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P62492 (RB11A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-11A

Short name=Rab-11
Gene names
Name:Rab11a
Synonyms:Rab11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Subunit structure

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. Ref.5 Ref.6 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Recycling endosome membrane; Peripheral membrane protein By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; 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.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processCell cycle
Protein transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Endosome
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis

Inferred from electronic annotation. Source: Ensembl

melanosome transport

Inferred from mutant phenotype Ref.9. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of axon extension

Inferred from mutant phenotype PubMed 22573681. Source: MGI

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of protein transport

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 22573681. Source: MGI

cleavage furrow

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 18656450. Source: MGI

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

perinuclear region of cytoplasm

Inferred from direct assay PubMed 22573681. Source: MGI

phagocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

recycling endosome

Inferred from direct assay Ref.9. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from sequence orthology PubMed 15229288. Source: MGI

transport vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Vps33bP590163EBI-770256,EBI-2656383

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 213212Ras-related protein Rab-11A
PRO_0000121152
Propeptide214 – 2163Removed in mature form Potential
PRO_0000370808

Regions

Nucleotide binding18 – 269GTP By similarity
Nucleotide binding66 – 705GTP By similarity
Nucleotide binding124 – 1274GTP By similarity
Nucleotide binding154 – 1563GTP By similarity
Motif40 – 489Effector region By similarity

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue2131Cysteine methyl ester Potential
Lipidation2121S-geranylgeranyl cysteine By similarity
Lipidation2131S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict1801Q → H in AAF36458. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P62492 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 76FC1E113A29B269

FASTA21624,394
        10         20         30         40         50         60 
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI 

        70         80         90        100        110        120 
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM 

       130        140        150        160        170        180 
LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ 

       190        200        210 
MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI 

« Hide

References

« Hide 'large scale' references
[1]"Genomic structure of murine rab11 family members."
Bhartur S.G., Calhoun B.C., Woodrum J., Kurkjian J., Iyer S., Lai F., Goldenring J.R.
Biochem. Biophys. Res. Commun. 269:611-617(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization."
Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z. expand/collapse author list , Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.
Nat. Genet. 42:303-312(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23282.1.
RefSeqNP_059078.2. NM_017382.5.
UniGeneMm.1387.

3D structure databases

ProteinModelPortalP62492.
SMRP62492. Positions 6-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62492. 14 interactions.
MINTMINT-4131841.

PTM databases

PhosphoSiteP62492.

Proteomic databases

PaxDbP62492.
PRIDEP62492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000172298; ENSMUSP00000129163; ENSMUSG00000004771.
GeneID53869.
KEGGmmu:53869.
UCSCuc009qce.1. mouse.

Organism-specific databases

CTD8766.
MGIMGI:1858202. Rab11a.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP62492.
KOK07904.
OMAAMGTRDD.
OrthoDBEOG7SFHZ2.
PhylomeDBP62492.
TreeFamTF300099.

Gene expression databases

ArrayExpressP62492.
BgeeP62492.
CleanExMM_RAB11A.
GenevestigatorP62492.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio310717.
PROP62492.
SOURCESearch...

Entry information

Entry nameRB11A_MOUSE
AccessionPrimary (citable) accession number: P62492
Secondary accession number(s): P24410, Q3V1Z6, Q9JLX1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot