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P46638 (RB11B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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-11B
Gene names
Name:Rab11b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length218 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 plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis. Ref.4 Ref.5 Ref.6 Ref.7

Subunit structure

Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4 By similarity. May interact with TBC1D14 By similarity. Interacts with ATP6V1E1 By similarity. Interacts with KCNMA1. Ref.8

Subcellular location

Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Probable. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus By similarity. Ref.4

Tissue specificity

Abundantly expressed in brain, heart and testis. Also detected in kidney and pancreatic islets. Ref.5

Post-translational modification

Citrullinated by PADI4.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cytoplasmic vesicle
Endosome
Membrane
Synapse
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Citrullination
Lipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to acidity

Inferred from sequence or structural similarity. Source: UniProtKB

constitutive secretory pathway

Inferred from sequence or structural similarity. Source: UniProtKB

insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype Ref.5. Source: UniProtKB

melanosome transport

Inferred from mutant phenotype Ref.6. Source: UniProtKB

receptor recycling

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulated secretory pathway

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of anion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endocytic recycling

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of protein localization to cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde transport, endosome to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

transferrin transport

Inferred from mutant phenotype Ref.4. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay PubMed 18656450. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from sequence orthology PubMed 12051767. Source: MGI

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

phagocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from direct assay Ref.6. Source: UniProtKB

recycling endosome membrane

Inferred from direct assay Ref.4. Source: UniProtKB

synaptic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.4. Source: UniProtKB

GTPase activity

Inferred from mutant phenotype Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1C3VLD34EBI-1634944,EBI-6512684

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 215214Ras-related protein Rab-11B
PRO_0000121159
Propeptide216 – 2183Removed in mature form Potential
PRO_0000370816

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 residue41Citrulline
Modified residue2151Cysteine methyl ester Potential
Lipidation2141S-geranylgeranyl cysteine By similarity
Lipidation2151S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis251S → N: Dominant negative mutant locked in the inactive GDP-bound form; partially relocalizes to the Golgi and alters endocytic recycling. Ref.4
Mutagenesis701Q → L: Constitutively active mutant locked in the active GTP-bound form; alters endocytic recycling. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P46638 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8DE0A98739EBD9FF

FASTA21824,489
        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 AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ 

       190        200        210 
IADRAAHDES PGNNVVDISV PPTTDGQRPN KLQCCQSL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of mouse Rab11b: a new type of mammalian YPT/Rab protein."
Lai F., Stubbs L., Artzt K.
Genomics 22:610-616(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"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/6 and FVB/N.
Tissue: Brain and Colon.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-24; 42-51; 62-72; 75-104; 111-125 AND 167-174, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"Rab11b is essential for recycling of transferrin to the plasma membrane."
Schlierf B., Fey G.H., Hauber J., Hocke G.M., Rosorius O.
Exp. Cell Res. 259:257-265(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTIC RECYCLING, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-25 AND GLN-70.
[5]"Rab11 and its effector Rip11 participate in regulation of insulin granule exocytosis."
Sugawara K., Shibasaki T., Mizoguchi A., Saito T., Seino S.
Genes Cells 14:445-456(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EXOCYTOSIS, TISSUE SPECIFICITY.
[6]"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.
[7]"Rab11b regulates the trafficking and recycling of the epithelial sodium channel (ENaC)."
Butterworth M.B., Edinger R.S., Silvis M.R., Gallo L.I., Liang X., Apodaca G., Frizzell R.A., Fizzell R.A., Johnson J.P.
Am. J. Physiol. 302:F581-F590(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The large conductance calcium-activated K(+) channel interacts with the small GTPase Rab11b."
Sokolowski S., Harvey M., Sakai Y., Jordan A., Sokolowski B.
Biochem. Biophys. Res. Commun. 426:221-225(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNMA1.
[9]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26528 mRNA. Translation: AAC42093.1.
BC054753 mRNA. Translation: AAH54753.1.
BC085270 mRNA. Translation: AAH85270.1.
PIRA55005.
RefSeqNP_033023.1. NM_008997.3.
UniGeneMm.387587.

3D structure databases

ProteinModelPortalP46638.
SMRP46638. Positions 8-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP46638. 4 interactions.
MINTMINT-1862423.

PTM databases

PhosphoSiteP46638.

Proteomic databases

PaxDbP46638.
PRIDEP46638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057373; ENSMUSP00000110021; ENSMUSG00000077450.
GeneID19326.
KEGGmmu:19326.
UCSCuc008bzm.1. mouse.

Organism-specific databases

CTD9230.
MGIMGI:99425. Rab11b.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP46638.
KOK07905.
OMAIQVDAKT.
OrthoDBEOG7SFHZ2.
PhylomeDBP46638.
TreeFamTF300099.

Gene expression databases

ArrayExpressP46638.
BgeeP46638.
CleanExMM_RAB11B.
GenevestigatorP46638.

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

ChiTaRSRAB11B. mouse.
NextBio296291.
PROP46638.
SOURCESearch...

Entry information

Entry nameRB11B_MOUSE
AccessionPrimary (citable) accession number: P46638
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 124 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