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ADP-ribosylation factor 6

 ARF6_HUMAN              Reviewed;         175 AA.
P62330; P26438; Q6FGZ2;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 162.
RecName: Full=ADP-ribosylation factor 6;
Name=ARF6 {ECO:0000312|HGNC:HGNC:659};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1993656;
Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.;
"Molecular identification of ADP-ribosylation factor mRNAs and their
expression in mammalian cells.";
J. Biol. Chem. 266:2772-2777(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=14659046; DOI=10.1089/104454903770946719;
Lebeda R.A., Johnson S.K., Stewart M.I., Haun R.S.;
"Sequence, genomic organization, and expression of the human ADP-
ribosylation factor 6 (ARF6) gene: a class III ARF.";
DNA Cell Biol. 22:737-741(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin, and Uterus;
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).
[9]
MYRISTOYLATION AT GLY-2, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF GLY-2.
PubMed=7589240; DOI=10.1006/excr.1995.1362;
D'Souza-Schorey C., Stahl P.D.;
"Myristoylation is required for the intracellular localization and
endocytic function of ARF6.";
Exp. Cell Res. 221:153-159(1995).
[10]
ENZYME REGULATION.
TISSUE=Leukocyte;
PubMed=11062263; DOI=10.1083/jcb.151.3.627;
Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J.,
Hsu V.W., Donaldson J.G., Randazzo P.A.;
"ACAPs are arf6 GTPase-activating proteins that function in the cell
periphery.";
J. Cell Biol. 151:627-638(2000).
[11]
INTERACTION WITH PIP5K1C.
PubMed=12847086; DOI=10.1083/jcb.200301006;
Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.;
"ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by
activating phosphatidylinositol phosphate kinase type Igamma.";
J. Cell Biol. 162:113-124(2003).
[12]
INTERACTION WITH USP6.
PubMed=15509780; DOI=10.1128/MCB.24.22.9752-9762.2004;
Martinu L., Masuda-Robens J.M., Robertson S.E., Santy L.C.,
Casanova J.E., Chou M.M.;
"The TBC (Tre-2/Bub2/Cdc16) domain protein TRE17 regulates plasma
membrane-endosomal trafficking through activation of Arf6.";
Mol. Cell. Biol. 24:9752-9762(2004).
[13]
FUNCTION, AND MUTAGENESIS OF THR-27 AND GLN-67.
PubMed=14978216; DOI=10.1091/mbc.E03-07-0493;
Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
"Regulation of dendritic branching and filopodia formation in
hippocampal neurons by specific acylated protein motifs.";
Mol. Biol. Cell 15:2205-2217(2004).
[14]
INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X.,
Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
"Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control
membrane traffic in cytokinesis.";
EMBO J. 24:3389-3399(2005).
[15]
INTERACTION WITH HERC1.
PubMed=15642342; DOI=10.1016/j.febslet.2004.11.095;
Garcia-Gonzalo F.R., Bartrons R., Ventura F., Rosa J.L.;
"Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-
mediated guanine nucleotide release from ARF proteins.";
FEBS Lett. 579:343-348(2005).
[16]
INTERACTION WITH ARHGAP21.
PubMed=15793564; DOI=10.1038/ncb1244;
Dubois T., Paleotti O., Mironov A.A. Jr., Fraisier V., Stradal T.E.B.,
De Matteis M.A., Franco M., Chavrier P.;
"Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control
Arp2/3 complex and F-actin dynamics.";
Nat. Cell Biol. 7:353-364(2005).
[17]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-27 AND GLN-67, AND
INTERACTION WITH ASAP3.
PubMed=16737952; DOI=10.1074/mcp.M600050-MCP200;
Fang Z., Miao Y., Ding X., Deng H., Liu S., Wang F., Zhou R.,
Watson C., Fu C., Hu Q., Lillard J.W. Jr., Powell M., Chen Y.,
Forte J.G., Yao X.;
"Proteomic identification and functional characterization of a novel
ARF6 GTPase-activating protein, ACAP4.";
Mol. Cell. Proteomics 5:1437-1449(2006).
[18]
INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
PubMed=17030804; DOI=10.1073/pnas.0605357103;
Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
Wakatsuki S.;
"Structural basis for Rab11-dependent membrane recruitment of a family
of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
[19]
MUTAGENESIS OF THR-27, AND SUBCELLULAR LOCATION.
PubMed=17398095; DOI=10.1016/j.cub.2007.03.007;
Hofmann I., Thompson A., Sanderson C.M., Munro S.;
"The Arl4 family of small G proteins can recruit the cytohesin Arf6
exchange factors to the plasma membrane.";
Curr. Biol. 17:711-716(2007).
[20]
INTERACTION WITH RAB11FIP3.
PubMed=17628206; DOI=10.1016/j.ejcb.2007.05.004;
Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R.,
Sentz D., Holmes R.K., Prekeris R.;
"Molecular characterization of Rab11-FIP3 binding to ARF GTPases.";
Eur. J. Cell Biol. 86:417-431(2007).
[21]
INTERACTION WITH NCS1, AND SUBCELLULAR LOCATION.
PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
"Specificity, promiscuity and localization of ARF protein interactions
with NCS-1 and phosphatidylinositol-4 kinase-III beta.";
Traffic 8:1080-1092(2007).
[22]
FUNCTION, AND ENZYME REGULATION.
PubMed=18400762; DOI=10.1074/jbc.M709717200;
Ha V.L., Bharti S., Inoue H., Vass W.C., Campa F., Nie Z.,
de Gramont A., Ward Y., Randazzo P.A.;
"ASAP3 is a focal adhesion-associated Arf GAP that functions in cell
migration and invasion.";
J. Biol. Chem. 283:14915-14926(2008).
[23]
INTERACTION WITH TBC1D24.
PubMed=20727515; DOI=10.1016/j.ajhg.2010.07.020;
Falace A., Filipello F., La Padula V., Vanni N., Madia F.,
De Pietri Tonelli D., de Falco F.A., Striano P., Dagna Bricarelli F.,
Minetti C., Benfenati F., Fassio A., Zara F.;
"TBC1D24, an ARF6-interacting protein, is mutated in familial
infantile myoclonic epilepsy.";
Am. J. Hum. Genet. 87:365-370(2010).
[24]
SUBCELLULAR LOCATION.
PubMed=19948740; DOI=10.1074/jbc.M109.069385;
Wan T., Liu T., Zhang H., Tang S., Min W.;
"AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.";
J. Biol. Chem. 285:3750-3757(2010).
[25]
SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
PubMed=20682791; DOI=10.1074/jbc.M110.154120;
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
Hughes R.E., Rechsteiner M.;
"A protein interaction network for Ecm29 links the 26 S proteasome to
molecular motors and endosomal components.";
J. Biol. Chem. 285:31616-31633(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
INTERACTION WITH MICALL1, AND SUBCELLULAR LOCATION.
PubMed=21951725; DOI=10.1111/j.1600-0854.2011.01294.x;
Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.;
"MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and
Arf6 with Rab8a.";
Traffic 13:82-93(2012).
[28]
SUBCELLULAR LOCATION.
PubMed=23603394; DOI=10.1016/j.febslet.2013.03.042;
Ueda T., Hanai A., Takei T., Kubo K., Ohgi M., Sakagami H.,
Takahashi S., Shin H.W., Nakayama K.;
"EFA6 activates Arf6 and participates in its targeting to the Flemming
body during cytokinesis.";
FEBS Lett. 587:1617-1623(2013).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH GDP.
PubMed=10881192; DOI=10.1038/75863;
Menetrey J., Macia E., Pasqualato S., Franco M., Cherfils J.;
"Structure of Arf6-GDP suggests a basis for guanine nucleotide
exchange factors specificity.";
Nat. Struct. Biol. 7:466-469(2000).
[33]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, AND
FUNCTION.
PubMed=11266366; DOI=10.1093/embo-reports/kve043;
Pasqualato S., Menetrey J., Franco M., Cherfils J.;
"The structural GDP/GTP cycle of human Arf6.";
EMBO Rep. 2:234-238(2001).
[34]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND
V.CHOLERAE ENTEROTOXIN SUBUNIT A1, SUBUNIT, AND FUNCTION (MICROBIAL
INFECTION).
PubMed=16099990; DOI=10.1126/science.1113398;
O'Neal C.J., Jobling M.G., Holmes R.K., Hol W.G.;
"Structural basis for the activation of cholera toxin by human ARF6-
GTP.";
Science 309:1093-1096(2005).
[35]
STRUCTURE BY NMR OF 2-11.
PubMed=16839550; DOI=10.1016/j.febslet.2006.06.086;
Gizachew D., Oswald R.;
"NMR structural studies of the myristoylated N-terminus of ADP
ribosylation factor 6 (Arf6).";
FEBS Lett. 580:4296-4301(2006).
[36]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 13-175 IN COMPLEX WITH GTP
AND SPAG9, AND INTERACTION WITH SPAG9.
PubMed=19644450; DOI=10.1038/emboj.2009.209;
Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F.,
England P., Franco M., Chavrier P., Houdusse A., Menetrey J.;
"The structural basis of Arf effector specificity: the crystal
structure of ARF6 in a complex with JIP4.";
EMBO J. 28:2835-2845(2009).
[37]
X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 11-175 IN COMPLEX WITH GDP
ASAP3 AND CALCIUM IONS, AND INTERACTION WITH ASAP3.
PubMed=20510928; DOI=10.1016/j.cell.2010.03.051;
Ismail S.A., Vetter I.R., Sot B., Wittinghofer A.;
"The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory
mechanism.";
Cell 141:812-821(2010).
[38]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 14-175 IN COMPLEX WITH GTP
AND E.COLI ESPG, FUNCTION, AND SUBUNIT.
PubMed=21170023; DOI=10.1038/nature09593;
Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C.,
Bresson S.M., Tomchick D.R., Alto N.M.;
"The assembly of a GTPase-kinase signalling complex by a bacterial
catalytic scaffold.";
Nature 469:107-111(2011).
[39]
X-RAY CRYSTALLOGRAPHY (4.10 ANGSTROMS) OF 14-173 IN COMPLEX WITH GTP;
RAB1A AND E.COLI ESPG, AND SUBUNIT.
PubMed=22939626; DOI=10.1016/j.cell.2012.06.050;
Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.;
"Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1
inactivation to counteract host defenses.";
Cell 150:1029-1041(2012).
[40]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-173 IN COMPLEX WITH CYTH3
AND GTP, AND SUBUNIT.
PubMed=23940353; DOI=10.1073/pnas.1301883110;
Malaby A.W., van den Berg B., Lambright D.G.;
"Structural basis for membrane recruitment and allosteric activation
of cytohesin family Arf GTPase exchange factors.";
Proc. Natl. Acad. Sci. U.S.A. 110:14213-14218(2013).
-!- FUNCTION: GTP-binding protein involved in protein trafficking that
regulates endocytic recycling and cytoskeleton remodeling
(PubMed:11266366, PubMed:21170023, PubMed:16737952,
PubMed:7589240, PubMed:18400762). 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). 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
(PubMed:14978216). Plays an important role in membrane
trafficking, during junctional remodeling and epithelial
polarization. Regulates surface levels of adherens junction
proteins such as CDH1 (By similarity).
{ECO:0000250|UniProtKB:P62331, ECO:0000269|PubMed:11266366,
ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16099990,
ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:18400762,
ECO:0000269|PubMed:21170023, ECO:0000269|PubMed:7589240}.
-!- FUNCTION: (Microbial infection) Functions as an allosteric
activator of the cholera toxin catalytic subunit, an ADP-
ribosyltransferase. {ECO:0000269|PubMed:16099990}.
-!- ENZYME REGULATION: 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.
{ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:18400762}.
-!- SUBUNIT: 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
GGA1 (By similarity). Interacts with C9orf72 (By similarity).
{ECO:0000250|UniProtKB:P62331, ECO:0000250|UniProtKB:P62332,
ECO:0000269|PubMed:12847086, ECO:0000269|PubMed:15509780,
ECO:0000269|PubMed:15642342, ECO:0000269|PubMed:15793564,
ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:16737952,
ECO:0000269|PubMed:17030804, ECO:0000269|PubMed:17555535,
ECO:0000269|PubMed:17628206, ECO:0000269|PubMed:19644450,
ECO:0000269|PubMed:20510928, ECO:0000269|PubMed:20682791,
ECO:0000269|PubMed:20727515, ECO:0000269|PubMed:21951725,
ECO:0000269|PubMed:23940353}.
-!- SUBUNIT: (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. {ECO:0000269|PubMed:16099990}.
-!- SUBUNIT: (Microbial infection) Interacts with EspG from
enteropathogenic E.coli. {ECO:0000269|PubMed:21170023,
ECO:0000269|PubMed:22939626}.
-!- SUBUNIT: (Microbial infection) Identified in a complex with RAB1A
and EspG from enteropathogenic E.coli.
{ECO:0000269|PubMed:22939626}.
-!- INTERACTION:
P53365:ARFIP2; NbExp=4; IntAct=EBI-638181, EBI-638194;
P21283:ATP6V1C1; NbExp=4; IntAct=EBI-638181, EBI-988663;
Q02241:KIF23; NbExp=23; IntAct=EBI-638181, EBI-306852;
O60271:SPAG9; NbExp=8; IntAct=EBI-638181, EBI-1023301;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:23603394,
ECO:0000269|PubMed:7589240}. Cell membrane
{ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:17398095,
ECO:0000269|PubMed:17555535}; Lipid-anchor
{ECO:0000269|PubMed:7589240}. Endosome membrane
{ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20682791,
ECO:0000269|PubMed:21951725}; Lipid-anchor. Recycling endosome
membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cell
projection, filopodium membrane; Lipid-anchor. Cell projection,
ruffle {ECO:0000269|PubMed:16737952}. Cleavage furrow
{ECO:0000269|PubMed:23603394}. Midbody, Midbody ring
{ECO:0000269|PubMed:23603394}. 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 (PubMed:23603394). Recruitement to the midbody
ring requires both activation by PSD/EFA6A and interaction with
KIF23/MKLP1 (By similarity). 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. Colocalizes with DAB2IP at the
plasma membrane and endocytic vesicles (By similarity).
Myristoylation is required for proper localization to membranes
(PubMed:7589240). {ECO:0000250, ECO:0000250|UniProtKB:P62331,
ECO:0000269|PubMed:23603394, ECO:0000269|PubMed:7589240}.
-!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart,
substantia nigra, and kidney. {ECO:0000269|PubMed:14659046}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M57763; AAA90928.1; -; mRNA.
EMBL; AY296206; AAP50257.1; -; Genomic_DNA.
EMBL; AF047432; AAC39877.1; -; mRNA.
EMBL; AF493885; AAM12599.1; -; mRNA.
EMBL; AK313790; BAG36527.1; -; mRNA.
EMBL; CR541964; CAG46762.1; -; mRNA.
EMBL; CH471078; EAW65740.1; -; Genomic_DNA.
EMBL; BC002952; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC008918; AAH08918.1; -; mRNA.
CCDS; CCDS9695.1; -.
PIR; B23741; B23741.
RefSeq; NP_001654.1; NM_001663.3.
UniGene; Hs.525330; -.
UniGene; Hs.719973; -.
PDB; 1E0S; X-ray; 2.28 A; A=2-175.
PDB; 2A5D; X-ray; 1.80 A; A=1-175.
PDB; 2A5F; X-ray; 2.02 A; A=1-175.
PDB; 2A5G; X-ray; 2.66 A; A=1-175.
PDB; 2BAO; NMR; -; A=2-11.
PDB; 2BAU; NMR; -; A=2-11.
PDB; 2J5X; X-ray; 2.80 A; A/B=2-175.
PDB; 2W83; X-ray; 1.93 A; A/B/E=13-175.
PDB; 3LVQ; X-ray; 3.38 A; E=11-175.
PDB; 3LVR; X-ray; 3.38 A; E=11-175.
PDB; 3N5C; X-ray; 1.82 A; A/B=14-175.
PDB; 3PCR; X-ray; 2.50 A; B=14-175.
PDB; 4FME; X-ray; 4.10 A; C/F=14-173.
PDB; 4KAX; X-ray; 1.85 A; A=14-173.
PDB; 6BBP; EM; 35.00 A; A=2-173.
PDB; 6BBQ; EM; 35.00 A; A=2-173.
PDBsum; 1E0S; -.
PDBsum; 2A5D; -.
PDBsum; 2A5F; -.
PDBsum; 2A5G; -.
PDBsum; 2BAO; -.
PDBsum; 2BAU; -.
PDBsum; 2J5X; -.
PDBsum; 2W83; -.
PDBsum; 3LVQ; -.
PDBsum; 3LVR; -.
PDBsum; 3N5C; -.
PDBsum; 3PCR; -.
PDBsum; 4FME; -.
PDBsum; 4KAX; -.
PDBsum; 6BBP; -.
PDBsum; 6BBQ; -.
ProteinModelPortal; P62330; -.
SMR; P62330; -.
BioGrid; 106877; 70.
DIP; DIP-33352N; -.
IntAct; P62330; 26.
MINT; P62330; -.
STRING; 9606.ENSP00000298316; -.
ChEMBL; CHEMBL5987; -.
DrugBank; DB01864; 5'-Guanosine-Diphosphate-Monothiophosphate.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
DrugBank; DB08231; MYRISTIC ACID.
iPTMnet; P62330; -.
PhosphoSitePlus; P62330; -.
SwissPalm; P62330; -.
BioMuta; ARF6; -.
DMDM; 51316984; -.
EPD; P62330; -.
MaxQB; P62330; -.
PaxDb; P62330; -.
PeptideAtlas; P62330; -.
PRIDE; P62330; -.
ProteomicsDB; 57396; -.
TopDownProteomics; P62330; -.
DNASU; 382; -.
Ensembl; ENST00000298316; ENSP00000298316; ENSG00000165527.
GeneID; 382; -.
KEGG; hsa:382; -.
UCSC; uc001wxg.5; human.
CTD; 382; -.
DisGeNET; 382; -.
EuPathDB; HostDB:ENSG00000165527.6; -.
GeneCards; ARF6; -.
HGNC; HGNC:659; ARF6.
HPA; CAB002778; -.
MIM; 600464; gene.
neXtProt; NX_P62330; -.
OpenTargets; ENSG00000165527; -.
PharmGKB; PA24942; -.
eggNOG; KOG0071; Eukaryota.
eggNOG; ENOG410XP1U; LUCA.
GeneTree; ENSGT00780000121855; -.
HOGENOM; HOG000163691; -.
HOVERGEN; HBG002073; -.
InParanoid; P62330; -.
KO; K07941; -.
OMA; IQDREMK; -.
OrthoDB; EOG091G0OXD; -.
PhylomeDB; P62330; -.
TreeFam; TF300808; -.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8875656; MET receptor recycling.
SignaLink; P62330; -.
SIGNOR; P62330; -.
ChiTaRS; ARF6; human.
EvolutionaryTrace; P62330; -.
GeneWiki; ARF6; -.
GenomeRNAi; 382; -.
PRO; PR:P62330; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000165527; -.
CleanEx; HS_ARF6; -.
Genevisible; P62330; HS.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0032456; P:endocytic recycling; IDA:UniProtKB.
GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0033028; P:myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; TAS:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB.
GO; GO:0097178; P:ruffle assembly; IDA:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB.
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:0000269|PubMed:25255805}.
CHAIN 2 175 ADP-ribosylation factor 6.
/FTId=PRO_0000207400.
NP_BIND 23 28 GTP. {ECO:0000269|PubMed:16099990,
ECO:0000269|PubMed:19644450,
ECO:0000269|PubMed:21170023,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23940353}.
NP_BIND 41 44 GTP. {ECO:0000269|PubMed:16099990,
ECO:0000269|PubMed:19644450,
ECO:0000269|PubMed:21170023,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23940353}.
NP_BIND 63 67 GTP. {ECO:0000269|PubMed:16099990,
ECO:0000269|PubMed:19644450,
ECO:0000269|PubMed:21170023,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23940353}.
NP_BIND 122 125 GTP. {ECO:0000269|PubMed:16099990,
ECO:0000269|PubMed:19644450,
ECO:0000269|PubMed:21170023,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23940353}.
NP_BIND 155 156 GTP. {ECO:0000269|PubMed:16099990,
ECO:0000269|PubMed:19644450,
ECO:0000269|PubMed:21170023,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23940353}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:7589240}.
MUTAGEN 2 2 G->A: Fails to associate with membranes.
{ECO:0000269|PubMed:7589240}.
MUTAGEN 27 27 T->N: Fails to associate with membranes.
Does not inhibit filopodia formation.
{ECO:0000269|PubMed:14978216,
ECO:0000269|PubMed:16737952,
ECO:0000269|PubMed:17398095}.
MUTAGEN 67 67 Q->L: Inhibits filopodia formation and
dendritic branching.
{ECO:0000269|PubMed:14978216,
ECO:0000269|PubMed:16737952}.
HELIX 3 9 {ECO:0000244|PDB:1E0S}.
STRAND 13 19 {ECO:0000244|PDB:2A5D}.
HELIX 26 35 {ECO:0000244|PDB:2A5D}.
STRAND 39 44 {ECO:0000244|PDB:1E0S}.
STRAND 45 54 {ECO:0000244|PDB:2A5D}.
STRAND 57 64 {ECO:0000244|PDB:2A5D}.
HELIX 65 67 {ECO:0000244|PDB:3N5C}.
HELIX 68 77 {ECO:0000244|PDB:2A5D}.
TURN 78 80 {ECO:0000244|PDB:1E0S}.
STRAND 83 89 {ECO:0000244|PDB:2A5D}.
HELIX 93 95 {ECO:0000244|PDB:2A5D}.
HELIX 96 107 {ECO:0000244|PDB:2A5D}.
HELIX 110 112 {ECO:0000244|PDB:2A5D}.
STRAND 116 122 {ECO:0000244|PDB:2A5D}.
STRAND 125 128 {ECO:0000244|PDB:3LVQ}.
HELIX 132 138 {ECO:0000244|PDB:2A5D}.
HELIX 141 143 {ECO:0000244|PDB:2A5D}.
STRAND 149 153 {ECO:0000244|PDB:2A5D}.
TURN 156 159 {ECO:0000244|PDB:2A5D}.
HELIX 162 172 {ECO:0000244|PDB:2A5D}.
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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