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P35281 (RAB10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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-10
Gene names
Name:Rab10
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
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 By similarity. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. Finally, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. Ref.3

Enzyme regulation

Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). That Rab is activated by the DENND4C guanine exchange factor (GEF) By similarity.

Subunit structure

Interacts (GDP-bound form) with LLGL1; the interaction is direct and promotes RAB10 association with membranes and activation through competition with the Rab inhibitor GDI1. Ref.3

Subcellular location

Cytoplasmic vesicle membrane By similarity; Lipid-anchor Probable; Cytoplasmic side Probable. Golgi apparatustrans-Golgi network membrane By similarity. Endosome membrane By similarity. Recycling endosome membrane By similarity. Cytoplasmic vesiclephagosome membrane By similarity. Cell projectioncilium. Endoplasmic reticulum membrane By similarity. Note: Associates with SLC2A4/GLUT4 storage vesicles By similarity. Localizes to the base of the cilium. Transiently associates with phagosomes By similarity. Localizes to the endoplasmic reticulum at domains of new tubule growth By similarity. Ref.2

Tissue specificity

Highest levels in neural and muscle tissues.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell projection
Cytoplasmic vesicle
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi to plasma membrane transport

Inferred from mutant phenotype Ref.3. Source: UniProtKB

axonogenesis

Inferred from mutant phenotype Ref.3. Source: UniProtKB

basolateral protein localization

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to antibiotic

Inferred from expression pattern PubMed 7688123. Source: RGD

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum tubular network organization

Inferred from sequence or structural similarity. Source: UniProtKB

endosomal transport

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of neuroblast polarity

Inferred from mutant phenotype Ref.3. Source: UniProtKB

establishment of protein localization to endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

polarized epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum tubular network

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

insulin-responsive compartment

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay PubMed 7688123. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 7688123. Source: RGD

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

primary cilium

Inferred from direct assay Ref.2. Source: UniProtKB

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from direct assay PubMed 7688123. Source: RGD

   Molecular_functionGDP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Ras-related protein Rab-10
PRO_0000121148

Regions

Nucleotide binding16 – 238GTP By similarity
Nucleotide binding64 – 685GTP By similarity
Nucleotide binding122 – 1254GTP By similarity
Motif38 – 469Effector region By similarity

Amino acid modifications

Modified residue1021N6-acetyllysine By similarity
Lipidation1991S-geranylgeranyl cysteine By similarity
Lipidation2001S-geranylgeranyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P35281 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: EFAF804FD4C3B6A3

FASTA20022,858
        10         20         30         40         50         60 
MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIEIDFKIKT VELQGKKIKL 

        70         80         90        100        110        120 
QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI SKWLRNIDQH ANEDVERMLL 

       130        140        150        160        170        180 
RNKCDMDHKR VVPKGKGEQI AREHRIRFFE TSAKANINIE KAFLTLPEDI LRKTPVKEPN 

       190        200 
SENVDISSGG GVTGWKSKCC 

« Hide

References

[1]"Rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain."
Elferink L.A., Anzai K., Scheller R.H.
J. Biol. Chem. 267:5768-5775(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Rab10 associates with primary cilia and the exocyst complex in renal epithelial cells."
Babbey C.M., Bacallao R.L., Dunn K.W.
Am. J. Physiol. 299:F495-506(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"Lgl1 activation of rab10 promotes axonal membrane trafficking underlying neuronal polarization."
Wang T., Liu Y., Xu X.H., Deng C.Y., Wu K.Y., Zhu J., Fu X.Q., He M., Luo Z.G.
Dev. Cell 21:431-444(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AXON DEVELOPMENT, INTERACTION WITH LLGL1 AND GDI1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83677 mRNA. Translation: AAA41991.1.
PIRB42148.
UniGeneRn.65864.

3D structure databases

ProteinModelPortalP35281.
SMRP35281. Positions 4-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP35281. 2 interactions.
MINTMINT-4590846.

PTM databases

PhosphoSiteP35281.

Proteomic databases

PRIDEP35281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD620879. Rab10.

Phylogenomic databases

HOVERGENHBG009351.
PhylomeDBP35281.

Gene expression databases

GenevestigatorP35281.

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

PROP35281.

Entry information

Entry nameRAB10_RAT
AccessionPrimary (citable) accession number: P35281
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 99 of the entry and version 1 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