ARF6_MOUSE
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 03-AUG-2022, entry version 170.
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, Pancreas,
RC 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:29420262,
CC PubMed:20080746). 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 + H(+) + phosphate; 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. Interacts
CC with MICALL1. Interacts with CYTH3 (By similarity). Interacts with
CC KIF23, forming heterodimers and heterotetramers. Interacts with SPAG9
CC and RAB11FIP4 (PubMed:22522702). Interacts with C9orf72
CC (PubMed:27723745). Interacts (GTP-bound form) with TJAP1/PILT
CC (PubMed:22841714). {ECO:0000250|UniProtKB:P62330,
CC ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11950392,
CC ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:22841714,
CC 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}.
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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 PDBsum; 3VHX; -.
DR AlphaFoldDB; P62331; -.
DR SMR; P62331; -.
DR BioGRID; 198189; 15.
DR IntAct; P62331; 11.
DR MINT; P62331; -.
DR STRING; 10090.ENSMUSP00000055862; -.
DR ChEMBL; CHEMBL1075274; -.
DR iPTMnet; P62331; -.
DR PhosphoSitePlus; P62331; -.
DR SwissPalm; P62331; -.
DR EPD; P62331; -.
DR jPOST; P62331; -.
DR PaxDb; P62331; -.
DR PeptideAtlas; P62331; -.
DR PRIDE; P62331; -.
DR ProteomicsDB; 273921; -.
DR Antibodypedia; 3459; 474 antibodies from 37 providers.
DR DNASU; 11845; -.
DR Ensembl; ENSMUST00000050063; ENSMUSP00000055862; ENSMUSG00000044147.
DR GeneID; 11845; -.
DR KEGG; mmu:11845; -.
DR UCSC; uc007nsj.1; mouse.
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; WSVIPTI; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P62331; -.
DR TreeFam; TF300808; -.
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 75 CRISPR screens.
DR ChiTaRS; Arf6; mouse.
DR PRO; PR:P62331; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P62331; protein.
DR Bgee; ENSMUSG00000044147; Expressed in conjunctival fornix and 285 other tissues.
DR ExpressionAtlas; P62331; baseline and differential.
DR Genevisible; P62331; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:BHF-UCL.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:Ensembl.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; TAS:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
DR GO; GO:0031996; F:thioesterase binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:1902217; P:erythrocyte apoptotic process; IMP:MGI.
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:MGI.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
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:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
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:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:MGI.
DR GO; GO:0034143; P:regulation of toll-like receptor 4 signaling pathway; NAS:BHF-UCL.
DR GO; GO:0097178; P:ruffle assembly; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04149; Arf6; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041838; Arf6.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
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 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
