RB11B_MOUSE
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 03-AUG-2022, entry version 186.
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, Pancreas,
RC 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. {ECO:0000269|PubMed:10942597,
CC ECO:0000269|PubMed:19335615, ECO:0000269|PubMed:21291502,
CC 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).
CC {ECO:0000250|UniProtKB:Q15907, ECO:0000269|PubMed:22935415,
CC 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}.
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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; 11.
DR IntAct; P46638; 14.
DR MINT; P46638; -.
DR STRING; 10090.ENSMUSP00000110021; -.
DR iPTMnet; P46638; -.
DR PhosphoSitePlus; P46638; -.
DR EPD; P46638; -.
DR jPOST; P46638; -.
DR PaxDb; P46638; -.
DR PeptideAtlas; P46638; -.
DR PRIDE; P46638; -.
DR ProteomicsDB; 300245; -.
DR TopDownProteomics; P46638; -.
DR Antibodypedia; 24871; 189 antibodies from 30 providers.
DR DNASU; 19326; -.
DR Ensembl; ENSMUST00000057373; ENSMUSP00000110021; ENSMUSG00000077450.
DR GeneID; 19326; -.
DR KEGG; mmu:19326; -.
DR UCSC; uc008bzm.1; mouse.
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; NIRAQIW; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; P46638; -.
DR TreeFam; TF300099; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19326; 7 hits in 74 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 222 other tissues.
DR ExpressionAtlas; P46638; baseline and differential.
DR Genevisible; P46638; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
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: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:0006887; P:exocytosis; IBA:GO_Central.
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:0044070; P:regulation of anion transport; ISS:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP: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 GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
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
