ID RB11A_MOUSE Reviewed; 216 AA.
AC P62492; P24410; Q3V1Z6; Q9JLX1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=Ras-related protein Rab-11A {ECO:0000303|PubMed:26506309};
DE Short=Rab-11 {ECO:0000303|PubMed:26506309};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62491};
DE Flags: Precursor;
GN Name=Rab11a {ECO:0000312|MGI:MGI:1858202};
GN Synonyms=Rab11 {ECO:0000303|PubMed:10708602};
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 [GENOMIC DNA].
RX PubMed=10708602; DOI=10.1006/bbrc.2000.2334;
RA Bhartur S.G., Calhoun B.C., Woodrum J., Kurkjian J., Iyer S., Lai F.,
RA Goldenring J.R.;
RT "Genomic structure of murine rab11 family members.";
RL Biochem. Biophys. Res. Commun. 269:611-617(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [4]
RP PROTEIN SEQUENCE OF 14-24; 42-51 AND 83-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH EXOC6.
RX PubMed=15292201; DOI=10.1074/jbc.m402264200;
RA Zhang X.-M., Ellis S., Sriratana A., Mitchell C.A., Rowe T.;
RT "Sec15 is an effector for the Rab11 GTPase in mammalian cells.";
RL J. Biol. Chem. 279:43027-43034(2004).
RN [6]
RP INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP INTERACTION WITH VIPAS39.
RX PubMed=20190753; DOI=10.1038/ng.538;
RA Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P.,
RA Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H., Knisely A.S.,
RA Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT cholestasis syndrome phenotype with defects in epithelial polarization.";
RL Nat. Genet. 42:303-312(2010).
RN [9]
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 [10]
RP INTERACTION WITH SH3BP5.
RX PubMed=26506309; DOI=10.1016/j.devcel.2015.09.013;
RA Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T., Nakai J.,
RA Hara T., Sato K., Sato K.;
RT "REI-1 is a guanine nucleotide exchange factor regulating RAB-11
RT localization and function in C. elegans embryos.";
RL Dev. Cell 35:211-221(2015).
RN [11]
RP INTERACTION WITH TBC1D12.
RX PubMed=28384198; DOI=10.1371/journal.pone.0174883;
RA Oguchi M.E., Noguchi K., Fukuda M.;
RT "TBC1D12 is a novel Rab11-binding protein that modulates neurite outgrowth
RT of PC12 cells.";
RL PLoS ONE 12:E0174883-E0174883(2017).
RN [12]
RP INTERACTION WITH RELCH, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A
RP COMPLEX WITH RECHL AND OSBP1.
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 (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 (By
CC similarity). 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
CC (PubMed:21291502). Promotes Rabin8/RAB3IP preciliary vesicular
CC trafficking to mother centriole by forming a ciliary targeting complex
CC containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby
CC regulating ciliogenesis initiation. On the contrary, upon LPAR1
CC receptor signaling pathway activation, interaction with phosphorylated
CC WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia
CC growth (By similarity). Participates in the export of a subset of
CC neosynthesized proteins through a Rab8-Rab10-Rab11-endososomal
CC dependent export route via interaction with WDR44 (By similarity).
CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62494,
CC ECO:0000269|PubMed:21291502}.
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). Interacts with EVI5; EVI5 and
CC RAB11FIP3 may be mutually exclusive and compete for binding RAB11A (By
CC similarity). Forms a complex with RAB11FIP3 and dynein intermediate
CC chain DYNC1LI1; the interaction between RAB11A1 and RAB11FIP3 is
CC direct; the complex regulates endocytic trafficking (By similarity).
CC Interacts with RAB11FIP5 (By similarity). Interacts with STXBP6 (By
CC similarity). Interacts (GDP-bound form) with ZFYVE27 (By similarity).
CC Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39 (PubMed:17509819,
CC PubMed:20190753). Interacts with EXOC6 in a GTP-dependent manner
CC (PubMed:15292201). Interacts with BIRC6/bruce (By similarity). May
CC interact with TBC1D14 (By similarity). Interacts with UNC119; in a cell
CC cycle-dependent manner (By similarity). GDP-bound and nucleotide-free
CC forms interact with SH3BP5 (PubMed:26506309). Interacts (GDP-bound
CC form) with KIF5A in a ZFYVE27-dependent manner (By similarity).
CC Interacts (GDP-bound form) with RELCH (PubMed:29514919). Found in a
CC complex composed of RELCH, OSBP1 and RAB11A (PubMed:29514919).
CC Interacts with TBC1D12 (PubMed:28384198). Interacts with DEF6 (By
CC similarity). Interacts with VPS33B (By similarity). Interacts with
CC ATP9A (By similarity). Forms a heterotetramer with RAB11FIP3; the GTP-
CC bound form is preferred for binding. Forms a complex with Rabin8/RAB3IP
CC and RAB11FIP3, probably a heterohexamer with two of each protein
CC subunit, where Rabin8/RAB3IP and RAB11FIP3 simultaneously bind to
CC RAB11A; the complex promotes preciliary trafficking and cilia growth.
CC Forms a complex containing RAB11A, ASAP1, Rabin8/RAB3IP, RAP11FIP3 and
CC ARF4; the complex promotes preciliary trafficking; the complex binds to
CC RHO in photoreceptor cells and promotes RHO ciliary transport.
CC Interacts (GTP-bound form) with WDR44; the interaction prevents RAB11A-
CC RAB3IP-RAB11FIP3 complex formation (By similarity).
CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62494,
CC ECO:0000269|PubMed:15292201, ECO:0000269|PubMed:17509819,
CC ECO:0000269|PubMed:26506309, ECO:0000269|PubMed:28384198,
CC ECO:0000269|PubMed:29514919}.
CC -!- INTERACTION:
CC P62492; P59016: Vps33b; NbExp=3; IntAct=EBI-770256, EBI-2656383;
CC P62492; Q62739: Rab3ip; Xeno; NbExp=4; IntAct=EBI-770256, EBI-2028671;
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:0000269|PubMed:29514919}; 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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF127669; AAF36458.1; -; Genomic_DNA.
DR EMBL; AK014268; BAB29233.1; -; mRNA.
DR EMBL; AK132072; BAE20971.1; -; mRNA.
DR EMBL; AK132159; BAE21003.1; -; mRNA.
DR EMBL; AK147122; BAE27693.1; -; mRNA.
DR EMBL; BC010722; AAH10722.1; -; mRNA.
DR CCDS; CCDS23282.1; -.
DR RefSeq; NP_059078.2; NM_017382.5.
DR AlphaFoldDB; P62492; -.
DR SMR; P62492; -.
DR BioGRID; 207498; 17.
DR IntAct; P62492; 25.
DR MINT; P62492; -.
DR STRING; 10090.ENSMUSP00000129163; -.
DR GlyGen; P62492; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62492; -.
DR PhosphoSitePlus; P62492; -.
DR SwissPalm; P62492; -.
DR jPOST; P62492; -.
DR PaxDb; 10090-ENSMUSP00000129163; -.
DR PeptideAtlas; P62492; -.
DR ProteomicsDB; 255112; -.
DR Pumba; P62492; -.
DR TopDownProteomics; P62492; -.
DR Antibodypedia; 4588; 548 antibodies from 39 providers.
DR DNASU; 53869; -.
DR Ensembl; ENSMUST00000172298.8; ENSMUSP00000129163.2; ENSMUSG00000004771.13.
DR GeneID; 53869; -.
DR KEGG; mmu:53869; -.
DR UCSC; uc009qce.1; mouse.
DR AGR; MGI:1858202; -.
DR CTD; 8766; -.
DR MGI; MGI:1858202; Rab11a.
DR VEuPathDB; HostDB:ENSMUSG00000004771; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000154914; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P62492; -.
DR OMA; ITAIYQM; -.
DR OrthoDB; 3487147at2759; -.
DR PhylomeDB; P62492; -.
DR TreeFam; TF300099; -.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 53869; 3 hits in 79 CRISPR screens.
DR ChiTaRS; Rab11a; mouse.
DR PRO; PR:P62492; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P62492; Protein.
DR Bgee; ENSMUSG00000004771; Expressed in lip and 265 other cell types or tissues.
DR ExpressionAtlas; P62492; baseline and differential.
DR Genevisible; P62492; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030666; C:endocytic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
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:MGI.
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; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
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:0030953; P:astral microtubule organization; ISO:MGI.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
DR GO; GO:0072594; P:establishment of protein localization to organelle; ISO:MGI.
DR GO; GO:0051650; P:establishment of vesicle localization; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:1990182; P:exosomal secretion; ISO:MGI.
DR GO; GO:0032402; P:melanosome transport; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISO:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0036258; P:multivesicular body assembly; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:MGI.
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:MGI.
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; ISO:MGI.
DR GO; GO:0010796; P:regulation of multivesicular body size; ISO:MGI.
DR GO; GO:1904779; P:regulation of protein localization to centrosome; ISS:UniProtKB.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
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.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell membrane; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; Golgi apparatus; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; 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_0000121152"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370808"
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"
FT CONFLICT 180
FT /note="Q -> H (in Ref. 1; AAF36458)"
FT /evidence="ECO:0000305"
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
//
