RB11A_HUMAN
ID RB11A_HUMAN Reviewed; 216 AA.
AC P62491; B2R4B6; B4DT13; P24410; Q5TZN9; Q9JLX1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 197.
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:0000269|PubMed:15837192, ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804};
DE AltName: Full=YL8;
DE Flags: Precursor;
GN Name=RAB11A {ECO:0000312|HGNC:HGNC:9760};
GN Synonyms=RAB11 {ECO:0000303|PubMed:12470645};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1704119;
RA Drivas G.T., Shih A., Coutavas E.E., D'Eustachio P., Rush M.G.;
RT "Identification and characterization of a human homolog of the
RT Schizosaccharomyces pombe ras-like gene YPT-3.";
RL Oncogene 6:3-9(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zahraoui A., Joberty G., Tavitian A.;
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9662449; DOI=10.1016/s0014-5793(98)00607-3;
RA Gromov P.S., Celis J.E., Hansen C., Tommerup N., Gromova I., Madsen P.;
RT "Human rab11a: transcription, chromosome mapping and effect on the
RT expression levels of host GTP-binding proteins.";
RL FEBS Lett. 429:359-364(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [11]
RP PROTEIN SEQUENCE OF 2-24; 34-58; 62-72; 75-95 AND 133-140, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Platelet;
RA Bienvenut W.V.;
RL Submitted (OCT-2005) to UniProtKB.
RN [12]
RP INTERACTION WITH RAB11FIP1; RAB11FIP2; RAB11FIP3 AND RAB11FIP4.
RX PubMed=11495908; DOI=10.1074/jbc.m104831200;
RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R.,
RA Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.;
RT "Identification and characterization of a family of Rab11-interacting
RT proteins.";
RL J. Biol. Chem. 276:39067-39075(2001).
RN [13]
RP INTERACTION WITH RAB11FIP4.
RX PubMed=12470645; DOI=10.1016/s0006-291x(02)02720-1;
RA Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.;
RT "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its
RT overexpression condenses the Rab11 positive compartment in HeLa cells.";
RL Biochem. Biophys. Res. Commun. 299:770-779(2002).
RN [14]
RP INTERACTION WITH RAB11FIP4.
RC TISSUE=Cervix carcinoma;
RX PubMed=11786538; DOI=10.1074/jbc.m108665200;
RA Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B.,
RA Bucci C., McCaffrey M.W.;
RT "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein.";
RL J. Biol. Chem. 277:12190-12199(2002).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=11994279; DOI=10.1074/jbc.m200757200;
RA Lindsay A.J., McCaffrey M.W.;
RT "Rab11-FIP2 functions in transferrin recycling and associates with
RT endosomal membranes via its COOH-terminal domain.";
RL J. Biol. Chem. 277:27193-27199(2002).
RN [16]
RP INTERACTION WITH RAB11FIP1.
RX PubMed=15280022; DOI=10.1016/j.febslet.2004.06.068;
RA Lindsay A.J., McCaffrey M.W.;
RT "Characterisation of the Rab binding properties of Rab coupling protein
RT (RCP) by site-directed mutagenesis.";
RL FEBS Lett. 571:86-92(2004).
RN [17]
RP INTERACTION WITH RAB11FIP2.
RX PubMed=15173169; DOI=10.1074/jbc.m404633200;
RA Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H.,
RA Prekeris R.;
RT "Molecular characterization of Rab11 interactions with members of the
RT family of Rab11-interacting proteins.";
RL J. Biol. Chem. 279:33430-33437(2004).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=15304524; DOI=10.1242/jcs.01280;
RA Lindsay A.J., McCaffrey M.W.;
RT "The C2 domains of the class I Rab11 family of interacting proteins target
RT recycling vesicles to the plasma membrane.";
RL J. Cell Sci. 117:4365-4375(2004).
RN [19]
RP INTERACTION WITH RAB11FIP1, AND SUBCELLULAR LOCATION.
RX PubMed=15181150; DOI=10.1091/mbc.e03-12-0918;
RA Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H.,
RA Prekeris R.;
RT "The RCP-Rab11 complex regulates endocytic protein sorting.";
RL Mol. Biol. Cell 15:3530-3541(2004).
RN [20]
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
RX PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
RA Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R.,
RA Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane
RT traffic in cytokinesis.";
RL EMBO J. 24:3389-3399(2005).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND RAB11FIP4,
RP AND MUTAGENESIS OF SER-25.
RX PubMed=15601896; DOI=10.1091/mbc.e04-10-0927;
RA Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S.,
RA Frey A.M., Peden A.A., Gould G.W., Prekeris R.;
RT "The FIP3-Rab11 protein complex regulates recycling endosome targeting to
RT the cleavage furrow during late cytokinesis.";
RL Mol. Biol. Cell 16:849-860(2005).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF SER-25 AND GLN-70.
RX PubMed=15689490; DOI=10.1091/mbc.e04-10-0867;
RA Lock J.G., Stow J.L.;
RT "Rab11 in recycling endosomes regulates the sorting and basolateral
RT transport of E-cadherin.";
RL Mol. Biol. Cell 16:1744-1755(2005).
RN [23]
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).
RN [24]
RP FUNCTION, INTERACTION WITH MYO5B, AND IDENTIFICATION IN A COMPLEX WITH
RP MYO5B AND CFTR.
RX PubMed=17462998; DOI=10.1074/jbc.m608531200;
RA Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S.,
RA Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E.,
RA Langford G.M., Fukuda M., Stanton B.A.;
RT "Myosin Vb is required for trafficking of the cystic fibrosis transmembrane
RT conductance regulator in Rab11a-specific apical recycling endosomes in
RT polarized human airway epithelial cells.";
RL J. Biol. Chem. 282:23725-23736(2007).
RN [25]
RP INTERACTION WITH RAB11FIP3 AND EVI5.
RX PubMed=17229837; DOI=10.1073/pnas.0610500104;
RA Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R.,
RA Scheller R.H., Jackson P.K., Eldridge A.G.;
RT "Identification of Rab11 as a small GTPase binding protein for the Evi5
RT oncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007).
RN [26]
RP INTERACTION WITH BIRC6/BRUCE.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled by
RT BRUCE.";
RL Cell 132:832-845(2008).
RN [27]
RP FUNCTION, INTERACTION WITH NPC1L1, AND MUTAGENESIS OF SER-25.
RX PubMed=19542231; DOI=10.1074/jbc.m109.034355;
RA Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L.,
RA Song B.-L.;
RT "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-
RT regulated translocation of NPC1L1 to the cell surface.";
RL J. Biol. Chem. 284:22481-22490(2009).
RN [28]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20890297; DOI=10.1038/ncb2106;
RA Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J.,
RA Martin-Belmonte F., Mostov K.E.;
RT "A molecular network for de novo generation of the apical surface and
RT lumen.";
RL Nat. Cell Biol. 12:1035-1045(2010).
RN [29]
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 [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP INTERACTION WITH ZFYVE27 AND KIF5A.
RX PubMed=21976701; DOI=10.1091/mbc.e11-01-0068;
RA Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
RT "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes
RT in vesicular transport during process formation.";
RL Mol. Biol. Cell 22:4602-4620(2011).
RN [32]
RP FUNCTION, AND INTERACTION WITH MYO5B.
RX PubMed=21282656; DOI=10.1073/pnas.1010754108;
RA Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.;
RT "Rab GTPase-Myo5B complexes control membrane recycling and epithelial
RT polarization.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011).
RN [33]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [34]
RP INTERACTION WITH TBC1D14.
RX PubMed=22613832; DOI=10.1083/jcb.201111079;
RA Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.;
RT "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive
RT recycling endosomes.";
RL J. Cell Biol. 197:659-675(2012).
RN [35]
RP INTERACTION WITH UNC119.
RX PubMed=23535298; DOI=10.4161/cc.24404;
RA Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.;
RT "UNC119a bridges the transmission of Fyn signals to Rab11, leading to the
RT completion of cytokinesis.";
RL Cell Cycle 12:1303-1315(2013).
RN [36]
RP ISOPRENYLATION AT CYS-212 AND CYS-213, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=24023390; DOI=10.1074/mcp.m113.030114;
RA Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T.,
RA Tran J.C., Thomas P.M., Kelleher N.L.;
RT "Large-scale top down proteomics of the human proteome: membrane proteins,
RT mitochondria, and senescence.";
RL Mol. Cell. Proteomics 12:3465-3473(2013).
RN [37]
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 [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [39]
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 [40]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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).
RN [41]
RP GLYCOSYLATION AT ARG-4 (MICROBIAL INFECTION).
RX PubMed=32974215; DOI=10.3389/fcimb.2020.00419;
RA Gan J., Scott N.E., Newson J.P.M., Wibawa R.R., Wong Fok Lung T.,
RA Pollock G.L., Ng G.Z., van Driel I., Pearson J.S., Hartland E.L.,
RA Giogha C.;
RT "The Salmonella effector SseK3 targets small Rab GTPases.";
RL Front. Cell. Infect. Microbiol. 10:419-419(2020).
RN [42]
RP INTERACTION WITH DEF6.
RX PubMed=31308374; DOI=10.1038/s41467-019-10812-x;
RA Serwas N.K., Hoeger B., Ardy R.C., Stulz S.V., Sui Z., Memaran N.,
RA Meeths M., Krolo A., Yuece Petronczki O., Pfajfer L., Hou T.Z.,
RA Halliday N., Santos-Valente E., Kalinichenko A., Kennedy A., Mace E.M.,
RA Mukherjee M., Tesi B., Schrempf A., Pickl W.F., Loizou J.I., Kain R.,
RA Bidmon-Fliegenschnee B., Schickel J.N., Glauzy S., Huemer J., Garncarz W.,
RA Salzer E., Pierides I., Bilic I., Thiel J., Priftakis P., Banerjee P.P.,
RA Foerster-Waldl E., Medgyesi D., Huber W.D., Orange J.S., Meffre E.,
RA Sansom D.M., Bryceson Y.T., Altman A., Boztug K.;
RT "Human DEF6 deficiency underlies an immunodeficiency syndrome with systemic
RT autoimmunity and aberrant CTLA-4 homeostasis.";
RL Nat. Commun. 10:3106-3106(2019).
RN [43]
RP ERRATUM OF PUBMED:31308374.
RX PubMed=31578334; DOI=10.1038/s41467-019-12454-5;
RA Serwas N.K., Hoeger B., Ardy R.C., Stulz S.V., Sui Z., Memaran N.,
RA Meeths M., Krolo A., Petronczki O.Y., Pfajfer L., Hou T.Z., Halliday N.,
RA Santos-Valente E., Kalinichenko A., Kennedy A., Mace E.M., Mukherjee M.,
RA Tesi B., Schrempf A., Pickl W.F., Loizou J.I., Kain R.,
RA Bidmon-Fliegenschnee B., Schickel J.N., Glauzy S., Huemer J., Garncarz W.,
RA Salzer E., Pierides I., Bilic I., Thiel J., Priftakis P., Banerjee P.P.,
RA Foerster-Waldl E., Medgyesi D., Huber W.D., Orange J.S., Meffre E.,
RA Sansom D.M., Bryceson Y.T., Altman A., Boztug K.;
RL Nat. Commun. 10:4555-4555(2019).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP ANALOG.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP ANALOG
RP AND GDP, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-70.
RX PubMed=15837192; DOI=10.1016/j.str.2005.01.014;
RA Pasqualato S., Cherfils J.;
RT "Crystallographic evidence for substrate-assisted GTP hydrolysis by a small
RT GTP binding protein.";
RL Structure 13:533-540(2005).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 6-175 IN COMPLEX WITH GTP AND
RP RAB11FIP3, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-70.
RX PubMed=17007872; DOI=10.1016/j.jmb.2006.08.064;
RA Eathiraj S., Mishra A., Prekeris R., Lambright D.G.;
RT "Structural basis for Rab11-mediated recruitment of FIP3 to recycling
RT endosomes.";
RL J. Mol. Biol. 364:121-135(2006).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 7-173 IN COMPLEX WITH GTP,
RP CATALYTIC ACTIVITY, INTERACTION WITH RAB11FIP3 AND RAB11FIP4, AND
RP MUTAGENESIS OF GLN-70.
RX PubMed=17030804; DOI=10.1073/pnas.0605357103;
RA Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
RA Wakatsuki S.;
RT "Structural basis for Rab11-dependent membrane recruitment of a family of
RT Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP,
RP CATALYTIC ACTIVITY, INTERACTION WITH RAB11FIP2, AND MUTAGENESIS OF GLN-70.
RX PubMed=16905101; DOI=10.1016/j.str.2006.06.010;
RA Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.;
RT "Crystal structure of rab11 in complex with rab11 family interacting
RT protein 2.";
RL Structure 14:1273-1283(2006).
RN [49] {ECO:0007744|PDB:6DJL}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SH3BP5, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-13; VAL-22; LYS-24; SER-25; PHE-36;
RP LEU-38; SER-40; LYS-41; ILE-44; GLN-70; ARG-82 AND SER-154.
RX PubMed=30217979; DOI=10.1038/s41467-018-06196-z;
RA Jenkins M.L., Margaria J.P., Stariha J.T.B., Hoffmann R.M., McPhail J.A.,
RA Hamelin D.J., Boulanger M.J., Hirsch E., Burke J.E.;
RT "Structural determinants of Rab11 activation by the guanine nucleotide
RT exchange factor SH3BP5.";
RL Nat. Commun. 9:3772-3772(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 RAB11A
CC regulates endocytic recycling. Acts as a major regulator of membrane
CC delivery during cytokinesis. Together with MYO5B and RAB8A participates
CC in epithelial cell polarization. Together with RAB3IP, RAB8A, the
CC exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes
CC transcytosis of PODXL to the apical membrane initiation sites (AMIS),
CC apical surface formation and lumenogenesis. Together with MYO5B
CC participates in CFTR trafficking to the plasma membrane and TF
CC (Transferrin) recycling in nonpolarized cells. Required in a complex
CC with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma
CC membrane. Participates in the sorting and basolateral transport of CDH1
CC from the Golgi apparatus to the plasma membrane. Regulates the
CC recycling of FCGRT (receptor of Fc region of monomeric Ig G) to
CC basolateral membranes. May also play a role in melanosome transport and
CC release from melanocytes. {ECO:0000269|PubMed:15601896,
CC ECO:0000269|PubMed:15689490, ECO:0000269|PubMed:17462998,
CC ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:20890297,
CC ECO:0000269|PubMed:21282656}.
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:15837192, ECO:0000269|PubMed:16905101,
CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:15837192, ECO:0000269|PubMed:16905101,
CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804};
CC -!- SUBUNIT: Interacts with RAB11FIP5 and STXBP6. Interacts with SGSM1,
CC SGSM2 and SGSM3 (By similarity). Interacts with EXOC6 in a GTP-
CC dependent manner (By similarity). Interacts with RAB11FIP1, RAB11FIP2,
CC RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5
CC and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A.
CC Interacts with RAB11FIP5 (By similarity). Interacts with STXBP6 (By
CC similarity). Interacts with VIPAS39. Interacts with MYO5B. Found in a
CC complex with MYO5B and CFTR. Interacts with NPC1L1. Interacts (GDP-
CC bound form) with ZFYVE27 (PubMed:21976701, PubMed:17082457). Interacts
CC with BIRC6/bruce. May interact with TBC1D14. Interacts with UNC119; in
CC a cell cycle-dependent manner. GDP-bound and nucleotide-free forms
CC interact with SH3BP5 (PubMed:26506309, PubMed:30217979). Interacts
CC (GDP-bound form) with KIF5A in a ZFYVE27-dependent manner
CC (PubMed:21976701). Interacts (GDP-bound form) with RELCH (By
CC similarity). Found in a complex composed of RELCH, OSBP1 and RAB11A (By
CC similarity). Interacts with TBC1D12 (PubMed:28384198). Interacts with
CC DEF6 (PubMed:31308374). {ECO:0000250, ECO:0000250|UniProtKB:P62492,
CC ECO:0000250|UniProtKB:P62494, ECO:0000269|PubMed:11495908,
CC ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:12470645,
CC ECO:0000269|PubMed:15173169, ECO:0000269|PubMed:15181150,
CC ECO:0000269|PubMed:15280022, ECO:0000269|PubMed:15601896,
CC ECO:0000269|PubMed:15837192, ECO:0000269|PubMed:16034420,
CC ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:16905101,
CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804,
CC ECO:0000269|PubMed:17082457, ECO:0000269|PubMed:17229837,
CC ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:18329369,
CC ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:20190753,
CC ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:21976701,
CC ECO:0000269|PubMed:22613832, ECO:0000269|PubMed:23535298,
CC ECO:0000269|PubMed:26506309, ECO:0000269|PubMed:28384198,
CC ECO:0000269|PubMed:30217979, ECO:0000269|PubMed:31308374}.
CC -!- INTERACTION:
CC P62491; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-745098, EBI-10254793;
CC P62491; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-745098, EBI-2118090;
CC P62491; O60447: EVI5; NbExp=6; IntAct=EBI-745098, EBI-852291;
CC P62491; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-745098, EBI-712105;
CC P62491; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-745098, EBI-2796400;
CC P62491; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-745098, EBI-14093244;
CC P62491; Q9UBF8-2: PI4KB; NbExp=5; IntAct=EBI-745098, EBI-16107849;
CC P62491; Q7L804: RAB11FIP2; NbExp=13; IntAct=EBI-745098, EBI-1049676;
CC P62491; O75154-1: RAB11FIP3; NbExp=16; IntAct=EBI-745098, EBI-15605207;
CC P62491; Q86YS3-1: RAB11FIP4; NbExp=2; IntAct=EBI-745098, EBI-15605259;
CC P62491; Q9BXF6: RAB11FIP5; NbExp=4; IntAct=EBI-745098, EBI-1387068;
CC P62491; Q96QF0-2: RAB3IP; NbExp=8; IntAct=EBI-745098, EBI-747865;
CC P62491; P46937: YAP1; NbExp=2; IntAct=EBI-745098, EBI-1044059;
CC P62491; Q5T4F4: ZFYVE27; NbExp=4; IntAct=EBI-745098, EBI-3892947;
CC P62491; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-745098, EBI-749023;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15304524};
CC Lipid-anchor {ECO:0000305|PubMed:24023390}. Recycling endosome membrane
CC {ECO:0000269|PubMed:11994279, ECO:0000269|PubMed:15181150,
CC ECO:0000269|PubMed:29514919}; Lipid-anchor
CC {ECO:0000305|PubMed:24023390}. Cleavage furrow
CC {ECO:0000269|PubMed:15601896}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:30217979}. Note=Translocates with RAB11FIP2 from
CC the vesicles of the endocytic recycling compartment (ERC) to the plasma
CC membrane (PubMed:11994279). Localizes to the cleavage furrow
CC (PubMed:15601896). Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL
CC and RAB8A in apical membrane initiation sites (AMIS) during the
CC generation of apical surface and lumenogenesis (PubMed:20890297).
CC Recruited to phagosomes containing S.aureus or M.tuberculosis
CC (PubMed:21255211). {ECO:0000269|PubMed:11994279,
CC ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:20890297,
CC ECO:0000269|PubMed:21255211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62491-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62491-2; Sequence=VSP_046755;
CC -!- PTM: (Microbial infection) Glycosylated on arginine residues by
CC S.typhimurium protein Ssek3. {ECO:0000269|PubMed:32974215}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X53143; CAA37300.1; -; mRNA.
DR EMBL; X56740; CAA40064.1; -; mRNA.
DR EMBL; AF000231; AAC32887.1; -; mRNA.
DR EMBL; AF498946; AAM21094.1; -; mRNA.
DR EMBL; CR407669; CAG28597.1; -; mRNA.
DR EMBL; CR536493; CAG38732.1; -; mRNA.
DR EMBL; BT020151; AAV38953.1; -; mRNA.
DR EMBL; BT020154; AAV38956.1; -; mRNA.
DR EMBL; AK300008; BAG61825.1; -; mRNA.
DR EMBL; AK311770; BAG34713.1; -; mRNA.
DR EMBL; AC011939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77752.1; -; Genomic_DNA.
DR EMBL; BC013348; AAH13348.1; -; mRNA.
DR CCDS; CCDS10212.1; -. [P62491-1]
DR CCDS; CCDS58373.1; -. [P62491-2]
DR PIR; S47169; S47169.
DR RefSeq; NP_001193765.1; NM_001206836.1. [P62491-2]
DR RefSeq; NP_004654.1; NM_004663.4. [P62491-1]
DR PDB; 1OIV; X-ray; 1.98 A; A/B=1-173.
DR PDB; 1OIW; X-ray; 2.05 A; A=1-173.
DR PDB; 1OIX; X-ray; 1.70 A; A=1-173.
DR PDB; 1YZK; X-ray; 2.00 A; A=8-175.
DR PDB; 2D7C; X-ray; 1.75 A; A/B=7-173.
DR PDB; 2GZD; X-ray; 2.44 A; A/B=2-173.
DR PDB; 2GZH; X-ray; 2.47 A; A=2-173.
DR PDB; 2HV8; X-ray; 1.86 A; A/B/C=6-175.
DR PDB; 4C4P; X-ray; 2.00 A; A=1-173.
DR PDB; 4D0L; X-ray; 2.94 A; B/D/F=1-216.
DR PDB; 4D0M; X-ray; 6.00 A; B/D/H/J/N/P/R/T/X/Z/d/h=1-216.
DR PDB; 4LWZ; X-ray; 2.55 A; A/C=1-177.
DR PDB; 4LX0; X-ray; 2.19 A; A/C=1-177.
DR PDB; 4UJ3; X-ray; 3.00 A; A/D/G/J/M/P/S/V=4-186.
DR PDB; 4UJ4; X-ray; 4.20 A; A/D/G/J=4-186.
DR PDB; 4UJ5; X-ray; 2.60 A; A/B=6-186.
DR PDB; 5C46; X-ray; 2.65 A; F=1-216.
DR PDB; 5C4G; X-ray; 3.20 A; B=1-216.
DR PDB; 5EUQ; X-ray; 3.20 A; B=1-216.
DR PDB; 5EZ5; X-ray; 2.40 A; A/B=8-175.
DR PDB; 5FBL; X-ray; 3.37 A; B=1-216.
DR PDB; 5FBQ; X-ray; 3.79 A; B=1-216.
DR PDB; 5FBR; X-ray; 3.28 A; B=1-216.
DR PDB; 5FBV; X-ray; 3.29 A; B=1-216.
DR PDB; 5FBW; X-ray; 3.49 A; B=1-216.
DR PDB; 5JCZ; X-ray; 2.06 A; A/D/I=1-177.
DR PDB; 6DJL; X-ray; 3.10 A; A/F/G/H=1-216.
DR PDB; 6IXV; X-ray; 3.80 A; E/F/G/H=1-173.
DR PDBsum; 1OIV; -.
DR PDBsum; 1OIW; -.
DR PDBsum; 1OIX; -.
DR PDBsum; 1YZK; -.
DR PDBsum; 2D7C; -.
DR PDBsum; 2GZD; -.
DR PDBsum; 2GZH; -.
DR PDBsum; 2HV8; -.
DR PDBsum; 4C4P; -.
DR PDBsum; 4D0L; -.
DR PDBsum; 4D0M; -.
DR PDBsum; 4LWZ; -.
DR PDBsum; 4LX0; -.
DR PDBsum; 4UJ3; -.
DR PDBsum; 4UJ4; -.
DR PDBsum; 4UJ5; -.
DR PDBsum; 5C46; -.
DR PDBsum; 5C4G; -.
DR PDBsum; 5EUQ; -.
DR PDBsum; 5EZ5; -.
DR PDBsum; 5FBL; -.
DR PDBsum; 5FBQ; -.
DR PDBsum; 5FBR; -.
DR PDBsum; 5FBV; -.
DR PDBsum; 5FBW; -.
DR PDBsum; 5JCZ; -.
DR PDBsum; 6DJL; -.
DR PDBsum; 6IXV; -.
DR AlphaFoldDB; P62491; -.
DR SMR; P62491; -.
DR BioGRID; 114299; 673.
DR CORUM; P62491; -.
DR DIP; DIP-29138N; -.
DR IntAct; P62491; 165.
DR MINT; P62491; -.
DR STRING; 9606.ENSP00000261890; -.
DR DrugBank; DB01864; 5'-Guanosine-Diphosphate-Monothiophosphate.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR GlyGen; P62491; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62491; -.
DR PhosphoSitePlus; P62491; -.
DR SwissPalm; P62491; -.
DR BioMuta; RAB11A; -.
DR DMDM; 50402542; -.
DR OGP; P62491; -.
DR EPD; P62491; -.
DR jPOST; P62491; -.
DR MassIVE; P62491; -.
DR MaxQB; P62491; -.
DR PaxDb; P62491; -.
DR PeptideAtlas; P62491; -.
DR PRIDE; P62491; -.
DR ProteomicsDB; 5063; -.
DR ProteomicsDB; 57402; -. [P62491-1]
DR TopDownProteomics; P62491-1; -. [P62491-1]
DR Antibodypedia; 4588; 502 antibodies from 39 providers.
DR DNASU; 8766; -.
DR Ensembl; ENST00000261890.7; ENSP00000261890.2; ENSG00000103769.10. [P62491-1]
DR Ensembl; ENST00000569896.1; ENSP00000456420.1; ENSG00000103769.10. [P62491-2]
DR GeneID; 8766; -.
DR KEGG; hsa:8766; -.
DR MANE-Select; ENST00000261890.7; ENSP00000261890.2; NM_004663.5; NP_004654.1.
DR UCSC; uc002apk.4; human. [P62491-1]
DR CTD; 8766; -.
DR DisGeNET; 8766; -.
DR GeneCards; RAB11A; -.
DR HGNC; HGNC:9760; RAB11A.
DR HPA; ENSG00000103769; Low tissue specificity.
DR MalaCards; RAB11A; -.
DR MIM; 605570; gene.
DR neXtProt; NX_P62491; -.
DR OpenTargets; ENSG00000103769; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA34101; -.
DR VEuPathDB; HostDB:ENSG00000103769; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000154914; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P62491; -.
DR OMA; SMKEDYY; -.
DR PhylomeDB; P62491; -.
DR TreeFam; TF300099; -.
DR PathwayCommons; P62491; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; P62491; -.
DR SIGNOR; P62491; -.
DR BioGRID-ORCS; 8766; 90 hits in 1082 CRISPR screens.
DR ChiTaRS; RAB11A; human.
DR EvolutionaryTrace; P62491; -.
DR GeneWiki; RAB11A; -.
DR GenomeRNAi; 8766; -.
DR Pharos; P62491; Tbio.
DR PRO; PR:P62491; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P62491; protein.
DR Bgee; ENSG00000103769; Expressed in esophagus squamous epithelium and 206 other tissues.
DR ExpressionAtlas; P62491; baseline and differential.
DR Genevisible; P62491; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0030133; C:transport vesicle; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; NAS:UniProtKB.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IGI:ARUK-UCL.
DR GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IMP:UniProtKB.
DR GO; GO:0051650; P:establishment of vesicle localization; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:1990182; P:exosomal secretion; IMP:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0048227; P:plasma membrane to endosome transport; NAS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0010796; P:regulation of multivesicular body size; IMP:UniProtKB.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell membrane;
KW Cytoplasmic vesicle; Direct protein sequencing; Endosome; Glycoprotein;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.11"
FT CHAIN 2..213
FT /note="Ras-related protein Rab-11A"
FT /id="PRO_0000121151"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370807"
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:0000269|PubMed:16905101,
FT ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804,
FT ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD,
FT ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8,
FT ECO:0007744|PDB:5EZ5"
FT BINDING 37..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD,
FT ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8,
FT ECO:0007744|PDB:5EZ5"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16905101,
FT ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804,
FT ECO:0007744|PDB:1OIW, ECO:0007744|PDB:4D0L,
FT ECO:0007744|PDB:4D0M, ECO:0007744|PDB:5C46,
FT ECO:0007744|PDB:5FBL"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16905101,
FT ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804,
FT ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD,
FT ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8,
FT ECO:0007744|PDB:5EZ5"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16905101,
FT ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804,
FT ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD,
FT ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8,
FT ECO:0007744|PDB:5EZ5"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|Ref.11"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:24023390"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:24023390"
FT CARBOHYD 4
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:32974215"
FT VAR_SEQ 147..216
FT /note="GLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPI
FT HVPPTTENKPKVQCCQNI -> EANVRQTRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046755"
FT MUTAGEN 13
FT /note="K->N: Abolishes SH3BP5-mediated guanine nucleotide
FT exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 22
FT /note="V->M: Impairs protein folding."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 24
FT /note="K->R: Impairs protein folding and decreases affinity
FT for guanine nucleotides."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 25
FT /note="S->N: Dominant-negative mutant. Induces increased
FT number of binucleated cells, indicating defects in
FT cytokinesis. Inhibits the transport of NPC1L1 to the plama
FT membrane. Disrupts the trafficking of CDH1 to the plasma
FT membrane and promotes accumulation of CDH1 in RAB11A
FT endosomes in nonpolarized cells. Promotes mistargeting of
FT CDH1 to the apical membrane in polarized cells."
FT /evidence="ECO:0000269|PubMed:15601896,
FT ECO:0000269|PubMed:15689490, ECO:0000269|PubMed:19542231,
FT ECO:0000269|PubMed:30217979"
FT MUTAGEN 36
FT /note="F->A: Nearly abolishes SH3BP5-mediated guanine
FT nucleotide exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 38
FT /note="L->P: Decreases SH3BP5-mediated guanine nucleotide
FT exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 38
FT /note="L->P: Nearly abolishes SH3BP5-mediated guanine
FT nucleotide exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 40
FT /note="S->F: Nearly abolishes SH3BP5-mediated guanine
FT nucleotide exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 41
FT /note="K->A: Mildly decreases SH3BP5-mediated guanine
FT nucleotide exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 41
FT /note="K->P: Abolishes SH3BP5-mediated guanine nucleotide
FT exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 44
FT /note="I->A: Abolishes SH3BP5-mediated guanine nucleotide
FT exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 70
FT /note="Q->L: Constitutively active mutant. Decreases GTPase
FT activity. Disrupts the trafficking of CDH1 to the plasma
FT membrane and promotes accumulation of CDH1 in RAB11A
FT endosomes in nonpolarized cells. Promotes mistargeting of
FT CDH1 to the apical membrane in polarized cells."
FT /evidence="ECO:0000269|PubMed:15689490,
FT ECO:0000269|PubMed:15837192, ECO:0000269|PubMed:16905101,
FT ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804,
FT ECO:0000269|PubMed:30217979"
FT MUTAGEN 82
FT /note="R->C: Decreases SH3BP5-mediated guanine nucleotide
FT exchange."
FT /evidence="ECO:0000269|PubMed:30217979"
FT MUTAGEN 154
FT /note="S->L: Impairs protein folding."
FT /evidence="ECO:0000269|PubMed:30217979"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:6DJL"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:1OIX"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6DJL"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:6DJL"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:1OIX"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:1OIX"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1OIX"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1OIX"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:1OIX"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1OIX"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1OIX"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:1OIX"
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
