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Q5U316 (RAB35_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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-35
Gene names
Name:Rab35
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length201 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth By similarity.

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 guanine exchange factors DENND1A, DENND1B and DENND1C By similarity.

Subunit structure

Interacts with DENND1A and DENND1B; in a nucleotide-dependent manner. Interacts with DENND1C; weak interaction which is nucleotide-independent. Interacts (GTP-bound form) with ACAP2 and MICALL1; the interaction is direct and probably recruits ACAP2 and MICALL1 to membranes. Interacts with EHD1; the interaction is indirect through MICALL1 and probably recruits EHD1 to membranes. Ref.2

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Membraneclathrin-coated pit By similarity. Cytoplasmic vesicleclathrin-coated vesicle By similarity. Endosome. Melanosome By similarity. Note: Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. Ref.2

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Coated pit
Cytoplasmic vesicle
Endosome
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to nerve growth factor stimulus

Inferred from direct assay Ref.2. Source: UniProtKB

cytokinesis

Inferred from electronic annotation. Source: Ensembl

endosomal transport

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to endosome

Inferred from mutant phenotype Ref.2. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell projection membrane

Inferred from electronic annotation. Source: Ensembl

clathrin-coated endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome membrane

Inferred from direct assay Ref.2. Source: UniProtKB

intercellular bridge

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGDP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Ras-related protein Rab-35
PRO_0000121247

Regions

Nucleotide binding15 – 228GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding120 – 1234GTP By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Lipidation2001S-geranylgeranyl cysteine By similarity
Lipidation2011S-geranylgeranyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5U316 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 31EB15D6D42E076E

FASTA20123,025
        10         20         30         40         50         60 
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ 

        70         80         90        100        110        120 
IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN 

       130        140        150        160        170        180 
KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ 

       190        200 
QQQQNDVVKL TKNSKRKKRC C 

« Hide

References

« Hide 'large scale' references
[1]"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: Testis.
[2]"Rab35 establishes the EHD1-association site by coordinating two distinct effectors during neurite outgrowth."
Kobayashi H., Fukuda M.
J. Cell Sci. 126:2424-2435(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACAP2; EHD1 AND MICALL1, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC085769 mRNA. Translation: AAH85769.1.
RefSeqNP_001013064.1. NM_001013046.1.
UniGeneRn.18008.

3D structure databases

ProteinModelPortalQ5U316.
SMRQ5U316. Positions 4-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000029070.

PTM databases

PhosphoSiteQ5U316.

Proteomic databases

PaxDbQ5U316.
PRIDEQ5U316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000030031; ENSRNOP00000029070; ENSRNOG00000022014.
GeneID288700.
KEGGrno:288700.
UCSCRGD:1306362. rat.

Organism-specific databases

CTD11021.
RGD1306362. Rab35.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00740000115017.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ5U316.
KOK07876.
OMANRILVGN.
OrthoDBEOG7VB2H4.
TreeFamTF105954.

Gene expression databases

GenevestigatorQ5U316.

Family and domain databases

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

NextBio628573.
PROQ5U316.

Entry information

Entry nameRAB35_RAT
AccessionPrimary (citable) accession number: Q5U316
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 7, 2004
Last modified: February 19, 2014
This is version 86 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