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<entry dataset="Swiss-Prot" created="2004-07-05" modified="2025-04-09" version="204" xmlns="http://uniprot.org/uniprot">
  <accession>P62330</accession>
  <accession>P26438</accession>
  <accession>Q6FGZ2</accession>
  <name>ARF6_HUMAN</name>
  <protein>
    <recommendedName>
      <fullName evidence="37">ADP-ribosylation factor 6</fullName>
      <ecNumber evidence="31">3.6.5.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="37 39" type="primary">ARF6</name>
  </gene>
  <organism>
    <name type="scientific">Homo sapiens</name>
    <name type="common">Human</name>
    <dbReference type="NCBI Taxonomy" id="9606"/>
    <lineage>
      <taxon>Eukaryota</taxon>
      <taxon>Metazoa</taxon>
      <taxon>Chordata</taxon>
      <taxon>Craniata</taxon>
      <taxon>Vertebrata</taxon>
      <taxon>Euteleostomi</taxon>
      <taxon>Mammalia</taxon>
      <taxon>Eutheria</taxon>
      <taxon>Euarchontoglires</taxon>
      <taxon>Primates</taxon>
      <taxon>Haplorrhini</taxon>
      <taxon>Catarrhini</taxon>
      <taxon>Hominidae</taxon>
      <taxon>Homo</taxon>
    </lineage>
  </organism>
  <reference key="1">
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    <scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
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    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>TISSUE SPECIFICITY</scope>
  </reference>
  <reference key="3">
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
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      <tissue>Umbilical cord blood</tissue>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
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      <tissue>Brain</tissue>
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        <person name="Kikuchi H."/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
    <source>
      <tissue>Trachea</tissue>
    </source>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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        <consortium name="The MGC Project Team"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
    <source>
      <tissue>Skin</tissue>
      <tissue>Uterus</tissue>
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    <scope>MYRISTOYLATION AT GLY-2</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>MUTAGENESIS OF GLY-2</scope>
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    <scope>ACTIVITY REGULATION</scope>
    <source>
      <tissue>Leukocyte</tissue>
    </source>
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      <title>GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.</title>
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    <scope>INTERACTION WITH GGA1; GGA2 AND GGA3</scope>
  </reference>
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      <title>ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma.</title>
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    <scope>INTERACTION WITH PIP5K1C</scope>
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    </citation>
    <scope>INTERACTION WITH USP6</scope>
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    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>MUTAGENESIS OF THR-27 AND GLN-67</scope>
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    <scope>INTERACTION WITH RAB11FIP3 AND RAB11FIP4</scope>
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      <dbReference type="PubMed" id="15642342"/>
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    <scope>INTERACTION WITH HERC1</scope>
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    <scope>INTERACTION WITH ARHGAP21</scope>
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      <dbReference type="PubMed" id="16737952"/>
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    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>MUTAGENESIS OF THR-27 AND GLN-67</scope>
    <scope>INTERACTION WITH ASAP3</scope>
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      <dbReference type="PubMed" id="17030804"/>
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    <scope>INTERACTION WITH RAB11FIP3 AND RAB11FIP4</scope>
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    <scope>MUTAGENESIS OF THR-27</scope>
    <scope>SUBCELLULAR LOCATION</scope>
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    <scope>INTERACTION WITH NCS1</scope>
    <scope>SUBCELLULAR LOCATION</scope>
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    <scope>SUBCELLULAR LOCATION</scope>
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    <scope>FUNCTION</scope>
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    <scope>INTERACTION WITH CD36</scope>
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  <comment type="function">
    <text evidence="1 2 4 8 12 14 19 25 31 32 33 35 36">GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling (PubMed:11266366, PubMed:16737952, PubMed:18400762, PubMed:21170023, PubMed:32103017, PubMed:7589240). GTP-bound form plays an important role in the transport of multiple palmitoylated proteins form the Golgi to the plasma membrane (PubMed:37461827). Required for normal completion of mitotic cytokinesis (By similarity). Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers (By similarity). Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension (PubMed:14978216). Potentiates the neurite outgrowth in primary neurons by interacting with the molecular adapter APBB1 (PubMed:36250347). Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization (PubMed:36017701). Regulates surface levels of adherens junction proteins such as CDH1 (By similarity). Required for NTRK1 sorting to the recycling pathway from early endosomes (By similarity).</text>
  </comment>
  <comment type="function">
    <text evidence="12">(Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.</text>
  </comment>
  <comment type="function">
    <text evidence="34">(Microbial infection) Plays a key role in the endocytosis of enterovirus 71 and thus viral entry into brain microvascular endothelial cells.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="31">
      <text>GTP + H2O = GDP + phosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19669"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="EC" id="3.6.5.2"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="31">
      <dbReference type="Rhea" id="RHEA:19670"/>
    </physiologicalReaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2 3 19 32">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). Activated by ASAP3. Inactivated by ACAP1 and ACAP2. Activated by NGF via NTRK1 (By similarity). Activated by PRKAA2 through its C-terminal regulatory domain (PubMed:36017701).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 5 6 9 10 11 13 14 15 17 18 20 22 23 24 26 29 32 33 35">Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392). Interacts with PIP5K1C (PubMed:12847086). Interacts with USP6 (via Rab-GAP TBC domain) (PubMed:15509780). Interacts with RAB11FIP3 and RAB11FIP4 (PubMed:16148947, PubMed:17030804, PubMed:17628206). Interacts with HERC1 (PubMed:15642342). Interacts with ARHGAP21 (PubMed:15793564). Interacts with ASAP3; the interaction is stabilized by calcium ions (PubMed:16737952, PubMed:20510928). Interacts with NCS1/FREQ at the plasma membrane (PubMed:17555535). Interacts with TBC1D24 (PubMed:20727515). Interacts with ECPAS (PubMed:20682791). Interacts with MICALL1 (PubMed:21951725). Interacts with SPAG9 homodimers, forming heterotetramers (PubMed:19644450). Interacts with CYTH3 (PubMed:23940353). Interacts with ASAP2 (By similarity). Interacts with UACA (By similarity). Interacts with KIF23, forming heterodimers and heterotetramers (By similarity). Interacts with C9orf72 (By similarity). Interacts (GTP-bound form) with TJAP1/PILT (By similarity). Interacts with PRKAA2 (PubMed:36017701). Interacts with CD36 (when palmitoylated); this interaction mediates CD36 transport from the Golgi to the plasma membrane (PubMed:37461827). Interacts with APBB1 (PubMed:36250347).</text>
  </comment>
  <comment type="subunit">
    <text evidence="12">(Microbial infection) Interacts with the V.cholerae enterotoxin subunit A1; this causes a conformation change so that the toxin can bind NAD and catalyze the ADP-ribosylation of Gs alpha.</text>
  </comment>
  <comment type="subunit">
    <text evidence="25 27">(Microbial infection) Interacts with EspG from enteropathogenic E.coli.</text>
  </comment>
  <comment type="subunit">
    <text evidence="27">(Microbial infection) Identified in a complex with RAB1A and EspG from enteropathogenic E.coli.</text>
  </comment>
  <comment type="subunit">
    <text evidence="34">(Microbial infection) Interacts with human enterovirus 71 protein VP1.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-81694">
      <id>O00213</id>
      <label>APBB1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>9</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-638194">
      <id>P53365</id>
      <label>ARFIP2</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>4</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-988663">
      <id>P21283</id>
      <label>ATP6V1C1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>4</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-447404">
      <id>Q9NZ52</id>
      <label>GGA3</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-306852">
      <id>Q02241</id>
      <label>KIF23</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>23</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-16439278">
      <id>Q6FHY5</id>
      <label>MEOX2</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-13301517">
      <id>Q96S97</id>
      <label>MYADM</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-21502566">
      <id>O60271-2</id>
      <label>SPAG9</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>8</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-10968870">
      <id>Q9ULP9-2</id>
      <label>TBC1D24</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-638181">
      <id>P62330</id>
    </interactant>
    <interactant intactId="EBI-25475891">
      <id>PRO_0000449632</id>
      <label>rep</label>
      <dbReference type="UniProtKB" id="P0DTD1"/>
    </interactant>
    <organismsDiffer>true</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="14 28 31 32 36">Cytoplasm</location>
      <location evidence="14 28 31 32 36">Cytosol</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="14 16 17 31 32 34">Cell membrane</location>
      <topology evidence="31 36">Lipid-anchor</topology>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="21 23 26">Endosome membrane</location>
      <topology evidence="31 36">Lipid-anchor</topology>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="26">Recycling endosome membrane</location>
      <topology evidence="31 36">Lipid-anchor</topology>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="8">Cell projection</location>
      <location evidence="8">Filopodium membrane</location>
      <topology evidence="31 36">Lipid-anchor</topology>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="14">Cell projection</location>
      <location evidence="14">Ruffle</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="28">Cleavage furrow</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="28">Midbody</location>
      <location evidence="28">Midbody ring</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Early endosome membrane</location>
      <topology evidence="1">Lipid-anchor</topology>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Golgi apparatus</location>
      <location evidence="1">trans-Golgi network membrane</location>
      <topology evidence="1">Lipid-anchor</topology>
    </subcellularLocation>
    <text evidence="16 21 28 31 36">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 (PubMed:23603394). Recruitment to the midbody ring requires both activation by PSD/EFA6A and interaction with KIF23/MKLP1 (PubMed:23603394). 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:23603394). Recruited to the cell membrane in association with CYTH2 and ARL4C (PubMed:17398095). Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles (PubMed:19948740). Myristoylation is required for proper localization to membranes: myristoylation on Lys-3 allows ARF6 to remain on membranes during the GTPase cycle (PubMed:32103017, PubMed:7589240).</text>
  </comment>
  <comment type="tissue specificity">
    <text evidence="7">Ubiquitous, with higher levels in heart, substantia nigra, and kidney.</text>
  </comment>
  <comment type="PTM">
    <text evidence="31">GTP-bound form is myristoylated on Lys-3 by NMT1 and NMT2, allowing ARF6 to remain on membranes during the GTPase cycle, thereby promoting its activity (PubMed:32103017). GDP-bound inactive form is demyristoylated on Lys-3 by SIRT2 at early endosomes or endocytic recycling compartment to allow its efficient activation by a guanine exchange factor (GEF) after GDP release (PubMed:32103017).</text>
  </comment>
  <comment type="similarity">
    <text evidence="38">Belongs to the small GTPase superfamily. Arf family.</text>
  </comment>
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    <property type="molecule type" value="mRNA"/>
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    <property type="protein sequence ID" value="AAP50257.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="protein sequence ID" value="AAC39877.1"/>
    <property type="molecule type" value="mRNA"/>
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    <property type="protein sequence ID" value="AAM12599.1"/>
    <property type="molecule type" value="mRNA"/>
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    <property type="protein sequence ID" value="BAG36527.1"/>
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    <property type="protein sequence ID" value="CAG46762.1"/>
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    <property type="protein sequence ID" value="EAW65740.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="status" value="NOT_ANNOTATED_CDS"/>
    <property type="molecule type" value="mRNA"/>
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    <property type="molecule type" value="mRNA"/>
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    <property type="nucleotide sequence ID" value="NM_001663.4"/>
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    <property type="generic name" value="Myristic acid"/>
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    <property type="glycosylation" value="1 site, 1 O-linked glycan (1 site)"/>
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    <property type="gene designation" value="ARF6"/>
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  <sequence length="175" mass="20082" checksum="49E38E59AEA52B98" modified="2007-01-23" version="2">MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS</sequence>
</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>