ARF6_HUMAN
ID ARF6_HUMAN Reviewed; 175 AA.
AC P62330; P26438; Q6FGZ2;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=ADP-ribosylation factor 6 {ECO:0000303|Ref.6};
DE EC=3.6.5.2 {ECO:0000269|PubMed:32103017};
GN Name=ARF6 {ECO:0000303|Ref.6, ECO:0000312|HGNC:HGNC:659};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1993656; DOI=10.1016/s0021-9258(18)49913-9;
RA Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.;
RT "Molecular identification of ADP-ribosylation factor mRNAs and their
RT expression in mammalian cells.";
RL J. Biol. Chem. 266:2772-2777(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=14659046; DOI=10.1089/104454903770946719;
RA Lebeda R.A., Johnson S.K., Stewart M.I., Haun R.S.;
RT "Sequence, genomic organization, and expression of the human ADP-
RT ribosylation factor 6 (ARF6) gene: a class III ARF.";
RL DNA Cell Biol. 22:737-741(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [9]
RP MYRISTOYLATION AT GLY-2, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-2.
RX PubMed=7589240; DOI=10.1006/excr.1995.1362;
RA D'Souza-Schorey C., Stahl P.D.;
RT "Myristoylation is required for the intracellular localization and
RT endocytic function of ARF6.";
RL Exp. Cell Res. 221:153-159(1995).
RN [10]
RP ACTIVITY REGULATION.
RC TISSUE=Leukocyte;
RX PubMed=11062263; DOI=10.1083/jcb.151.3.627;
RA Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W.,
RA Donaldson J.G., Randazzo P.A.;
RT "ACAPs are arf6 GTPase-activating proteins that function in the cell
RT periphery.";
RL J. Cell Biol. 151:627-638(2000).
RN [11]
RP INTERACTION WITH GGA1; GGA2 AND GGA3.
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 [12]
RP INTERACTION WITH PIP5K1C.
RX PubMed=12847086; DOI=10.1083/jcb.200301006;
RA Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.;
RT "ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by
RT activating phosphatidylinositol phosphate kinase type Igamma.";
RL J. Cell Biol. 162:113-124(2003).
RN [13]
RP INTERACTION WITH USP6.
RX PubMed=15509780; DOI=10.1128/mcb.24.22.9752-9762.2004;
RA Martinu L., Masuda-Robens J.M., Robertson S.E., Santy L.C., Casanova J.E.,
RA Chou M.M.;
RT "The TBC (Tre-2/Bub2/Cdc16) domain protein TRE17 regulates plasma membrane-
RT endosomal trafficking through activation of Arf6.";
RL Mol. Cell. Biol. 24:9752-9762(2004).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-27 AND GLN-67.
RX PubMed=14978216; DOI=10.1091/mbc.e03-07-0493;
RA Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
RT "Regulation of dendritic branching and filopodia formation in hippocampal
RT neurons by specific acylated protein motifs.";
RL Mol. Biol. Cell 15:2205-2217(2004).
RN [15]
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
RX PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
RA Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R.,
RA Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane
RT traffic in cytokinesis.";
RL EMBO J. 24:3389-3399(2005).
RN [16]
RP INTERACTION WITH HERC1.
RX PubMed=15642342; DOI=10.1016/j.febslet.2004.11.095;
RA Garcia-Gonzalo F.R., Bartrons R., Ventura F., Rosa J.L.;
RT "Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated
RT guanine nucleotide release from ARF proteins.";
RL FEBS Lett. 579:343-348(2005).
RN [17]
RP INTERACTION WITH ARHGAP21.
RX PubMed=15793564; DOI=10.1038/ncb1244;
RA Dubois T., Paleotti O., Mironov A.A. Jr., Fraisier V., Stradal T.E.B.,
RA De Matteis M.A., Franco M., Chavrier P.;
RT "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control
RT Arp2/3 complex and F-actin dynamics.";
RL Nat. Cell Biol. 7:353-364(2005).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-27 AND GLN-67, AND
RP INTERACTION WITH ASAP3.
RX PubMed=16737952; DOI=10.1074/mcp.m600050-mcp200;
RA Fang Z., Miao Y., Ding X., Deng H., Liu S., Wang F., Zhou R., Watson C.,
RA Fu C., Hu Q., Lillard J.W. Jr., Powell M., Chen Y., Forte J.G., Yao X.;
RT "Proteomic identification and functional characterization of a novel ARF6
RT GTPase-activating protein, ACAP4.";
RL Mol. Cell. Proteomics 5:1437-1449(2006).
RN [19]
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
RX PubMed=17030804; DOI=10.1073/pnas.0605357103;
RA Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
RA Wakatsuki S.;
RT "Structural basis for Rab11-dependent membrane recruitment of a family of
RT Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
RN [20]
RP MUTAGENESIS OF THR-27, AND SUBCELLULAR LOCATION.
RX PubMed=17398095; DOI=10.1016/j.cub.2007.03.007;
RA Hofmann I., Thompson A., Sanderson C.M., Munro S.;
RT "The Arl4 family of small G proteins can recruit the cytohesin Arf6
RT exchange factors to the plasma membrane.";
RL Curr. Biol. 17:711-716(2007).
RN [21]
RP INTERACTION WITH RAB11FIP3.
RX PubMed=17628206; DOI=10.1016/j.ejcb.2007.05.004;
RA Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R., Sentz D.,
RA Holmes R.K., Prekeris R.;
RT "Molecular characterization of Rab11-FIP3 binding to ARF GTPases.";
RL Eur. J. Cell Biol. 86:417-431(2007).
RN [22]
RP INTERACTION WITH NCS1, AND SUBCELLULAR LOCATION.
RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT "Specificity, promiscuity and localization of ARF protein interactions with
RT NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL Traffic 8:1080-1092(2007).
RN [23]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=18400762; DOI=10.1074/jbc.m709717200;
RA Ha V.L., Bharti S., Inoue H., Vass W.C., Campa F., Nie Z., de Gramont A.,
RA Ward Y., Randazzo P.A.;
RT "ASAP3 is a focal adhesion-associated Arf GAP that functions in cell
RT migration and invasion.";
RL J. Biol. Chem. 283:14915-14926(2008).
RN [24]
RP INTERACTION WITH TBC1D24.
RX PubMed=20727515; DOI=10.1016/j.ajhg.2010.07.020;
RA Falace A., Filipello F., La Padula V., Vanni N., Madia F.,
RA De Pietri Tonelli D., de Falco F.A., Striano P., Dagna Bricarelli F.,
RA Minetti C., Benfenati F., Fassio A., Zara F.;
RT "TBC1D24, an ARF6-interacting protein, is mutated in familial infantile
RT myoclonic epilepsy.";
RL Am. J. Hum. Genet. 87:365-370(2010).
RN [25]
RP SUBCELLULAR LOCATION.
RX PubMed=19948740; DOI=10.1074/jbc.m109.069385;
RA Wan T., Liu T., Zhang H., Tang S., Min W.;
RT "AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.";
RL J. Biol. Chem. 285:3750-3757(2010).
RN [26]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP INTERACTION WITH MICALL1, AND SUBCELLULAR LOCATION.
RX PubMed=21951725; DOI=10.1111/j.1600-0854.2011.01294.x;
RA Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.;
RT "MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6
RT with Rab8a.";
RL Traffic 13:82-93(2012).
RN [29]
RP SUBCELLULAR LOCATION.
RX PubMed=23603394; DOI=10.1016/j.febslet.2013.03.042;
RA Ueda T., Hanai A., Takei T., Kubo K., Ohgi M., Sakagami H., Takahashi S.,
RA Shin H.W., Nakayama K.;
RT "EFA6 activates Arf6 and participates in its targeting to the Flemming body
RT during cytokinesis.";
RL FEBS Lett. 587:1617-1623(2013).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [33]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MYRISTOYLATION AT
RP LYS-3, AND MUTAGENESIS OF LYS-3; THR-27 AND GLN-67.
RX PubMed=32103017; DOI=10.1038/s41467-020-14893-x;
RA Kosciuk T., Price I.R., Zhang X., Zhu C., Johnson K.N., Zhang S.,
RA Halaby S.L., Komaniecki G.P., Yang M., DeHart C.J., Thomas P.M.,
RA Kelleher N.L., Fromme J.C., Lin H.;
RT "NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase
RT cycle.";
RL Nat. Commun. 11:1067-1067(2020).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=10881192; DOI=10.1038/75863;
RA Menetrey J., Macia E., Pasqualato S., Franco M., Cherfils J.;
RT "Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange
RT factors specificity.";
RL Nat. Struct. Biol. 7:466-469(2000).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, AND
RP FUNCTION.
RX PubMed=11266366; DOI=10.1093/embo-reports/kve043;
RA Pasqualato S., Menetrey J., Franco M., Cherfils J.;
RT "The structural GDP/GTP cycle of human Arf6.";
RL EMBO Rep. 2:234-238(2001).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND V.CHOLERAE
RP ENTEROTOXIN SUBUNIT A1, SUBUNIT, AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=16099990; DOI=10.1126/science.1113398;
RA O'Neal C.J., Jobling M.G., Holmes R.K., Hol W.G.;
RT "Structural basis for the activation of cholera toxin by human ARF6-GTP.";
RL Science 309:1093-1096(2005).
RN [37]
RP STRUCTURE BY NMR OF 2-11.
RX PubMed=16839550; DOI=10.1016/j.febslet.2006.06.086;
RA Gizachew D., Oswald R.;
RT "NMR structural studies of the myristoylated N-terminus of ADP ribosylation
RT factor 6 (Arf6).";
RL FEBS Lett. 580:4296-4301(2006).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 13-175 IN COMPLEX WITH GTP AND
RP SPAG9, AND INTERACTION WITH SPAG9.
RX PubMed=19644450; DOI=10.1038/emboj.2009.209;
RA Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F.,
RA England P., Franco M., Chavrier P., Houdusse A., Menetrey J.;
RT "The structural basis of Arf effector specificity: the crystal structure of
RT ARF6 in a complex with JIP4.";
RL EMBO J. 28:2835-2845(2009).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 11-175 IN COMPLEX WITH GDP ASAP3
RP AND CALCIUM IONS, AND INTERACTION WITH ASAP3.
RX PubMed=20510928; DOI=10.1016/j.cell.2010.03.051;
RA Ismail S.A., Vetter I.R., Sot B., Wittinghofer A.;
RT "The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory
RT mechanism.";
RL Cell 141:812-821(2010).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 14-175 IN COMPLEX WITH GTP AND
RP E.COLI ESPG, FUNCTION, AND SUBUNIT.
RX PubMed=21170023; DOI=10.1038/nature09593;
RA Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C.,
RA Bresson S.M., Tomchick D.R., Alto N.M.;
RT "The assembly of a GTPase-kinase signalling complex by a bacterial
RT catalytic scaffold.";
RL Nature 469:107-111(2011).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (4.10 ANGSTROMS) OF 14-173 IN COMPLEX WITH GTP; RAB1A
RP AND E.COLI ESPG, AND SUBUNIT.
RX PubMed=22939626; DOI=10.1016/j.cell.2012.06.050;
RA Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.;
RT "Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1
RT inactivation to counteract host defenses.";
RL Cell 150:1029-1041(2012).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-173 IN COMPLEX WITH CYTH3 AND
RP GTP, AND SUBUNIT.
RX PubMed=23940353; DOI=10.1073/pnas.1301883110;
RA Malaby A.W., van den Berg B., Lambright D.G.;
RT "Structural basis for membrane recruitment and allosteric activation of
RT cytohesin family Arf GTPase exchange factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14213-14218(2013).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking that
CC regulates endocytic recycling and cytoskeleton remodeling
CC (PubMed:11266366, PubMed:21170023, PubMed:16737952, PubMed:7589240,
CC PubMed:18400762, PubMed:32103017). Required for normal completion of
CC mitotic cytokinesis (By similarity). Plays a role in the reorganization
CC of the actin cytoskeleton and the formation of stress fibers (By
CC similarity). Involved in the regulation of dendritic spine development,
CC contributing to the regulation of dendritic branching and filopodia
CC extension (PubMed:14978216). Plays an important role in membrane
CC trafficking, during junctional remodeling and epithelial polarization.
CC Regulates surface levels of adherens junction proteins such as CDH1 (By
CC similarity). Required for NTRK1 sorting to the recycling pathway from
CC early endosomes (By similarity). {ECO:0000250|UniProtKB:P62331,
CC ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11266366,
CC ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16099990,
CC ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:18400762,
CC ECO:0000269|PubMed:21170023, ECO:0000269|PubMed:32103017,
CC ECO:0000269|PubMed:7589240}.
CC -!- FUNCTION: (Microbial infection) Functions as an allosteric activator of
CC the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
CC {ECO:0000269|PubMed:16099990}.
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:0000269|PubMed:32103017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:32103017};
CC -!- ACTIVITY REGULATION: Activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). Activated by
CC ASAP3. Inactivated by ACAP1 and ACAP2. Activated by NGF via NTRK1 (By
CC similarity). {ECO:0000250|UniProtKB:P62332,
CC ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:18400762}.
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). Interacts with PIP5K1C (PubMed:12847086).
CC Interacts with USP6 (via Rab-GAP TBC domain) (PubMed:15509780).
CC Interacts with RAB11FIP3 and RAB11FIP4 (PubMed:16148947,
CC PubMed:17030804, PubMed:17628206). Interacts with HERC1
CC (PubMed:15642342). Interacts with ARHGAP21 (PubMed:15793564). Interacts
CC with ASAP3; the interaction is stabilized by calcium ions
CC (PubMed:16737952, PubMed:20510928). Interacts with NCS1/FREQ at the
CC plasma membrane (PubMed:17555535). Interacts with TBC1D24
CC (PubMed:20727515). Interacts with ECPAS (PubMed:20682791). Interacts
CC with MICALL1 (PubMed:21951725). Interacts with SPAG9 homodimers,
CC forming heterotetramers (PubMed:19644450). Interacts with CYTH3
CC (PubMed:23940353). Interacts with ASAP2 (By similarity). Interacts with
CC UACA (By similarity). Interacts with KIF23, forming heterodimers and
CC heterotetramers (By similarity). Interacts with C9orf72 (By
CC similarity). Interacts (GTP-bound form) with TJAP1/PILT (By
CC similarity). {ECO:0000250|UniProtKB:P62331,
CC ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11950392,
CC ECO:0000269|PubMed:12847086, ECO:0000269|PubMed:15509780,
CC ECO:0000269|PubMed:15642342, ECO:0000269|PubMed:15793564,
CC ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:16737952,
CC ECO:0000269|PubMed:17030804, ECO:0000269|PubMed:17555535,
CC ECO:0000269|PubMed:17628206, ECO:0000269|PubMed:19644450,
CC ECO:0000269|PubMed:20510928, ECO:0000269|PubMed:20682791,
CC ECO:0000269|PubMed:20727515, ECO:0000269|PubMed:21951725,
CC ECO:0000269|PubMed:23940353}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the V.cholerae
CC enterotoxin subunit A1; this causes a conformation change so that the
CC toxin can bind NAD and catalyze the ADP-ribosylation of Gs alpha.
CC {ECO:0000269|PubMed:16099990}.
CC -!- SUBUNIT: (Microbial infection) Interacts with EspG from
CC enteropathogenic E.coli. {ECO:0000269|PubMed:21170023,
CC ECO:0000269|PubMed:22939626}.
CC -!- SUBUNIT: (Microbial infection) Identified in a complex with RAB1A and
CC EspG from enteropathogenic E.coli. {ECO:0000269|PubMed:22939626}.
CC -!- INTERACTION:
CC P62330; O00213: APBB1; NbExp=9; IntAct=EBI-638181, EBI-81694;
CC P62330; P53365: ARFIP2; NbExp=4; IntAct=EBI-638181, EBI-638194;
CC P62330; P21283: ATP6V1C1; NbExp=4; IntAct=EBI-638181, EBI-988663;
CC P62330; Q9NZ52: GGA3; NbExp=3; IntAct=EBI-638181, EBI-447404;
CC P62330; Q02241: KIF23; NbExp=23; IntAct=EBI-638181, EBI-306852;
CC P62330; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-638181, EBI-16439278;
CC P62330; O60271: SPAG9; NbExp=8; IntAct=EBI-638181, EBI-1023301;
CC P62330; Q9ULP9-2: TBC1D24; NbExp=2; IntAct=EBI-638181, EBI-10968870;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16737952,
CC ECO:0000269|PubMed:23603394, ECO:0000269|PubMed:32103017,
CC ECO:0000269|PubMed:7589240}. Cell membrane
CC {ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:17398095,
CC ECO:0000269|PubMed:17555535, ECO:0000269|PubMed:32103017}; Lipid-anchor
CC {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Endosome
CC membrane {ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20682791,
CC ECO:0000269|PubMed:21951725}; Lipid-anchor
CC {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Recycling
CC endosome membrane {ECO:0000269|PubMed:21951725}; Lipid-anchor
CC {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Cell
CC projection, filopodium membrane {ECO:0000269|PubMed:14978216}; Lipid-
CC anchor {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Cell
CC projection, ruffle {ECO:0000269|PubMed:16737952}. Cleavage furrow
CC {ECO:0000269|PubMed:23603394}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:23603394}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P62331}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62331}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:P62331}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62331}. Note=Distributed uniformly on the
CC plasma membrane, as well as throughout the cytoplasm during metaphase.
CC Subsequently concentrated at patches in the equatorial region at the
CC onset of cytokinesis, and becomes distributed in the equatorial region
CC concurrent with cleavage furrow ingression. In late stages of
CC cytokinesis, concentrates at the midbody ring/Flemming body
CC (PubMed:23603394). Recruitment to the midbody ring requires both
CC activation by PSD/EFA6A and interaction with KIF23/MKLP1
CC (PubMed:23603394). 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:23603394). Recruited to the cell membrane in association with
CC CYTH2 and ARL4C (PubMed:17398095). Colocalizes with DAB2IP at the
CC plasma membrane and endocytic vesicles (PubMed:19948740).
CC Myristoylation is required for proper localization to membranes:
CC myristoylation on Lys-3 allows ARF6 to remain on membranes during the
CC GTPase cycle (PubMed:7589240, PubMed:32103017).
CC {ECO:0000269|PubMed:17398095, ECO:0000269|PubMed:19948740,
CC ECO:0000269|PubMed:23603394, ECO:0000269|PubMed:32103017,
CC ECO:0000269|PubMed:7589240}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, substantia
CC nigra, and kidney. {ECO:0000269|PubMed:14659046}.
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 (PubMed:32103017). GDP-bound inactive form is
CC demyristoylated on Lys-3 by SIRT2 at early endosomes or endocytic
CC recycling compartment to allow its efficient activation by a guanine
CC exchange factor (GEF) after GDP release (PubMed:32103017).
CC {ECO:0000269|PubMed:32103017}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; M57763; AAA90928.1; -; mRNA.
DR EMBL; AY296206; AAP50257.1; -; Genomic_DNA.
DR EMBL; AF047432; AAC39877.1; -; mRNA.
DR EMBL; AF493885; AAM12599.1; -; mRNA.
DR EMBL; AK313790; BAG36527.1; -; mRNA.
DR EMBL; CR541964; CAG46762.1; -; mRNA.
DR EMBL; CH471078; EAW65740.1; -; Genomic_DNA.
DR EMBL; BC002952; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC008918; AAH08918.1; -; mRNA.
DR CCDS; CCDS9695.1; -.
DR PIR; B23741; B23741.
DR RefSeq; NP_001654.1; NM_001663.3.
DR PDB; 1E0S; X-ray; 2.28 A; A=2-175.
DR PDB; 2A5D; X-ray; 1.80 A; A=1-175.
DR PDB; 2A5F; X-ray; 2.02 A; A=1-175.
DR PDB; 2A5G; X-ray; 2.66 A; A=1-175.
DR PDB; 2BAO; NMR; -; A=2-11.
DR PDB; 2BAU; NMR; -; A=2-11.
DR PDB; 2J5X; X-ray; 2.80 A; A/B=2-175.
DR PDB; 2W83; X-ray; 1.93 A; A/B/E=13-175.
DR PDB; 3LVQ; X-ray; 3.38 A; E=11-175.
DR PDB; 3LVR; X-ray; 3.38 A; E=11-175.
DR PDB; 3N5C; X-ray; 1.82 A; A/B=14-175.
DR PDB; 3PCR; X-ray; 2.50 A; B=14-175.
DR PDB; 4FME; X-ray; 4.10 A; C/F=14-173.
DR PDB; 4KAX; X-ray; 1.85 A; A=14-173.
DR PDB; 6BBP; EM; 35.00 A; A=2-173.
DR PDB; 6BBQ; EM; 35.00 A; A=2-173.
DR PDB; 6PAU; X-ray; 1.93 A; C=3-9.
DR PDBsum; 1E0S; -.
DR PDBsum; 2A5D; -.
DR PDBsum; 2A5F; -.
DR PDBsum; 2A5G; -.
DR PDBsum; 2BAO; -.
DR PDBsum; 2BAU; -.
DR PDBsum; 2J5X; -.
DR PDBsum; 2W83; -.
DR PDBsum; 3LVQ; -.
DR PDBsum; 3LVR; -.
DR PDBsum; 3N5C; -.
DR PDBsum; 3PCR; -.
DR PDBsum; 4FME; -.
DR PDBsum; 4KAX; -.
DR PDBsum; 6BBP; -.
DR PDBsum; 6BBQ; -.
DR PDBsum; 6PAU; -.
DR AlphaFoldDB; P62330; -.
DR SMR; P62330; -.
DR BioGRID; 106877; 521.
DR DIP; DIP-33352N; -.
DR IntAct; P62330; 46.
DR MINT; P62330; -.
DR STRING; 9606.ENSP00000298316; -.
DR BindingDB; P62330; -.
DR ChEMBL; CHEMBL5987; -.
DR DrugBank; DB01864; 5'-Guanosine-Diphosphate-Monothiophosphate.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB08231; Myristic acid.
DR iPTMnet; P62330; -.
DR PhosphoSitePlus; P62330; -.
DR SwissPalm; P62330; -.
DR BioMuta; ARF6; -.
DR DMDM; 51316984; -.
DR EPD; P62330; -.
DR jPOST; P62330; -.
DR MassIVE; P62330; -.
DR MaxQB; P62330; -.
DR PaxDb; P62330; -.
DR PeptideAtlas; P62330; -.
DR PRIDE; P62330; -.
DR ProteomicsDB; 57396; -.
DR TopDownProteomics; P62330; -.
DR Antibodypedia; 3459; 474 antibodies from 37 providers.
DR DNASU; 382; -.
DR Ensembl; ENST00000298316.7; ENSP00000298316.5; ENSG00000165527.8.
DR Ensembl; ENST00000693319.1; ENSP00000510419.1; ENSG00000165527.8.
DR GeneID; 382; -.
DR KEGG; hsa:382; -.
DR MANE-Select; ENST00000298316.7; ENSP00000298316.5; NM_001663.4; NP_001654.1.
DR UCSC; uc001wxg.5; human.
DR CTD; 382; -.
DR DisGeNET; 382; -.
DR GeneCards; ARF6; -.
DR HGNC; HGNC:659; ARF6.
DR HPA; ENSG00000165527; Low tissue specificity.
DR MIM; 600464; gene.
DR neXtProt; NX_P62330; -.
DR OpenTargets; ENSG00000165527; -.
DR PharmGKB; PA24942; -.
DR VEuPathDB; HostDB:ENSG00000165527; -.
DR eggNOG; KOG0071; Eukaryota.
DR GeneTree; ENSGT00940000156593; -.
DR HOGENOM; CLU_040729_9_4_1; -.
DR InParanoid; P62330; -.
DR OMA; WSVIPTI; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P62330; -.
DR TreeFam; TF300808; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P62330; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8875656; MET receptor recycling.
DR SignaLink; P62330; -.
DR SIGNOR; P62330; -.
DR BioGRID-ORCS; 382; 108 hits in 1058 CRISPR screens.
DR ChiTaRS; ARF6; human.
DR EvolutionaryTrace; P62330; -.
DR GeneWiki; ARF6; -.
DR GenomeRNAi; 382; -.
DR Pharos; P62330; Tbio.
DR PRO; PR:P62330; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P62330; protein.
DR Bgee; ENSG00000165527; Expressed in esophagus squamous epithelium and 211 other tissues.
DR Genevisible; P62330; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IDA:UniProtKB.
DR GO; GO:1902217; P:erythrocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; IEA:Ensembl.
DR GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; TAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISS:ARUK-UCL.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISS:ARUK-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IDA:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04149; Arf6; 1.
DR DisProt; DP02815; -.
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:0000269|PubMed:25255805"
FT CHAIN 2..175
FT /note="ADP-ribosylation factor 6"
FT /id="PRO_0000207400"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16099990,
FT ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:21170023,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23940353"
FT BINDING 41..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16099990,
FT ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:21170023,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23940353"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16099990,
FT ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:21170023,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23940353"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16099990,
FT ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:21170023,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23940353"
FT BINDING 155..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16099990,
FT ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:21170023,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23940353"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:7589240"
FT LIPID 3
FT /note="N6-myristoyl lysine"
FT /evidence="ECO:0000269|PubMed:32103017"
FT MUTAGEN 2
FT /note="G->A: Fails to associate with membranes."
FT /evidence="ECO:0000269|PubMed:7589240"
FT MUTAGEN 3
FT /note="K->R: Abolished lysine-myristoylation, leading to
FT decreased localization to membranes."
FT /evidence="ECO:0000269|PubMed:32103017"
FT MUTAGEN 27
FT /note="T->N: Constitutively inactivated. Fails to associate
FT with membranes. Does not inhibit filopodia formation."
FT /evidence="ECO:0000269|PubMed:14978216,
FT ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:17398095,
FT ECO:0000269|PubMed:32103017"
FT MUTAGEN 67
FT /note="Q->L: Constitutively active. Inhibits filopodia
FT formation and dendritic branching."
FT /evidence="ECO:0000269|PubMed:14978216,
FT ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:32103017"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1E0S"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2A5D"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1E0S"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:2A5D"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3N5C"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:2A5D"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1E0S"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2A5D"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2A5D"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3LVQ"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2A5D"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2A5D"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:2A5D"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:2A5D"
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
