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P62492

- RB11A_MOUSE

UniProt

P62492 - RB11A_MOUSE

Protein

Ras-related protein Rab-11A

Gene

Rab11a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes By similarity. May also play a role in melanosome transport and release from melanocytes.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269GTPBy similarity
    Nucleotide bindingi66 – 705GTPBy similarity
    Nucleotide bindingi124 – 1274GTPBy similarity
    Nucleotide bindingi154 – 1563GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cytokinesis Source: Ensembl
    2. melanosome transport Source: UniProtKB
    3. neuron projection development Source: UniProtKB
    4. positive regulation of axon extension Source: MGI
    5. protein localization to plasma membrane Source: UniProtKB
    6. protein transport Source: UniProtKB-KW
    7. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    8. regulation of protein transport Source: Ensembl
    9. small GTPase mediated signal transduction Source: InterPro
    10. vesicle-mediated transport Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_213947. Regulation of water balance by renal Aquaporins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-11A
    Short name:
    Rab-11
    Gene namesi
    Name:Rab11a
    Synonyms:Rab11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1858202. Rab11a.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Recycling endosome membrane By similarity; Peripheral membrane protein By similarity. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
    Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis By similarity. Recruited to phagosomes containing S.aureus or Mycobacterium By similarity.By similarity

    GO - Cellular componenti

    1. axon Source: MGI
    2. cleavage furrow Source: UniProtKB
    3. cytoplasm Source: MGI
    4. mitochondrion Source: MGI
    5. perinuclear region of cytoplasm Source: MGI
    6. phagocytic vesicle Source: UniProtKB
    7. phagocytic vesicle membrane Source: UniProtKB-SubCell
    8. plasma membrane Source: UniProtKB-SubCell
    9. protein complex Source: Ensembl
    10. recycling endosome Source: UniProtKB
    11. recycling endosome membrane Source: UniProtKB-SubCell
    12. trans-Golgi network Source: MGI
    13. transport vesicle Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 213212Ras-related protein Rab-11APRO_0000121152Add
    BLAST
    Propeptidei214 – 2163Removed in mature formSequence AnalysisPRO_0000370808

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycineBy similarity
    Lipidationi212 – 2121S-geranylgeranyl cysteineBy similarity
    Modified residuei213 – 2131Cysteine methyl esterSequence Analysis
    Lipidationi213 – 2131S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    PaxDbiP62492.
    PRIDEiP62492.

    PTM databases

    PhosphoSiteiP62492.

    Expressioni

    Gene expression databases

    ArrayExpressiP62492.
    BgeeiP62492.
    CleanExiMM_RAB11A.
    GenevestigatoriP62492.

    Interactioni

    Subunit structurei

    Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A. Interacts with RIP11 and STXBP6. Interacts (GDP-bound form) with ZFYVE27 By similarity. Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39. Interacts with EXOC6 in a GTP-dependent manner. Interacts with BIRC6/bruce By similarity. May interact with TBC1D14 By similarity. Interacts with UNC119; in a cell cycle-dependent manner By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rab3ipQ627394EBI-770256,EBI-2028671From a different organism.
    Vps33bP590163EBI-770256,EBI-2656383

    Protein-protein interaction databases

    IntActiP62492. 15 interactions.
    MINTiMINT-4131841.

    Structurei

    3D structure databases

    ProteinModelPortaliP62492.
    SMRiP62492. Positions 6-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi40 – 489Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiP62492.
    KOiK07904.
    OMAiAMGTRDD.
    OrthoDBiEOG7SFHZ2.
    PhylomeDBiP62492.
    TreeFamiTF300099.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00175. RAB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51419. RAB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P62492-1 [UniParc]FASTAAdd to Basket

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    MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT    50
    RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE 100
    NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF 150
    IETSALDSTN VEAAFQTILT EIYRIVSQKQ MSDRRENDMS PSNNVVPIHV 200
    PPTTENKPKV QCCQNI 216
    Length:216
    Mass (Da):24,394
    Last modified:January 23, 2007 - v3
    Checksum:i76FC1E113A29B269
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801Q → H in AAF36458. (PubMed:10708602)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127669 Genomic DNA. Translation: AAF36458.1.
    AK014268 mRNA. Translation: BAB29233.1.
    AK132072 mRNA. Translation: BAE20971.1.
    AK132159 mRNA. Translation: BAE21003.1.
    AK147122 mRNA. Translation: BAE27693.1.
    BC010722 mRNA. Translation: AAH10722.1.
    CCDSiCCDS23282.1.
    RefSeqiNP_059078.2. NM_017382.5.
    UniGeneiMm.1387.

    Genome annotation databases

    EnsembliENSMUST00000172298; ENSMUSP00000129163; ENSMUSG00000004771.
    GeneIDi53869.
    KEGGimmu:53869.
    UCSCiuc009qce.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127669 Genomic DNA. Translation: AAF36458.1 .
    AK014268 mRNA. Translation: BAB29233.1 .
    AK132072 mRNA. Translation: BAE20971.1 .
    AK132159 mRNA. Translation: BAE21003.1 .
    AK147122 mRNA. Translation: BAE27693.1 .
    BC010722 mRNA. Translation: AAH10722.1 .
    CCDSi CCDS23282.1.
    RefSeqi NP_059078.2. NM_017382.5.
    UniGenei Mm.1387.

    3D structure databases

    ProteinModelPortali P62492.
    SMRi P62492. Positions 6-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P62492. 15 interactions.
    MINTi MINT-4131841.

    PTM databases

    PhosphoSitei P62492.

    Proteomic databases

    PaxDbi P62492.
    PRIDEi P62492.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000172298 ; ENSMUSP00000129163 ; ENSMUSG00000004771 .
    GeneIDi 53869.
    KEGGi mmu:53869.
    UCSCi uc009qce.1. mouse.

    Organism-specific databases

    CTDi 8766.
    MGIi MGI:1858202. Rab11a.

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P62492.
    KOi K07904.
    OMAi AMGTRDD.
    OrthoDBi EOG7SFHZ2.
    PhylomeDBi P62492.
    TreeFami TF300099.

    Enzyme and pathway databases

    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_213947. Regulation of water balance by renal Aquaporins.

    Miscellaneous databases

    NextBioi 310717.
    PROi P62492.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62492.
    Bgeei P62492.
    CleanExi MM_RAB11A.
    Genevestigatori P62492.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion and Head.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
    4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 14-24; 42-51 AND 83-95, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "Sec15 is an effector for the Rab11 GTPase in mammalian cells."
      Zhang X.-M., Ellis S., Sriratana A., Mitchell C.A., Rowe T.
      J. Biol. Chem. 279:43027-43034(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EXOC6.
    6. "Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
      Yang H., Sasaki T., Minoshima S., Shimizu N.
      Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
    7. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: INTERACTION WITH VIPAS39.
    9. "The recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome trafficking."
      Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N., Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T., Sturm R.A., Stow J.L.
      Traffic 12:627-643(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MELANOSOME TRANSPORT.

    Entry informationi

    Entry nameiRB11A_MOUSE
    AccessioniPrimary (citable) accession number: P62492
    Secondary accession number(s): P24410, Q3V1Z6, Q9JLX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3