Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras-related protein Rab-11A

Gene

Rab11a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. microtubule binding Source: MGI
  4. myosin V binding Source: MGI

GO - Biological processi

  1. astral microtubule organization Source: MGI
  2. cytokinesis Source: Ensembl
  3. establishment of protein localization to membrane Source: MGI
  4. establishment of protein localization to organelle Source: MGI
  5. establishment of vesicle localization Source: MGI
  6. exocytosis Source: GO_Central
  7. exosomal secretion Source: MGI
  8. intracellular protein transport Source: GO_Central
  9. melanosome transport Source: UniProtKB
  10. metabolic process Source: MGI
  11. mitotic metaphase plate congression Source: MGI
  12. mitotic spindle assembly Source: MGI
  13. multivesicular body assembly Source: MGI
  14. neuron projection development Source: UniProtKB
  15. positive regulation of axon extension Source: MGI
  16. positive regulation of epithelial cell migration Source: MGI
  17. positive regulation of G2/M transition of mitotic cell cycle Source: MGI
  18. protein localization to plasma membrane Source: UniProtKB
  19. Rab protein signal transduction Source: GO_Central
  20. regulation of long-term neuronal synaptic plasticity Source: Ensembl
  21. regulation of multivesicular body size Source: MGI
  22. regulation of protein transport Source: Ensembl
  23. regulation of vesicle-mediated transport Source: MGI
  24. vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_315493. VxPx cargo-targeting to cilium.
REACT_328862. Anchoring of the basal body to the plasma membrane.

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 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1858202. Rab11a.

Subcellular locationi

  1. Cell membrane By similarity; Peripheral membrane protein By similarity
  2. Recycling endosome membrane By similarity; Peripheral membrane protein By similarity
  3. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity

  4. 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. cytoplasmic vesicle Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. Golgi apparatus Source: MGI
  7. membrane Source: MGI
  8. mitochondrion Source: MGI
  9. multivesicular body Source: MGI
  10. perinuclear region of cytoplasm Source: MGI
  11. phagocytic vesicle Source: UniProtKB
  12. phagocytic vesicle membrane Source: UniProtKB-SubCell
  13. plasma membrane Source: UniProtKB-SubCell
  14. protein complex Source: MGI
  15. recycling endosome Source: UniProtKB
  16. recycling endosome membrane Source: UniProtKB-SubCell
  17. spindle pole Source: MGI
  18. trans-Golgi network Source: MGI
  19. transport vesicle Source: Ensembl
  20. vesicle Source: MGI
Complete GO annotation...

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

MaxQBiP62492.
PaxDbiP62492.
PRIDEiP62492.

PTM databases

PhosphoSiteiP62492.

Expressioni

Gene expression databases

BgeeiP62492.
CleanExiMM_RAB11A.
ExpressionAtlasiP62492. baseline and differential.
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

« Hide

        10         20         30         40         50
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT
60 70 80 90 100
RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE
110 120 130 140 150
NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF
160 170 180 190 200
IETSALDSTN VEAAFQTILT EIYRIVSQKQ MSDRRENDMS PSNNVVPIHV
210
PPTTENKPKV QCCQNI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP62492. 15 interactions.
MINTiMINT-4131841.

PTM databases

PhosphoSiteiP62492.

Proteomic databases

MaxQBiP62492.
PaxDbiP62492.
PRIDEiP62492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8766.
MGIiMGI:1858202. Rab11a.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_315493. VxPx cargo-targeting to cilium.
REACT_328862. Anchoring of the basal body to the plasma membrane.

Miscellaneous databases

NextBioi310717.
PROiP62492.
SOURCEiSearch...

Gene expression databases

BgeeiP62492.
CleanExiMM_RAB11A.
ExpressionAtlasiP62492. baseline and differential.
GenevestigatoriP62492.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.