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ADP-ribosylation factor 6

 ARF6_MOUSE              Reviewed;         175 AA.
P62331; P26438;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-DEC-2017, entry version 142.
RecName: Full=ADP-ribosylation factor 6;
Name=Arf6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=ICR; TISSUE=Brain;
PubMed=8947846; DOI=10.1093/oxfordjournals.jbchem.a021484;
Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
"Structure and intracellular localization of mouse ADP-ribosylation
factors type 1 to type 6 (ARF1-ARF6).";
J. Biochem. 120:813-819(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION AS REGULATOR OF DENDRITIC SPINE DEVELOPMENT.
PubMed=16325184; DOI=10.1016/j.febslet.2005.11.022;
Miyazaki H., Yamazaki M., Watanabe H., Maehama T., Yokozeki T.,
Kanaho Y.;
"The small GTPase ADP-ribosylation factor 6 negatively regulates
dendritic spine formation.";
FEBS Lett. 579:6834-6838(2005).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
FUNCTION, AND MUTAGENESIS OF THR-27.
PubMed=20080746; DOI=10.1073/pnas.0908423107;
Ikenouchi J., Umeda M.;
"FRMD4A regulates epithelial polarity by connecting Arf6 activation
with the PAR complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:748-753(2010).
[6]
FUNCTION IN NEURITE OUTGROWTH, AND MUTAGENESIS OF GLN-67.
PubMed=23572513; DOI=10.1242/jcs.117846;
Kobayashi H., Fukuda M.;
"Rab35 establishes the EHD1-association site by coordinating two
distinct effectors during neurite outgrowth.";
J. Cell Sci. 126:2424-2435(2013).
[7]
INTERACTION WITH C9ORF72.
PubMed=27723745; DOI=10.1038/nn.4407;
Sivadasan R., Hornburg D., Drepper C., Frank N., Jablonka S.,
Hansel A., Lojewski X., Sterneckert J., Hermann A., Shaw P.J.,
Ince P.G., Mann M., Meissner F., Sendtner M.;
"C9ORF72 interaction with cofilin modulates actin dynamics in motor
neurons.";
Nat. Neurosci. 19:1610-1618(2016).
[8]
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, AND
SUBCELLULAR LOCATION.
PubMed=22522702; DOI=10.1038/emboj.2012.89;
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.;
"Structural basis for Arf6-MKLP1 complex formation on the Flemming
body responsible for cytokinesis.";
EMBO J. 31:2590-2603(2012).
-!- 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. Involved in epithelial polarization
(PubMed:20080746). {ECO:0000269|PubMed:16325184,
ECO:0000269|PubMed:20080746, ECO:0000269|PubMed:22522702,
ECO:0000269|PubMed:23572513}.
-!- 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).
{ECO:0000250|UniProtKB:P62330}.
-!- SUBUNIT: 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 (PubMed:22522702). Interacts with C9orf72
(PubMed:27723745). {ECO:0000250, ECO:0000269|PubMed:22522702,
ECO:0000269|PubMed:27723745}.
-!- INTERACTION:
Q9UJY5:GGA1 (xeno); NbExp=2; IntAct=EBI-988682, EBI-447141;
Q02241:KIF23 (xeno); NbExp=10; IntAct=EBI-988682, EBI-306852;
Q9ESN9:Mapk8ip3; NbExp=8; IntAct=EBI-988682, EBI-301496;
Q86YS3:RAB11FIP4 (xeno); NbExp=2; IntAct=EBI-988682, EBI-949727;
O60271:SPAG9 (xeno); NbExp=2; IntAct=EBI-988682, EBI-1023301;
Q58A65:Spag9; NbExp=10; IntAct=EBI-988682, EBI-6530207;
Q9DCD5:Tjap1; NbExp=3; IntAct=EBI-988682, EBI-775733;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P62330}. Cell membrane; Lipid-anchor
{ECO:0000250|UniProtKB:P62330}. Endosome membrane; Lipid-anchor
{ECO:0000250|UniProtKB:P62330}. Recycling endosome membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}. Cell projection,
filopodium membrane; Lipid-anchor. Cell projection, ruffle
{ECO:0000250|UniProtKB:P62330}. Cleavage furrow
{ECO:0000250|UniProtKB:P62330}. Midbody, Midbody ring
{ECO:0000269|PubMed:22522702}. Golgi apparatus
{ECO:0000250|UniProtKB:P62331}. Note=Distributed uniformly on the
plasma membrane, as well as throughout the cytoplasm during
metaphase. Subsequently concentrated at patches in the equatorial
region at the onset of cytokinesis, and becomes distributed in the
equatorial region concurrent with cleavage furrow ingression. In
late stages of cytokinesis, concentrates at the midbody
ring/Flemming body. Recruitement to the midbody ring requires both
activation by PSD/EFA6A and interaction with KIF23/MKLP1. After
abscission of the intercellular bridge, incorporated into one of
the daughter cells as a midbody remnant and localizes to punctate
structures beneath the plasma membrane (PubMed:22522702).
Recruited to the cell membrane in association with CYTH2 and
ARL4C. Colocalizes with DAB2IP at the plasma membrane and
endocytic vesicles. Myristoylation is required for proper
localization to membranes (By similarity).
{ECO:0000250|UniProtKB:P62330, ECO:0000269|PubMed:22522702}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:8947846}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D87903; BAA13495.1; -; mRNA.
EMBL; BC003478; AAH03478.1; -; mRNA.
EMBL; BC083112; AAH83112.1; -; mRNA.
CCDS; CCDS25952.1; -.
PIR; JC4950; JC4950.
RefSeq; NP_031507.1; NM_007481.3.
UniGene; Mm.27308; -.
PDB; 3VHX; X-ray; 2.81 A; A/C/E/G=13-175.
PDBsum; 3VHX; -.
ProteinModelPortal; P62331; -.
SMR; P62331; -.
BioGrid; 198189; 5.
IntAct; P62331; 12.
MINT; MINT-1866703; -.
STRING; 10090.ENSMUSP00000055862; -.
ChEMBL; CHEMBL1075274; -.
iPTMnet; P62331; -.
PhosphoSitePlus; P62331; -.
SwissPalm; P62331; -.
EPD; P62331; -.
PaxDb; P62331; -.
PeptideAtlas; P62331; -.
PRIDE; P62331; -.
Ensembl; ENSMUST00000050063; ENSMUSP00000055862; ENSMUSG00000044147.
GeneID; 11845; -.
KEGG; mmu:11845; -.
UCSC; uc007nsj.1; mouse.
CTD; 382; -.
MGI; MGI:99435; Arf6.
eggNOG; KOG0071; Eukaryota.
eggNOG; ENOG410XP1U; LUCA.
GeneTree; ENSGT00780000121855; -.
HOGENOM; HOG000163691; -.
HOVERGEN; HBG002073; -.
InParanoid; P62331; -.
KO; K07941; -.
OMA; IQDREMK; -.
OrthoDB; EOG091G0OXD; -.
PhylomeDB; P62331; -.
TreeFam; TF300808; -.
Reactome; R-MMU-8854214; TBC/RABGAPs.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8875656; MET receptor recycling.
PRO; PR:P62331; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000044147; -.
CleanEx; MM_ARF6; -.
ExpressionAtlas; P62331; baseline and differential.
Genevisible; P62331; MM.
GO; GO:0005938; C:cell cortex; ISO:MGI.
GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031527; C:filopodium membrane; ISO:MGI.
GO; GO:0090543; C:Flemming body; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; ISO:MGI.
GO; GO:0005525; F:GTP binding; TAS:BHF-UCL.
GO; GO:0003924; F:GTPase activity; TAS:BHF-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
GO; GO:0031996; F:thioesterase binding; ISO:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0033028; P:myeloid cell apoptotic process; IMP:MGI.
GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL.
GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; TAS:MGI.
GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI.
GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:MGI.
GO; GO:0034143; P:regulation of toll-like receptor 4 signaling pathway; NAS:BHF-UCL.
GO; GO:0031529; P:ruffle organization; ISO:MGI.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR024156; Small_GTPase_ARF.
InterPro; IPR006689; Small_GTPase_ARF/SAR.
Pfam; PF00025; Arf; 1.
PRINTS; PR00328; SAR1GTPBP.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51417; ARF; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Differentiation;
Endosome; ER-Golgi transport; Golgi apparatus; GTP-binding;
Lipoprotein; Membrane; Myristate; Neurogenesis; Nucleotide-binding;
Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P62330}.
CHAIN 2 175 ADP-ribosylation factor 6.
/FTId=PRO_0000207401.
NP_BIND 23 28 GTP. {ECO:0000269|PubMed:22522702}.
NP_BIND 41 44 GTP. {ECO:0000250}.
NP_BIND 63 67 GTP. {ECO:0000269|PubMed:22522702}.
NP_BIND 122 125 GTP. {ECO:0000269|PubMed:22522702}.
NP_BIND 155 156 GTP. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:P62330}.
MUTAGEN 27 27 T->N: Loss of activity; delays formation
of epithelial polarity.
{ECO:0000269|PubMed:20080746,
ECO:0000269|PubMed:22522702}.
MUTAGEN 67 67 Q->L: Probable constitutively active
mutant that prevents EHD1 localization to
endosome membranes.
{ECO:0000269|PubMed:22522702,
ECO:0000269|PubMed:23572513}.
MUTAGEN 76 76 H->A: Slightly impaired interaction with
KIF23. Abolishes interaction with GGA1,
SPAG9 and RAB11FIP4.
{ECO:0000269|PubMed:22522702}.
MUTAGEN 77 77 Y->A: Loss of interaction with KIF23,
GGA1, SPAG9 and RAB11FIP4.
{ECO:0000269|PubMed:22522702}.
STRAND 13 19 {ECO:0000244|PDB:3VHX}.
HELIX 26 35 {ECO:0000244|PDB:3VHX}.
STRAND 45 54 {ECO:0000244|PDB:3VHX}.
STRAND 57 64 {ECO:0000244|PDB:3VHX}.
TURN 68 70 {ECO:0000244|PDB:3VHX}.
HELIX 71 77 {ECO:0000244|PDB:3VHX}.
STRAND 82 89 {ECO:0000244|PDB:3VHX}.
HELIX 96 107 {ECO:0000244|PDB:3VHX}.
HELIX 110 112 {ECO:0000244|PDB:3VHX}.
STRAND 116 122 {ECO:0000244|PDB:3VHX}.
HELIX 132 138 {ECO:0000244|PDB:3VHX}.
STRAND 149 153 {ECO:0000244|PDB:3VHX}.
TURN 156 159 {ECO:0000244|PDB:3VHX}.
HELIX 162 171 {ECO:0000244|PDB:3VHX}.
SEQUENCE 175 AA; 20082 MW; 49E38E59AEA52B98 CRC64;
MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLYEGLTWLT SNYKS


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