem. 277:28271-28279(2002). RN [5] RP INTERACTION WITH ZFYVE27. RX PubMed=17082457; DOI=10.1126/science.1134027; RA Shirane M., Nakayama K.I.; RT "Protrudin induces neurite formation by directional membrane trafficking."; RL Science 314:818-821(2006). CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular CC membrane trafficking, from the formation of transport vesicles to their CC fusion with membranes (By similarity). Rabs cycle between an inactive CC GDP-bound form and an active GTP-bound form that is able to recruit to CC membranes different set of downstream effectors directly responsible CC for vesicle formation, movement, tethering and fusion (By similarity). CC The small Rab GTPase RAB11A regulates endocytic recycling CC (PubMed:11163216). Forms a functional Rab11/FIP3/dynein complex that CC regulates the movement of peripheral sorting endosomes (SE) along CC microtubule tracks toward the microtubule organizing center/centrosome, CC generating the endosomal recycling compartment (ERC) (By similarity). CC Acts as a major regulator of membrane delivery during cytokinesis. CC Together with MYO5B and RAB8A participates in epithelial cell CC polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, CC PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the CC apical membrane initiation sites (AMIS), apical surface formation and CC lumenogenesis. Together with MYO5B participates in CFTR trafficking to CC the plasma membrane and TF (Transferrin) recycling in nonpolarized CC cells. Required in a complex with MYO5B and RAB11FIP2 for the transport CC of NPC1L1 to the plasma membrane. Participates in the sorting and CC basolateral transport of CDH1 from the Golgi apparatus to the plasma CC membrane. Regulates the recycling of FCGRT (receptor of Fc region of CC monomeric Ig G) to basolateral membranes (By similarity). May also play CC a role in melanosome transport and release from melanocytes (By CC similarity). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to CC mother centriole by forming a ciliary targeting complex containing CC Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating CC ciliogenesis initiation. On the contrary, upon LPAR1 receptor signaling CC pathway activation, interaction with phosphorylated WDR44 prevents CC Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (By CC similarity). Participates in the export of a subset of neosynthesized CC proteins through a Rab8-Rab10-Rab11-endososomal dependent export route CC via interaction with WDR44 (By similarity). CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62492, CC ECO:0000269|PubMed:11163216}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000250|UniProtKB:P62491}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62491}; CC -!- SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C- CC terminus) and RAB11FIP4 (By similarity). Forms a complex with RAB11FIP3 CC and dynein intermediate chain DYNC1LI1; the interaction between RAB11A1 CC and RAB11FIP3 is direct; the complex regulates endocytic trafficking CC (By similarity). Interacts with EVI5; EVI5 and RAB11FIP3 may be CC mutually exclusive and compete for binding RAB11A (By similarity). CC Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39 (By similarity). CC Interacts with EXOC6 in a GTP-dependent manner. Interacts with CC RAB11FIP5 (PubMed:11163216). Interacts with STXBP6 (PubMed:12145319). CC Interacts (GDP-bound form) with ZFYVE27 (PubMed:17082457). Interacts CC with BIRC6/bruce (By similarity). May interact with TBC1D14 (By CC similarity). Interacts with UNC119; in a cell cycle-dependent manner CC (By similarity). GDP-bound and nucleotide-free forms interact with CC SH3BP5 (By similarity). Interacts (GDP-bound form) with KIF5A in a CC ZFYVE27-dependent manner (By similarity). Interacts (GDP-bound form) CC with RELCH (By similarity). Found in a complex composed of RELCH, OSBP1 CC and RAB11A (By similarity). Interacts with TBC1D12 (By similarity). CC Interacts with DEF6 (By similarity). Interacts with ATP9A (By CC similarity). Forms a heterotetramer with RAB11FIP3; the GTP-bound form CC is preferred for binding. Forms a complex with Rabin8/RAB3IP and CC RAB11FIP3, probably a heterohexamer with two of each protein subunit, CC where Rabin8/RAB3IP and RAB11FIP3 simultaneously bind to RAB11A; the CC complex promotes preciliary trafficking and cilia growth. Forms a CC complex containing RAB11A, ASAP1, Rabin8/RAB3IP, RAP11FIP3 and ARF4; CC the complex promotes preciliary trafficking; the complex binds to RHO CC in photoreceptor cells and promotes RHO ciliary transport. Interacts CC (GTP-bound form) with WDR44; the interaction prevents RAB11A-RAB3IP- CC RAB11FIP3 complex formation (By similarity). CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62492, CC ECO:0000269|PubMed:11163216, ECO:0000269|PubMed:12145319, CC ECO:0000269|PubMed:17082457}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62491}; CC Lipid-anchor {ECO:0000305}. Endosome membrane CC {ECO:0000250|UniProtKB:P62491}. Recycling endosome membrane CC {ECO:0000250|UniProtKB:P62491}; Lipid-anchor {ECO:0000305}. Cleavage CC furrow {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle, phagosome CC {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:P62491}. Golgi apparatus CC {ECO:0000250|UniProtKB:P62491}. Golgi apparatus, trans-Golgi network CC {ECO:0000250|UniProtKB:P62491}. Note=Localized to WDR44-positive CC endosomes and tubules. Translocates with RAB11FIP2 from the vesicles of CC the endocytic recycling compartment (ERC) to the plasma membrane. CC Localizes to the cleavage furrow. During interphase, localized in CC vesicles continuously moving from peripheral sorting endosomes towards CC the pericentrosomal ERC. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, CC PODXL and RAB8A in apical membrane initiation sites (AMIS) during the CC generation of apical surface and lumenogenesis. Localized to rhodopsin CC transport carriers when interacting with RAB11AFIP3 and ASAP1 in CC photoreceptors. {ECO:0000250|UniProtKB:P62491}. CC -!- TISSUE SPECIFICITY: Detected in various tissues, such as brain, testis, CC spleen, and heart. {ECO:0000269|PubMed:1711847}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M75153; AAA42012.1; -; mRNA. DR EMBL; BC085727; AAH85727.1; -; mRNA. DR PIR; JN0056; JN0056. DR RefSeq; NP_112414.1; NM_031152.2. DR AlphaFoldDB; P62494; -. DR SMR; P62494; -. DR BioGRID; 249688; 1. DR DIP; DIP-46857N; -. DR IntAct; P62494; 7. DR MINT; P62494; -. DR STRING; 10116.ENSRNOP00000015598; -. DR iPTMnet; P62494; -. DR PhosphoSitePlus; P62494; -. DR jPOST; P62494; -. DR PaxDb; 10116-ENSRNOP00000015598; -. DR Ensembl; ENSRNOT00000015598.4; ENSRNOP00000015598.3; ENSRNOG00000011302.4. DR Ensembl; ENSRNOT00055042525; ENSRNOP00055034730; ENSRNOG00055024661. DR Ensembl; ENSRNOT00060035605; ENSRNOP00060029272; ENSRNOG00060020490. DR Ensembl; ENSRNOT00065010010; ENSRNOP00065007285; ENSRNOG00065006474. DR GeneID; 81830; -. DR KEGG; rno:81830; -. DR UCSC; RGD:619762; rat. DR AGR; RGD:619762; -. DR CTD; 8766; -. DR RGD; 619762; Rab11a. DR eggNOG; KOG0087; Eukaryota. DR GeneTree; ENSGT00940000154914; -. DR HOGENOM; CLU_041217_23_0_1; -. DR InParanoid; P62494; -. DR OrthoDB; 3487147at2759; -. DR PhylomeDB; P62494; -. DR TreeFam; TF300099; -. DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium. DR Reactome; R-RNO-8854214; TBC/RABGAPs. DR Reactome; R-RNO-8873719; RAB geranylgeranylation. DR PRO; PR:P62494; -. DR Proteomes; UP000002494; Chromosome 8. DR Bgee; ENSRNOG00000011302; Expressed in stomach and 20 other cell types or tissues. DR GO; GO:0005814; C:centriole; ISO:RGD. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0030666; C:endocytic vesicle membrane; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; ISO:RGD. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0005771; C:multivesicular body; ISO:RGD. DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB. DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0055037; C:recycling endosome; IDA:MGI. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0000922; C:spindle pole; ISO:RGD. DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB. DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB. DR GO; GO:0030133; C:transport vesicle; IBA:GO_Central. DR GO; GO:0031982; C:vesicle; ISO:RGD. DR GO; GO:0051959; F:dynein light intermediate chain binding; ISS:UniProtKB. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0005525; F:GTP binding; IDA:RGD. DR GO; GO:0003924; F:GTPase activity; IDA:RGD. DR GO; GO:0008017; F:microtubule binding; ISO:RGD. DR GO; GO:0031489; F:myosin V binding; ISO:RGD. DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:RGD. DR GO; GO:0030953; P:astral microtubule organization; ISO:RGD. DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:RGD. DR GO; GO:0072594; P:establishment of protein localization to organelle; ISO:RGD. DR GO; GO:0051650; P:establishment of vesicle localization; ISO:RGD. DR GO; GO:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:1990182; P:exosomal secretion; ISO:RGD. DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB. DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISO:RGD. DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD. DR GO; GO:0036258; P:multivesicular body assembly; ISO:RGD. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:RGD. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:RGD. DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD. DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB. DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB. DR GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD. DR GO; GO:1902954; P:regulation of early endosome to recycling endosome transport; ISS:UniProtKB. DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD. DR GO; GO:0010796; P:regulation of multivesicular body size; ISO:RGD. DR GO; GO:1904779; P:regulation of protein localization to centrosome; ISS:UniProtKB. DR GO; GO:0051223; P:regulation of protein transport; IMP:RGD. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISO:RGD. DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD. DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO. DR CDD; cd01868; Rab11_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47979; DRAB11-RELATED; 1. DR PANTHER; PTHR47979:SF110; RAS-RELATED PROTEIN RAB-11A; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; P62494; RN. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Cell membrane; Cytoplasmic vesicle; Endosome; KW Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein; Membrane; KW Methylation; Nucleotide-binding; Prenylation; Protein transport; KW Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62491" FT CHAIN 2..213 FT /note="Ras-related protein Rab-11A" FT /id="PRO_0000121156" FT PROPEP 214..216 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000370812" FT REGION 183..211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 40..48 FT /note="Effector region" FT /evidence="ECO:0000255" FT BINDING 18..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62491" FT BINDING 37..43 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62491" FT BINDING 66..70 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62491" FT BINDING 124..127 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62491" FT BINDING 154..156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62491" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000250|UniProtKB:P62491" FT MOD_RES 213 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000255" FT LIPID 212 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62491" FT LIPID 213 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62491" SQ SEQUENCE 216 AA; 24394 MW; 76FC1E113A29B269 CRC64; MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI //