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P62331 (ARF6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
ADP-ribosylation factor 6
Gene names
Name:Arf6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. May also modulate vesicle budding and uncoating within the Golgi apparatus. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Ref.3 Ref.4 Ref.5

Enzyme regulation

Activation is generally mediated by guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by GTPases activating protein (GAP). Inactivated by ACAP1 and ACAP2 By similarity.

Subunit structure

Interacts with ARHGAP21, ASAP2, HERC1, PIP5K1C and UACA. Interacts with NCS1/FREQ at the plasma membrane. Interacts with RAB11FIP3. Interacts with USP6 (via Rab-GAP TBC domain). Interacts with ECM29. Interacts with TBC1D24. Interacts with MICALL1. Interacts with CYTH3 By similarity. Interacts with KIF23, forming heterodimers and heterotetramers. Interacts with GGA1, SPAG9 and RAB11FIP4. Ref.5

Subcellular location

Golgi apparatus By similarity. Cell membrane; Lipid-anchor By similarity. Endosome membrane; Lipid-anchor By similarity. Recycling endosome membrane; Lipid-anchor By similarity. Cell projectionfilopodium membrane; Lipid-anchor By similarity. Midbody. Cytoplasm. Cleavage furrow. Note: Recruited to the cell membrane in association with CYTH2 and ARL4C. Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles By similarity. Distributed throughout the cytoplasm during metaphase. Transiently detected at the ingressing cleavage furrow during mitotic cytokinesis. Recruited to the midbody at later stages of cytokinesis; this requires interaction with KIF23. Ref.1 Ref.5

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
ER-Golgi transport
Neurogenesis
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Endosome
Golgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Myristate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement PubMed 16751103. Source: GOC

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

establishment of epithelial cell polarity

Inferred from mutant phenotype PubMed 20080746. Source: MGI

hepatocyte apoptotic process

Inferred from mutant phenotype PubMed 16880525. Source: MGI

liver development

Inferred from mutant phenotype PubMed 16880525. Source: MGI

myeloid cell apoptotic process

Inferred from mutant phenotype PubMed 16880525. Source: MGI

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of establishment of protein localization to plasma membrane

Inferred from direct assay PubMed 16751103. Source: BHF-UCL

protein localization to cell surface

Inferred from direct assay PubMed 16751103. Source: BHF-UCL

protein localization to endosome

Inferred from mutant phenotype Ref.4. Source: UniProtKB

protein transport

Traceable author statement Ref.1. Source: MGI

regulation of Rac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

regulation of dendritic spine development

Inferred from mutant phenotype Ref.3. Source: UniProtKB

regulation of filopodium assembly

Inferred from electronic annotation. Source: Ensembl

regulation of toll-like receptor 4 signaling pathway

Non-traceable author statement PubMed 16751103. Source: BHF-UCL

ruffle organization

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: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from electronic annotation. Source: Ensembl

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.1. Source: MGI

early endosome

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.1. Source: MGI

recycling endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Traceable author statement PubMed 16751103. Source: BHF-UCL

GTPase activity

Traceable author statement PubMed 16751103. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GGA1Q9UJY52EBI-988682,EBI-447141From a different organism.
KIF23Q0224110EBI-988682,EBI-306852From a different organism.
Mapk8ip3Q9ESN98EBI-988682,EBI-301496
RAB11FIP4Q86YS32EBI-988682,EBI-949727From a different organism.
SPAG9O602712EBI-988682,EBI-1023301From a different organism.
Spag9Q58A6510EBI-988682,EBI-6530207
Tjap1Q9DCD53EBI-988682,EBI-775733

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 175174ADP-ribosylation factor 6
PRO_0000207401

Regions

Nucleotide binding23 – 286GTP
Nucleotide binding41 – 444GTP By similarity
Nucleotide binding63 – 675GTP
Nucleotide binding122 – 1254GTP
Nucleotide binding155 – 1562GTP By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity

Experimental info

Mutagenesis271T → N: Loss of activity. Ref.5
Mutagenesis671Q → L: Probable constitutively active mutant that prevents EHD1 localization to endosome membranes. Ref.4 Ref.5
Mutagenesis761H → A: Slightly impaired interaction with KIF23. Abolishes interaction with GGA1, SPAG9 and RAB11FIP4. Ref.5
Mutagenesis771Y → A: Loss of interaction with KIF23, GGA1, SPAG9 and RAB11FIP4. Ref.5

Secondary structure

............................ 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62331 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 49E38E59AEA52B98

FASTA17520,082
        10         20         30         40         50         60 
MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN 

        70         80         90        100        110        120 
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF 

       130        140        150        160        170 
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLYEGLTWLT SNYKS 

« Hide

References

« Hide 'large scale' references
[1]"Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6)."
Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.
J. Biochem. 120:813-819(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: ICR.
Tissue: Brain.
[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: FVB/N.
Tissue: Mammary tumor.
[3]"The small GTPase ADP-ribosylation factor 6 negatively regulates dendritic spine formation."
Miyazaki H., Yamazaki M., Watanabe H., Maehama T., Yokozeki T., Kanaho Y.
FEBS Lett. 579:6834-6838(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS REGULATOR OF DENDRITIC SPINE DEVELOPMENT.
[4]"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: FUNCTION IN NEURITE OUTGROWTH, MUTAGENESIS OF GLN-67.
[5]"Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis."
Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A., Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M., Kawasaki M., Kato R., Wakatsuki S., Nakayama K.
EMBO J. 31:2590-2603(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 13-175 IN COMPLEX WITH GTP AND KIF23, INTERACTION WITH KIF23; RAB11FIP4; GGA1 AND SPAG9, FUNCTION, MUTAGENESIS OF THR-27; GLN-67; HIS-76 AND TYR-77, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87903 mRNA. Translation: BAA13495.1.
BC003478 mRNA. Translation: AAH03478.1.
BC083112 mRNA. Translation: AAH83112.1.
PIRJC4950.
RefSeqNP_031507.1. NM_007481.3.
UniGeneMm.27308.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VHXX-ray2.81A/C/E/G13-175[»]
ProteinModelPortalP62331.
SMRP62331. Positions 12-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198189. 2 interactions.
IntActP62331. 12 interactions.
MINTMINT-1866703.
STRING10090.ENSMUSP00000055862.

Chemistry

ChEMBLCHEMBL1075274.

PTM databases

PhosphoSiteP62331.

Proteomic databases

PaxDbP62331.
PRIDEP62331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050063; ENSMUSP00000055862; ENSMUSG00000044147.
GeneID11845.
KEGGmmu:11845.
UCSCuc007nsj.1. mouse.

Organism-specific databases

CTD382.
MGIMGI:99435. Arf6.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidP62331.
KOK07941.
OMATELHRII.
OrthoDBEOG7F5133.
PhylomeDBP62331.
TreeFamTF300808.

Gene expression databases

ArrayExpressP62331.
BgeeP62331.
CleanExMM_ARF6.
GenevestigatorP62331.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio1599.
PROP62331.
SOURCESearch...

Entry information

Entry nameARF6_MOUSE
AccessionPrimary (citable) accession number: P62331
Secondary accession number(s): P26438
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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