ID RB11B_MOUSE Reviewed; 218 AA. AC P46638; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 195. DE RecName: Full=Ras-related protein Rab-11B; DE EC=3.6.5.2 {ECO:0000269|PubMed:10942597}; DE Flags: Precursor; GN Name=Rab11b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX PubMed=8001972; DOI=10.1006/geno.1994.1434; RA Lai F., Stubbs L., Artzt K.; RT "Molecular analysis of mouse Rab11b: a new type of mammalian YPT/Rab RT protein."; RL Genomics 22:610-616(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon; 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 PROTEIN SEQUENCE OF 5-24; 42-51; 62-72; 75-104; 111-125 AND 167-174, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP FUNCTION IN ENDOCYTIC RECYCLING, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, RP TOPOLOGY, AND MUTAGENESIS OF SER-25 AND GLN-70. RX PubMed=10942597; DOI=10.1006/excr.2000.4947; RA Schlierf B., Fey G.H., Hauber J., Hocke G.M., Rosorius O.; RT "Rab11b is essential for recycling of transferrin to the plasma membrane."; RL Exp. Cell Res. 259:257-265(2000). RN [5] RP FUNCTION IN EXOCYTOSIS, AND TISSUE SPECIFICITY. RX PubMed=19335615; DOI=10.1111/j.1365-2443.2009.01285.x; RA Sugawara K., Shibasaki T., Mizoguchi A., Saito T., Seino S.; RT "Rab11 and its effector Rip11 participate in regulation of insulin granule RT exocytosis."; RL Genes Cells 14:445-456(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION IN MELANOSOME TRANSPORT. RX PubMed=21291502; DOI=10.1111/j.1600-0854.2011.01172.x; RA Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N., RA Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T., RA Sturm R.A., Stow J.L.; RT "The recycling endosome protein Rab17 regulates melanocytic filopodia RT formation and melanosome trafficking."; RL Traffic 12:627-643(2011). RN [8] RP FUNCTION. RX PubMed=22129970; DOI=10.1152/ajprenal.00304.2011; RA Butterworth M.B., Edinger R.S., Silvis M.R., Gallo L.I., Liang X., RA Apodaca G., Frizzell R.A., Fizzell R.A., Johnson J.P.; RT "Rab11b regulates the trafficking and recycling of the epithelial sodium RT channel (ENaC)."; RL Am. J. Physiol. 302:F581-F590(2012). RN [9] RP INTERACTION WITH KCNMA1. RX PubMed=22935415; DOI=10.1016/j.bbrc.2012.08.067; RA Sokolowski S., Harvey M., Sakai Y., Jordan A., Sokolowski B.; RT "The large conductance calcium-activated K(+) channel interacts with the RT small GTPase Rab11b."; RL Biochem. Biophys. Res. Commun. 426:221-225(2012). RN [10] RP CITRULLINATION AT ARG-4. RX PubMed=24463520; DOI=10.1038/nature12942; RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.; RT "Citrullination regulates pluripotency and histone H1 binding to RT chromatin."; RL Nature 507:104-108(2014). RN [11] RP INTERACTION WITH RELCH. RX PubMed=29514919; DOI=10.1083/jcb.201709123; RA Sobajima T., Yoshimura S.I., Maeda T., Miyata H., Miyoshi E., Harada A.; RT "The Rab11-binding protein RELCH/KIAA1468 controls intracellular RT cholesterol distribution."; RL J. Cell Biol. 217:1777-1796(2018). 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. Rabs cycle between an inactive GDP-bound form CC and an active GTP-bound form that is able to recruit to membranes CC different set of downstream effectors directly responsible for vesicle CC formation, movement, tethering and fusion. The small Rab GTPase RAB11B CC plays a role in endocytic recycling, regulating apical recycling of CC several transmembrane proteins including cystic fibrosis transmembrane CC conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium CC voltage-gated channel, and voltage-dependent L-type calcium channel. CC May also regulate constitutive and regulated secretion, like insulin CC granule exocytosis. Required for melanosome transport and release from CC melanocytes. Also regulates V-ATPase intracellular transport in CC response to extracellular acidosis. Promotes Rabin8/RAB3IP preciliary CC vesicular trafficking to mother centriole by forming a ciliary CC targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and CC ARF4, thereby regulating ciliogenesis initiation. On the contrary, upon CC LPAR1 receptor signaling pathway activation, interaction with CC phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation CC and cilia growth (By similarity). {ECO:0000250|UniProtKB:Q15907, CC ECO:0000269|PubMed:10942597, ECO:0000269|PubMed:19335615, CC ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22129970}. 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:0000269|PubMed:10942597}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000269|PubMed:10942597}; CC -!- SUBUNIT: Interacts with KCNMA1 (PubMed:22935415). Interacts with CC RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4 (By similarity). May CC interact with TBC1D14 (By similarity). Interacts with ATP6V1E1 (By CC similarity). Interacts with PI4KB (By similarity). Interacts (GDP-bound CC form) with ZFYVE27 (By similarity). Interacts (GDP-bound form) with CC KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts with CC RELCH (PubMed:29514919). Interacts (in GTP-bound form) with TBC1D8B CC (via domain Rab-GAP TBC) (By similarity). Forms a complex containing CC RAB11B, ASAP1, Rabin8/RAB3IP, RAP11FIP3 and ARF4. Interacts with WDR44 CC (By similarity). {ECO:0000250|UniProtKB:Q15907, CC ECO:0000269|PubMed:22935415, ECO:0000269|PubMed:29514919}. CC -!- INTERACTION: CC P46638; C3VLD3: Kcnma1; NbExp=4; IntAct=EBI-1634944, EBI-6512684; CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane CC {ECO:0000305|PubMed:10942597}; Lipid-anchor CC {ECO:0000305|PubMed:10942597}; Cytoplasmic side CC {ECO:0000305|PubMed:10942597}. Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane {ECO:0000250|UniProtKB:O35509}; Lipid-anchor CC {ECO:0000250|UniProtKB:O35509}; Cytoplasmic side CC {ECO:0000250|UniProtKB:O35509}. Cytoplasmic vesicle, phagosome membrane CC {ECO:0000250|UniProtKB:Q15907}; Lipid-anchor CC {ECO:0000250|UniProtKB:Q15907}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q15907}. CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and testis. CC Also detected in kidney and pancreatic islets. CC {ECO:0000269|PubMed:19335615}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. 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; L26528; AAC42093.1; -; mRNA. DR EMBL; BC054753; AAH54753.1; -; mRNA. DR EMBL; BC085270; AAH85270.1; -; mRNA. DR CCDS; CCDS28628.1; -. DR PIR; A55005; A55005. DR RefSeq; NP_033023.1; NM_008997.3. DR AlphaFoldDB; P46638; -. DR SMR; P46638; -. DR BioGRID; 202532; 14. DR IntAct; P46638; 14. DR MINT; P46638; -. DR STRING; 10090.ENSMUSP00000110021; -. DR GlyGen; P46638; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P46638; -. DR PhosphoSitePlus; P46638; -. DR EPD; P46638; -. DR jPOST; P46638; -. DR PaxDb; 10090-ENSMUSP00000110021; -. DR PeptideAtlas; P46638; -. DR ProteomicsDB; 300245; -. DR Pumba; P46638; -. DR TopDownProteomics; P46638; -. DR Antibodypedia; 24871; 203 antibodies from 30 providers. DR DNASU; 19326; -. DR Ensembl; ENSMUST00000057373.14; ENSMUSP00000110021.5; ENSMUSG00000077450.14. DR GeneID; 19326; -. DR KEGG; mmu:19326; -. DR UCSC; uc008bzm.1; mouse. DR AGR; MGI:99425; -. DR CTD; 9230; -. DR MGI; MGI:99425; Rab11b. DR VEuPathDB; HostDB:ENSMUSG00000077450; -. DR eggNOG; KOG0087; Eukaryota. DR GeneTree; ENSGT00940000161659; -. DR HOGENOM; CLU_041217_23_0_1; -. DR InParanoid; P46638; -. DR OMA; YHIVSNK; -. DR OrthoDB; 3487147at2759; -. DR PhylomeDB; P46638; -. DR TreeFam; TF300099; -. DR Reactome; R-MMU-8854214; TBC/RABGAPs. DR Reactome; R-MMU-8873719; RAB geranylgeranylation. DR BioGRID-ORCS; 19326; 8 hits in 79 CRISPR screens. DR ChiTaRS; Rab11b; mouse. DR PRO; PR:P46638; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; P46638; Protein. DR Bgee; ENSMUSG00000077450; Expressed in cortical plate and 225 other cell types or tissues. DR ExpressionAtlas; P46638; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB. DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB. DR GO; GO:0031489; F:myosin V binding; ISO:MGI. DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:MGI. DR GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB. DR GO; GO:0045054; P:constitutive secretory pathway; ISS:UniProtKB. DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB. DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI. DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB. DR GO; GO:0032402; P:melanosome transport; IMP:UniProtKB. DR GO; GO:0001881; P:receptor recycling; IMP:UniProtKB. DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB. DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:UniProtKB. DR GO; GO:0044070; P:regulation of monoatomic anion transport; ISS:UniProtKB. DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0033572; P:transferrin transport; IMP:UniProtKB. 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:SF41; RAS-RELATED PROTEIN RAB-11B; 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; P46638; MM. PE 1: Evidence at protein level; KW Acetylation; Citrullination; Cytoplasmic vesicle; KW Direct protein sequencing; Endosome; GTP-binding; Hydrolase; Lipoprotein; KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport; KW Reference proteome; Synapse; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT CHAIN 2..215 FT /note="Ras-related protein Rab-11B" FT /id="PRO_0000121159" FT PROPEP 216..218 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:P51157" FT /id="PRO_0000370816" FT REGION 184..218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 40..48 FT /note="Effector region" FT /evidence="ECO:0000255" FT COMPBIAS 196..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 18..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT BINDING 66..70 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT BINDING 124..127 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT BINDING 154..156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT MOD_RES 4 FT /note="Citrulline" FT /evidence="ECO:0000269|PubMed:24463520" FT MOD_RES 215 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:P51157" FT LIPID 214 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT LIPID 215 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q15907" FT MUTAGEN 25 FT /note="S->N: Dominant negative mutant locked in the FT inactive GDP-bound form; partially relocalizes to the Golgi FT and alters endocytic recycling." FT /evidence="ECO:0000269|PubMed:10942597" FT MUTAGEN 70 FT /note="Q->L: Constitutively active mutant locked in the FT active GTP-bound form; alters endocytic recycling." FT /evidence="ECO:0000269|PubMed:10942597" SQ SEQUENCE 218 AA; 24489 MW; 8DE0A98739EBD9FF CRC64; MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ IADRAAHDES PGNNVVDISV PPTTDGQRPN KLQCCQSL //