RBCC

Full text data of RAB11A

RAB11A (RAB11) [Confidence: low (only semi-automatic identification from reviews)]
Ras-related protein Rab-11A; Rab-11 (YL8; Flags: Precursor)

UniProt P62491
ID RB11A_HUMAN Reviewed; 216 AA.
AC P62491; B2R4B6; B4DT13; P24410; Q5TZN9; Q9JLX1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Ras-related protein Rab-11A;
DE Short=Rab-11;
DE AltName: Full=YL8;
DE Flags: Precursor;
GN Name=RAB11A; Synonyms=RAB11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA 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
RT sequenced by 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS 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.,
RA Kumar R., 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
RT 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
RT 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
RT protein (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
RT target 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.,
RA Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control
RT membrane traffic in cytokinesis.";
RL EMBO J. 24:3389-3399(2005).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11FIP3 AND
RP RAB11FIP4, 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.,
RA Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.;
RT "The FIP3-Rab11 protein complex regulates recycling endosome targeting
RT to 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
RT 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
RT transmembrane conductance regulator in Rab11a-specific apical
RT recycling endosomes in 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
RT Evi5 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
RT by 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.,
RA Matthews R.P., Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H.,
RA Knisely A.S., 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
RT 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.,
RA Buerckstuemmer T., 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 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.,
RA 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 [32]
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
RT recruited to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [33]
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-
RT positive recycling endosomes.";
RL J. Cell Biol. 197:659-675(2012).
RN [34]
RP ISOPRENYLATION AT CYS-212 AND CYS-213, AND MASS 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
RT proteins, mitochondria, and senescence.";
RL Mol. Cell. Proteomics 0:0-0(2013).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-175 IN COMPLEX WITH GTP
RP 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-
RT 5.";
RL Nature 436:415-419(2005).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP
RP ANALOG AND GDP, 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
RT small GTP binding protein.";
RL Structure 13:533-540(2005).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 6-175 IN COMPLEX WITH GTP
RP AND RAB11FIP3, 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 [38]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 7-173 IN COMPLEX WITH GTP,
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4, AND 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
RT of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-173 IN COMPLEX WITH GTP,
RP 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.,
RA Khan A.R.;
RT "Crystal structure of rab11 in complex with rab11 family interacting
RT protein 2.";
RL Structure 14:1273-1283(2006).
CC -!- FUNCTION: The small GTPases Rab are key regulators of
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different set of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab regulates endocytic recycling. Acts
CC 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,
CC PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of
CC PODXL to the apical membrane initiation sites (AMIS), apical
CC 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
CC complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to
CC the plasma membrane. Participates in the sorting and basolateral
CC transport of CDH1 from the Golgi apparatus to the plasma membrane.
CC Regulates the recycling of FCGRT (receptor of Fc region of
CC monomeric Ig G) to basolateral membranes. May also play a role in
CC melanosome transport and release from melanocytes.
CC -!- SUBUNIT: Interacts with RIP11 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,
CC RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts
CC with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and
CC compete for binding RAB11A. Interacts with VIPAS39. Interacts with
CC MYO5B. Found in a complex with MYO5B and CFTR. Interacts with
CC NPC1L1. Interacts (GDP-bound form) with ZFYVE27. Interacts with
CC BIRC6/bruce. May interact with TBC1D14.
CC -!- INTERACTION:
CC Q7L804:RAB11FIP2; NbExp=2; IntAct=EBI-745098, EBI-1049676;
CC Q5T4F4:ZFYVE27; NbExp=4; IntAct=EBI-745098, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Recycling endosome membrane; Peripheral membrane protein. Cleavage
CC furrow. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle,
CC phagosome membrane; Lipid-anchor; Cytoplasmic side (By
CC similarity). Note=Translocates with RAB11FIP2 from the vesicles of
CC the endocytic recycling compartment (ERC) to the plasma membrane.
CC Localizes to the cleavage furrow. Colocalizes with PARD3, PRKCI,
CC EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites
CC (AMIS) during the generation of apical surface and lumenogenesis.
CC Recruited to phagosomes containing S.aureus or M.tuberculosis.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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 PIR; S47169; S47169.
DR RefSeq; NP_001193765.1; NM_001206836.1.
DR RefSeq; NP_004654.1; NM_004663.4.
DR UniGene; Hs.321541; -.
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=2-172.
DR PDB; 2GZH; X-ray; 2.47 A; A=2-172.
DR PDB; 2HV8; X-ray; 1.86 A; A/B/C=6-174.
DR PDB; 4C4P; X-ray; 2.00 A; A=1-173.
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 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; 4LWZ; -.
DR PDBsum; 4LX0; -.
DR ProteinModelPortal; P62491; -.
DR SMR; P62491; 6-173.
DR DIP; DIP-29138N; -.
DR IntAct; P62491; 20.
DR MINT; MINT-1434585; -.
DR STRING; 9606.ENSP00000261890; -.
DR PhosphoSite; P62491; -.
DR DMDM; 50402542; -.
DR OGP; P62491; -.
DR PaxDb; P62491; -.
DR PRIDE; P62491; -.
DR DNASU; 8766; -.
DR Ensembl; ENST00000261890; ENSP00000261890; ENSG00000103769.
DR Ensembl; ENST00000569896; ENSP00000456420; ENSG00000103769.
DR GeneID; 8766; -.
DR KEGG; hsa:8766; -.
DR UCSC; uc010ujk.2; human.
DR CTD; 8766; -.
DR GeneCards; GC15P066018; -.
DR HGNC; HGNC:9760; RAB11A.
DR HPA; CAB013097; -.
DR MIM; 605570; gene.
DR neXtProt; NX_P62491; -.
DR PharmGKB; PA34101; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P62491; -.
DR KO; K07904; -.
DR OMA; AMGTRDD; -.
DR PhylomeDB; P62491; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR SignaLink; P62491; -.
DR EvolutionaryTrace; P62491; -.
DR GeneWiki; RAB11A; -.
DR GenomeRNAi; 8766; -.
DR NextBio; 32876; -.
DR PRO; PR:P62491; -.
DR ArrayExpress; P62491; -.
DR Bgee; P62491; -.
DR CleanEx; HS_RAB11A; -.
DR Genevestigator; P62491; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; NAS:UniProtKB.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0048227; P:plasma membrane to endosome transport; NAS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0051223; P:regulation of protein transport; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0006833; P:water transport; TAS:Reactome.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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;
KW Cell membrane; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 213 Ras-related protein Rab-11A.
FT /FTId=PRO_0000121151.
FT PROPEP 214 216 Removed in mature form (Potential).
FT /FTId=PRO_0000370807.
FT NP_BIND 18 26 GTP.
FT NP_BIND 66 70 GTP.
FT NP_BIND 124 127 GTP.
FT NP_BIND 154 156 GTP.
FT MOTIF 40 48 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylglycine.
FT MOD_RES 213 213 Cysteine methyl ester (Potential).
FT LIPID 212 212 S-geranylgeranyl cysteine.
FT LIPID 213 213 S-geranylgeranyl cysteine.
FT VAR_SEQ 147 216 GLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRREN
FT DMSPSNNVVPIHVPPTTENKPKVQCCQNI -> EANVRQTR
FT K (in isoform 2).
FT /FTId=VSP_046755.
FT MUTAGEN 25 25 S->N: Dominant-negative mutant. Induces
FT increased number of binucleated cells,
FT indicating defects in cytokinesis.
FT Inhibits the transport of NPC1L1 to the
FT plama membrane. Disrupts the trafficking
FT of CDH1 to the plasma membrane and
FT promotes accumulation of CDH1 in RAB11A
FT endosomes in nonpolarized cells. Promotes
FT mistargeting of CDH1 to the apical
FT membrane in polarized cells.
FT MUTAGEN 70 70 Q->L: Constitutively active mutant.
FT Decreases GTPase activity. Disrupts the
FT trafficking of CDH1 to the plasma
FT membrane and promotes accumulation of
FT CDH1 in RAB11A endosomes in nonpolarized
FT cells. Promotes mistargeting of CDH1 to
FT the apical membrane in polarized cells.
FT STRAND 9 18
FT HELIX 24 33
FT STRAND 45 55
FT STRAND 58 67
FT STRAND 72 74
FT HELIX 78 81
FT STRAND 86 92
FT HELIX 96 100
FT HELIX 102 112
FT STRAND 118 124
FT HELIX 126 131
FT HELIX 136 145
FT STRAND 149 152
FT TURN 155 157
FT HELIX 161 172
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
//

MIM 605570
*RECORD*
*FIELD* NO
605570
*FIELD* TI
*605570 RAS-ASSOCIATED PROTEIN RAB11A; RAB11A
*FIELD* TX

DESCRIPTION

Small GTP-binding proteins of the RAB family, such as RAB11A, play
read moreessential roles in vesicle and granule targeting (Bao et al., 2002).

CLONING

Using PCR to amplify Ras and Ras-like sequences from carcinoma and
T-cell cDNA libraries, Drivas et al. (1991) obtained a cDNA encoding
RAB11A, which they termed YL8. RAB11A shares 69% homology with yeast
Ypt3. The deduced 651-amino acid protein has many conserved features of
Ras and Rab proteins, except that its C terminus lacks the cys-cys found
in other Rab family members. Northern blot analysis detected expression
in 4 tumor cell lines.

By screening lambda libraries for small GTP-binding proteins, Gromov et
al. (1998) identified 2 cDNAs, arising from alternative splicing, that
encode RAB11A. Northern blot analysis revealed ubiquitous expression of
1.0- and 2.3-kb RAB11A transcripts, with highest levels in heart and
lowest levels in liver. The larger transcript was more abundant in brain
and lung, whereas the smaller transcript was more abundant in placenta
and heart.

Using RT-PCR, Bao et al. (2002) cloned RAB11A from human platelets.
Western blot analysis detected RAB11A at an apparent molecular mass of
26 kD in human platelets and leukemia cell lines. Western blot analysis
of rat tissues detected high Rab11a expression in platelets and much
lower expression in kidney, liver, heart, lung, and brain. Differential
centrifugation of human platelets showed enrichment of RAB11A in the
granule/mitochondrion and membrane fractions, with a small amount in the
cytosolic fraction.

GENE FUNCTION

Bao et al. (2002) noted that mutation of a conserved glutamine (Q70) to
leucine within the GTP-binding motif of RAB11A does not inhibit its
GTPase activity (Casanova et al., 1999), in contrast to the effect of
similar mutations in most small GTPases. Bao et al. (2002) found that
mutation of the conserved glutamines in RAB31 (605694) and RAB32
(612906) also had no effect on their GTPase activities, suggesting that
these proteins form a subfamily of small GTPases.

Shirane and Nakayama (2006) identified protrudin (ZFYVE27; 610243) as a
mammalian protein that promoted neurite formation through interaction
with the guanosine diphosphate (GDP)-bound form of Rab11.
Phosphorylation of protrudin by extracellular signal-regulated kinase
(ERK; 600997) in response to nerve growth factor (NGFB; 162030) promoted
protrudin association with Rab11-GDP. Downregulation of protrudin by RNA
interference induced membrane extension in all directions and inhibited
neurite formation. Thus, Shirane and Nakayama (2006) concluded that
protrudin regulates Rab11-dependent membrane recycling to promote the
directional membrane trafficking required for neurite formation.

In muscle and fat cells, insulin (INS; 176730) stimulation activates a
signaling cascade that causes intracellular vesicles containing glucose
transporter-4 (GLUT4, or SLC2A4; 138190) to translocate to and fuse with
the plasma membrane. Using mass spectrometry, Larance et al. (2005)
identified Rab10 (612672), Rab11, and Rab14 (612673) on Glut4 vesicles
from cultured mouse adipocytes. These vesicles also contained the RAB
GTPase-activating protein As160 (TBC1D4; 612465), suggesting that the
RAB proteins may be AS160 substrates.

In lethal systemic anthrax, proliferating bacilli secrete large
quantities of the toxins lethal factor (LF) and edema factor (EF),
leading to widespread vascular leakage and shock. Host targets of LF
(mitogen-activated protein-kinase kinases) and EF (cAMP-dependent
processes) have been implicated in the initial phase of anthrax. In an
investigation of toxin action during the final stage of infection,
Guichard et al. (2010) used Drosophila melanogaster to identify the
Rab11/Sec15 (609672) exocyst, which acts at the last step of endocytic
recycling, as a novel target of both EF and LF. EF reduces levels of
apically localized Rab11 and indirectly blocks vesicle formation by its
binding partner and effector Sec15 (Sec15-GFP), whereas LF acts more
directly to reduce Sec15-GFP vesicles. Convergent effects of EF and LF
on Rab11/Sec15 inhibited expression of and signaling by the Notch ligand
Delta and reduced DE-cadherin levels at adherens junctions. In human
endothelial cells, the 2 toxins acted in a conserved fashion to block
formation of Sec15 vesicles, inhibit Notch signaling through Delta
(DLL4; 605185), and reduce cadherin (CDH1; 192090) expression at
adherens junctions. Guichard et al. (2010) suggested that this
coordinated disruption of the Rab11/Sec15 exocyst by anthrax toxins may
contribute to toxin-dependent barrier disruption and vascular
dysfunction during Bacillus anthracis infection.

MAPPING

By radiation hybrid analysis and FISH, Gromov et al. (1998) mapped the
RAB11A gene to 15q21.3-q22.31.

*FIELD* RF
1. Bao, X.; Faris, A. E.; Jang, E. K.; Haslam, R. J.: Molecular cloning,
bacterial expression and properties of Rab31 and Rab32: new blood
platelet Rab proteins. Europ. J. Biochem. 269: 259-271, 2002.

2. Casanova, J. E.; Wang, X.; Kumar, R.; Bhartur, S. G.; Navarre,
J.; Woodrum, J. E.; Altschuler, Y.; Ray, G. S.; Goldenring, J. R.
: Association of Rab25 and Rab11a with the apical recycling system
of polarized Madin-Darby canine kidney cells. Molec. Biol. Cell 10:
47-61, 1999.

3. Drivas, G. T.; Shih, A.; Coutavas, E. E.; D'Eustachio, P.; Rush,
M. G.: Identification and characterization of a human homolog of
the Schizosaccharomyces pombe ras-like gene YPT-3. Oncogene 6: 3-9,
1991.

4. Gromov, P. S.; Celis, J. E.; Hansen, C.; Tommerup, N.; Gromova,
I.; Madsen, P.: Human rab11a: transcription, chromosome mapping
and effect on the expression levels of host GTP-binding proteins. FEBS
Lett. 429: 359-364, 1998.

5. Guichard, A.; McGillivray, S. M.; Cruz-Moreno, B.; van Sorge, N.
M.; Nizet, V.; Bier, E.: Anthrax toxins cooperatively inhibit endocytic
recycling by the Rab11/Sec15 exocyst. Nature 467: 854-858, 2010.

6. Larance, M.; Ramm, G.; Stockli, J.; van Dam, E. M.; Winata, S.;
Wasinger, V.; Simpson, F.; Graham, M.; Junutula, J. R.; Guilhaus,
M.; James, D. E.: Characterization of the role of the Rab GTPase-activating
protein AS160 in insulin-regulated GLUT4 trafficking. J. Biol. Chem. 280:
37803-37813, 2005.

7. Shirane, M.; Nakayama, K. I.: Protrudin induces neurite formation
by directional membrane trafficking. Science 314: 818-821, 2006.

*FIELD* CN
Ada Hamosh - updated: 11/11/2010
Patricia A. Hartz - updated: 7/2/2009
Patricia A. Hartz - updated: 2/27/2009
Ada Hamosh - updated: 11/28/2006

*FIELD* CD
Paul J. Converse: 1/22/2001

*FIELD* ED
alopez: 11/15/2010
terry: 11/11/2010
mgross: 7/10/2009
terry: 7/2/2009
mgross: 3/18/2009
terry: 2/27/2009
alopez: 12/6/2006
terry: 11/28/2006
carol: 3/14/2006
cwells: 11/7/2003
mgross: 1/22/2001

RBCC Red Blood Cell Collection

Full text data of RAB11A