ID ARF6_MOUSE Reviewed; 175 AA. AC P62331; P26438; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 189. DE RecName: Full=ADP-ribosylation factor 6; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62330}; GN Name=Arf6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=ICR; TISSUE=Brain; RX PubMed=8947846; DOI=10.1093/oxfordjournals.jbchem.a021484; RA Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.; RT "Structure and intracellular localization of mouse ADP-ribosylation factors RT type 1 to type 6 (ARF1-ARF6)."; RL J. Biochem. 120:813-819(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP INTERACTION WITH GGA1; GGA2 AND GGA3, AND SUBCELLULAR LOCATION. RX PubMed=11950392; DOI=10.1042/bj20020428; RA Takatsu H., Yoshino K., Toda K., Nakayama K.; RT "GGA proteins associate with Golgi membranes through interaction between RT their GGAH domains and ADP-ribosylation factors."; RL Biochem. J. 365:369-378(2002). RN [4] RP FUNCTION AS REGULATOR OF DENDRITIC SPINE DEVELOPMENT. RX PubMed=16325184; DOI=10.1016/j.febslet.2005.11.022; RA Miyazaki H., Yamazaki M., Watanabe H., Maehama T., Yokozeki T., Kanaho Y.; RT "The small GTPase ADP-ribosylation factor 6 negatively regulates dendritic RT spine formation."; RL FEBS Lett. 579:6834-6838(2005). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP FUNCTION, AND MUTAGENESIS OF THR-27. RX PubMed=20080746; DOI=10.1073/pnas.0908423107; RA Ikenouchi J., Umeda M.; RT "FRMD4A regulates epithelial polarity by connecting Arf6 activation with RT the PAR complex."; RL Proc. Natl. Acad. Sci. U.S.A. 107:748-753(2010). RN [7] RP INTERACTION WITH TJAP1, AND MUTAGENESIS OF THR-44 AND GLN-67. RX PubMed=22841714; DOI=10.1016/j.febslet.2012.07.051; RA Tamaki H., Sanda M., Katsumata O., Hara Y., Fukaya M., Sakagami H.; RT "Pilt is a coiled-coil domain-containing protein that localizes at the RT trans-Golgi complex and regulates its structure."; RL FEBS Lett. 586:3064-3070(2012). RN [8] RP FUNCTION IN NEURITE OUTGROWTH, AND MUTAGENESIS OF GLN-67. RX PubMed=23572513; DOI=10.1242/jcs.117846; RA Kobayashi H., Fukuda M.; RT "Rab35 establishes the EHD1-association site by coordinating two distinct RT effectors during neurite outgrowth."; RL J. Cell Sci. 126:2424-2435(2013). RN [9] RP INTERACTION WITH C9ORF72. RX PubMed=27723745; DOI=10.1038/nn.4407; RA Sivadasan R., Hornburg D., Drepper C., Frank N., Jablonka S., Hansel A., RA Lojewski X., Sterneckert J., Hermann A., Shaw P.J., Ince P.G., Mann M., RA Meissner F., Sendtner M.; RT "C9ORF72 interaction with cofilin modulates actin dynamics in motor RT neurons."; RL Nat. Neurosci. 19:1610-1618(2016). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=29420262; DOI=10.1126/science.aan0814; RA Mohanan V., Nakata T., Desch A.N., Levesque C., Boroughs A., Guzman G., RA Cao Z., Creasey E., Yao J., Boucher G., Charron G., Bhan A.K., Schenone M., RA Carr S.A., Reinecker H.C., Daly M.J., Rioux J.D., Lassen K.G., Xavier R.J.; RT "C1orf106 is a colitis risk gene that regulates stability of epithelial RT adherens junctions."; RL Science 359:1161-1166(2018). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 13-175 IN COMPLEX WITH GTP AND RP KIF23, INTERACTION WITH KIF23; RAB11FIP4; GGA1 AND SPAG9, FUNCTION, RP MUTAGENESIS OF THR-27; GLN-67; HIS-76 AND TYR-77, AND SUBCELLULAR LOCATION. RX PubMed=22522702; DOI=10.1038/emboj.2012.89; RA Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A., RA Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M., RA Kawasaki M., Kato R., Wakatsuki S., Nakayama K.; RT "Structural basis for Arf6-MKLP1 complex formation on the Flemming body RT responsible for cytokinesis."; RL EMBO J. 31:2590-2603(2012). CC -!- FUNCTION: GTP-binding protein involved in protein trafficking that CC regulates endocytic recycling and cytoskeleton remodeling CC (PubMed:11950392). Required for normal completion of mitotic CC cytokinesis. Involved in the regulation of dendritic spine development, CC contributing to the regulation of dendritic branching and filopodia CC extension. Plays an important role in membrane trafficking, during CC junctional remodeling and epithelial polarization. Regulates surface CC levels of adherens junction proteins such as CDH1 (PubMed:20080746, CC PubMed:29420262). Required for NTRK1 sorting to the recycling pathway CC from early endosomes (By similarity). {ECO:0000250|UniProtKB:P62332, CC ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:16325184, CC ECO:0000269|PubMed:20080746, ECO:0000269|PubMed:22522702, CC ECO:0000269|PubMed:23572513, ECO:0000269|PubMed:29420262}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000250|UniProtKB:P62330}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62330}; CC -!- ACTIVITY REGULATION: Activation is generally mediated by guanine CC exchange factor (GEF), while inactivation through hydrolysis of bound CC GTP is catalyzed by GTPases activating protein (GAP). Inactivated by CC ACAP1 and ACAP2 (By similarity). Activated by NGF via NTRK1 (By CC similarity). {ECO:0000250|UniProtKB:P62330, CC ECO:0000250|UniProtKB:P62332}. CC -!- SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the CC interaction is required for proper subcellular location of GGA1, GGA2 CC and GGA3 (PubMed:11950392, PubMed:22522702). Interacts with ARHGAP21, CC ASAP2, HERC1, PIP5K1C and UACA. Interacts with NCS1/FREQ at the plasma CC membrane. Interacts with RAB11FIP3. Interacts with USP6 (via Rab-GAP CC TBC domain). Interacts with ECPAS. Interacts with TBC1D24; the CC interaction leads to suppression of ARF6 activity which promotes CC dendritic spine maintenance (By similarity). Interacts with MICALL1. CC Interacts with CYTH3 (By similarity). Interacts with KIF23, forming CC heterodimers and heterotetramers. Interacts with SPAG9 and RAB11FIP4 CC (PubMed:22522702). Interacts with C9orf72 (PubMed:27723745). Interacts CC (GTP-bound form) with TJAP1/PILT (PubMed:22841714). CC {ECO:0000250|UniProtKB:P62330, ECO:0000250|UniProtKB:P62332, CC ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:22522702, CC ECO:0000269|PubMed:22841714, ECO:0000269|PubMed:27723745}. CC -!- INTERACTION: CC P62331; Q9ESN9: Mapk8ip3; NbExp=8; IntAct=EBI-988682, EBI-301496; CC P62331; Q58A65: Spag9; NbExp=10; IntAct=EBI-988682, EBI-6530207; CC P62331; Q9DCD5: Tjap1; NbExp=2; IntAct=EBI-988682, EBI-775733; CC P62331; Q9UJY5: GGA1; Xeno; NbExp=2; IntAct=EBI-988682, EBI-447141; CC P62331; Q02241: KIF23; Xeno; NbExp=10; IntAct=EBI-988682, EBI-306852; CC P62331; Q86YS3: RAB11FIP4; Xeno; NbExp=2; IntAct=EBI-988682, EBI-949727; CC P62331; O60271: SPAG9; Xeno; NbExp=2; IntAct=EBI-988682, EBI-1023301; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P62330}. Cell membrane CC {ECO:0000269|PubMed:29420262}; Lipid-anchor CC {ECO:0000250|UniProtKB:P62330}. Endosome membrane; Lipid-anchor CC {ECO:0000250|UniProtKB:P62330}. Recycling endosome membrane CC {ECO:0000250|UniProtKB:P62330}; Lipid-anchor CC {ECO:0000250|UniProtKB:P62330}. Cell projection, filopodium membrane CC {ECO:0000250|UniProtKB:P62330}; Lipid-anchor CC {ECO:0000250|UniProtKB:P62330}. Cell projection, ruffle CC {ECO:0000250|UniProtKB:P62330}. Cleavage furrow CC {ECO:0000250|UniProtKB:P62330}. Midbody, Midbody ring CC {ECO:0000269|PubMed:22522702}. Early endosome membrane CC {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. Golgi CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; CC Lipid-anchor {ECO:0000305}. Note=Distributed uniformly on the plasma CC membrane, as well as throughout the cytoplasm during metaphase (By CC similarity). Subsequently concentrated at patches in the equatorial CC region at the onset of cytokinesis, and becomes distributed in the CC equatorial region concurrent with cleavage furrow ingression (By CC similarity). In late stages of cytokinesis, concentrates at the midbody CC ring/Flemming body (By similarity). Recruitment to the midbody ring CC requires both activation by PSD/EFA6A and interaction with KIF23/MKLP1 CC (By similarity). After abscission of the intercellular bridge, CC incorporated into one of the daughter cells as a midbody remnant and CC localizes to punctate structures beneath the plasma membrane CC (PubMed:22522702). Recruited to the cell membrane in association with CC CYTH2 and ARL4C (By similarity). Colocalizes with DAB2IP at the plasma CC membrane and endocytic vesicles (By similarity). Myristoylation is CC required for proper localization to membranes: myristoylation on Lys-3 CC allows ARF6 to remain on membranes during the GTPase cycle (By CC similarity). {ECO:0000250|UniProtKB:P62330, CC ECO:0000269|PubMed:22522702}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8947846}. CC -!- PTM: GTP-bound form is myristoylated on Lys-3 by NMT1 and NMT2, CC allowing ARF6 to remain on membranes during the GTPase cycle, thereby CC promoting its activity. GDP-bound inactive form is demyristoylated on CC Lys-3 by SIRT2 at early endosomes or endocytic recycling compartment to CC allow its efficient activation by a guanine exchange factor (GEF) after CC GDP release. {ECO:0000250|UniProtKB:P62330}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D87903; BAA13495.1; -; mRNA. DR EMBL; BC003478; AAH03478.1; -; mRNA. DR EMBL; BC083112; AAH83112.1; -; mRNA. DR CCDS; CCDS25952.1; -. DR PIR; JC4950; JC4950. DR RefSeq; NP_031507.1; NM_007481.3. DR PDB; 3VHX; X-ray; 2.81 A; A/C/E/G=13-175. DR AlphaFoldDB; P62331; -. DR SMR; P62331; -. DR BioGRID; 198189; 20. DR FunCoup; P62331; 3012. DR IntAct; P62331; 11. DR MINT; P62331; -. DR STRING; 10090.ENSMUSP00000055862; -. DR ChEMBL; CHEMBL1075274; -. DR GlyGen; P62331; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62331; -. DR PhosphoSitePlus; P62331; -. DR SwissPalm; P62331; -. DR jPOST; P62331; -. DR PaxDb; 10090-ENSMUSP00000055862; -. DR PeptideAtlas; P62331; -. DR ProteomicsDB; 273921; -. DR Pumba; P62331; -. DR Antibodypedia; 3459; 475 antibodies from 41 providers. DR DNASU; 11845; -. DR Ensembl; ENSMUST00000050063.9; ENSMUSP00000055862.8; ENSMUSG00000044147.9. DR GeneID; 11845; -. DR KEGG; mmu:11845; -. DR UCSC; uc007nsj.1; mouse. DR AGR; MGI:99435; -. DR CTD; 382; -. DR MGI; MGI:99435; Arf6. DR VEuPathDB; HostDB:ENSMUSG00000044147; -. DR eggNOG; KOG0071; Eukaryota. DR GeneTree; ENSGT00940000156593; -. DR HOGENOM; CLU_040729_9_4_1; -. DR InParanoid; P62331; -. DR OMA; GGQISKM; -. DR OrthoDB; 2011769at2759; -. DR PhylomeDB; P62331; -. DR BRENDA; 3.6.5.2; 3474. DR Reactome; R-MMU-8854214; TBC/RABGAPs. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR Reactome; R-MMU-8875656; MET receptor recycling. DR BioGRID-ORCS; 11845; 11 hits in 80 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. DR EvolutionaryTrace; P62331; -. DR PRO; PR:P62331; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; P62331; protein. DR Bgee; ENSMUSG00000044147; Expressed in conjunctival fornix and 288 other cell types or tissues. DR ExpressionAtlas; P62331; baseline and differential. DR GO; GO:0005938; C:cell cortex; ISO:GO_Central. DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0005769; C:early endosome; ISO:GO_Central. DR GO; GO:0031901; C:early endosome membrane; EXP:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:BHF-UCL. DR GO; GO:0010008; C:endosome membrane; ISO:GO_Central. DR GO; GO:0031527; C:filopodium membrane; ISO:GO_Central. DR GO; GO:0090543; C:Flemming body; ISS:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISO:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:GO_Central. DR GO; GO:0030496; C:midbody; ISO:GO_Central. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0098794; C:postsynapse; ISO:GO_Central. DR GO; GO:0098793; C:presynapse; ISO:GO_Central. DR GO; GO:0055037; C:recycling endosome; ISO:GO_Central. DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB. DR GO; GO:0001726; C:ruffle; ISO:GO_Central. DR GO; GO:0003925; F:G protein activity; ISO:GO_Central. DR GO; GO:0019003; F:GDP binding; ISO:GO_Central. DR GO; GO:0005525; F:GTP binding; ISO:GO_Central. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:GO_Central. DR GO; GO:0035591; F:signaling adaptor activity; ISO:GO_Central. DR GO; GO:0031996; F:thioesterase binding; ISO:GO_Central. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:GO_Central. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:GO_Central. DR GO; GO:0032456; P:endocytic recycling; ISO:GO_Central. DR GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:MGI. DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0001889; P:liver development; IMP:MGI. DR GO; GO:0099562; P:maintenance of postsynaptic density structure; ISO:GO_Central. DR GO; GO:0033028; P:myeloid cell apoptotic process; IMP:MGI. DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:GO_Central. DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:GO_Central. DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IMP:ARUK-UCL. DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:ARUK-UCL. DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; ISO:GO_Central. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:GO_Central. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL. DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:GO_Central. DR GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL. DR GO; GO:1905345; P:protein localization to cleavage furrow; ISO:GO_Central. DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:GO_Central. DR GO; GO:0015031; P:protein transport; TAS:MGI. DR GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB. DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:GO_Central. DR GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI. DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:GO_Central. DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:GO_Central. DR GO; GO:0034143; P:regulation of toll-like receptor 4 signaling pathway; NAS:BHF-UCL. DR GO; GO:0097178; P:ruffle assembly; ISO:GO_Central. DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:GO_Central. DR GO; GO:0016192; P:vesicle-mediated transport; ISO:GO_Central. DR CDD; cd04149; Arf6; 1. DR FunFam; 3.40.50.300:FF:000286; ADP-ribosylation factor 6; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR041838; Arf6. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR024156; Small_GTPase_ARF. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51417; ARF; 1. DR PDBsum; 3VHX; -. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cell projection; KW Cytoplasm; Differentiation; Endosome; Golgi apparatus; GTP-binding; KW Hydrolase; Lipoprotein; Membrane; Myristate; Neurogenesis; KW Nucleotide-binding; Protein transport; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62330" FT CHAIN 2..175 FT /note="ADP-ribosylation factor 6" FT /id="PRO_0000207401" FT BINDING 23..28 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22522702" FT BINDING 41..44 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62330" FT BINDING 63..67 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22522702" FT BINDING 122..125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22522702" FT BINDING 155..156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62330" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250|UniProtKB:P62330" FT LIPID 3 FT /note="N6-myristoyl lysine" FT /evidence="ECO:0000250|UniProtKB:P62330" FT MUTAGEN 27 FT /note="T->N: Loss of activity; delays formation of FT epithelial polarity." FT /evidence="ECO:0000269|PubMed:20080746, FT ECO:0000269|PubMed:22522702" FT MUTAGEN 44 FT /note="T->N: Inactive GDP-bound form which does not bind FT TJAP1." FT /evidence="ECO:0000269|PubMed:22841714" FT MUTAGEN 67 FT /note="Q->L: Probable constitutively active mutant that FT prevents EHD1 localization to endosome membranes. No effect FT on interaction with TJAP1." FT /evidence="ECO:0000269|PubMed:22522702, FT ECO:0000269|PubMed:22841714, ECO:0000269|PubMed:23572513" FT MUTAGEN 76 FT /note="H->A: Slightly impaired interaction with KIF23. FT Abolishes interaction with GGA1, SPAG9 and RAB11FIP4." FT /evidence="ECO:0000269|PubMed:22522702" FT MUTAGEN 77 FT /note="Y->A: Loss of interaction with KIF23, GGA1, SPAG9 FT and RAB11FIP4." FT /evidence="ECO:0000269|PubMed:22522702" FT STRAND 13..19 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 26..35 FT /evidence="ECO:0007829|PDB:3VHX" FT STRAND 45..54 FT /evidence="ECO:0007829|PDB:3VHX" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:3VHX" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:3VHX" FT STRAND 82..89 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 96..107 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:3VHX" FT STRAND 116..122 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 132..138 FT /evidence="ECO:0007829|PDB:3VHX" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:3VHX" FT TURN 156..159 FT /evidence="ECO:0007829|PDB:3VHX" FT HELIX 162..171 FT /evidence="ECO:0007829|PDB:3VHX" SQ 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 //