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O35509 (RB11B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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

Subunit structure

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

Subcellular location

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

Post-translational modification

Citrullinated by PADI4 By similarity.

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
Reference proteome
Gene Ontology (GO)
   Biological_processcellular component movement

Non-traceable author statement PubMed 12051767. Source: RGD

cellular response to acidity

Inferred from sequence or structural similarity. Source: UniProtKB

constitutive secretory pathway

Inferred from mutant phenotype Ref.4. Source: UniProtKB

insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

receptor recycling

Inferred from sequence or structural similarity. Source: UniProtKB

regulated secretory pathway

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of anion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endocytic recycling

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 12051767. Source: MGI

mitochondrion

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptic vesicle

Inferred from direct assay Ref.4. 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 sequence or structural similarity. Source: UniProtKB

GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 215214Ras-related protein Rab-11B
PRO_0000121160
Propeptide216 – 2183Removed in mature form Potential
PRO_0000370817

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

Experimental info

Sequence conflict1201M → L in BAA22522. Ref.1
Sequence conflict135 – 1373PTD → CPLT in BAA22522. Ref.1
Sequence conflict145 – 1473KNN → RH in BAA22522. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35509 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8DF146BA39EBD9FF

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 PPTTDGQKPN KLQCCQNL 

« Hide

References

« Hide 'large scale' references
[1]"A novel YPT1/SEC4 related gene from rat brain."
Sakurada K., Aisaka K., Ito S., Takeyama Y., Hori Y., Takai Y.
Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]Zhao H., Gao L., Vaananen K.H.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Bone.
[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].
Tissue: Prostate.
[4]"Divergent functions of neuronal Rab11b in Ca2+-regulated versus constitutive exocytosis."
Khvotchev M.V., Ren M., Takamori S., Jahn R., Suedhof T.C.
J. Neurosci. 23:10531-10539(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EXOCYTOSIS, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D01046 mRNA. Translation: BAA22522.1.
AF286534 mRNA. Translation: AAG00542.1.
BC062041 mRNA. Translation: AAH62041.1.
RefSeqNP_116006.1. NM_032617.2.
UniGeneRn.124832.

3D structure databases

ProteinModelPortalO35509.
SMRO35509. Positions 8-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249465. 1 interaction.
IntActO35509. 1 interaction.
MINTMINT-4542683.
STRING10116.ENSRNOP00000010197.

PTM databases

PhosphoSiteO35509.

Proteomic databases

PaxDbO35509.
PRIDEO35509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010197; ENSRNOP00000010197; ENSRNOG00000007648.
GeneID79434.
KEGGrno:79434.
UCSCRGD:68369. rat.

Organism-specific databases

CTD9230.
RGD68369. Rab11b.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00710000106372.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidO35509.
KOK07905.
OMAIQVDAKT.
OrthoDBEOG7SFHZ2.
PhylomeDBO35509.
TreeFamTF300099.

Gene expression databases

GenevestigatorO35509.

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

NextBio614803.
PROO35509.

Entry information

Entry nameRB11B_RAT
AccessionPrimary (citable) accession number: O35509
Secondary accession number(s): Q9ET14
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 4 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