ARF6_DROME
ID ARF6_DROME Reviewed; 175 AA.
AC P40946; A4UZH7; Q0E966; Q9V7B0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ADP-ribosylation factor 6 {ECO:0000305};
DE Short=ARF6;
DE AltName: Full=ADP ribosylation factor at 51F {ECO:0000312|FlyBase:FBgn0013750};
DE AltName: Full=ADP-ribosylation factor 3 {ECO:0000303|PubMed:8063793};
GN Name=Arf51F {ECO:0000312|FlyBase:FBgn0013750};
GN Synonyms=Arf3 {ECO:0000303|PubMed:8063793},
GN Arf6 {ECO:0000312|FlyBase:FBgn0013750};
GN ORFNames=CG8156 {ECO:0000312|FlyBase:FBgn0013750};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8063793; DOI=10.1016/s0021-9258(17)31840-9;
RA Lee F.-J.S., Stevens L.A., Hall L.M., Murtagh J.J. Jr., Kao Y.L., Moss J.,
RA Vaughan M.;
RT "Characterization of class II and class III ADP-ribosylation factor genes
RT and proteins in Drosophila melanogaster.";
RL J. Biol. Chem. 269:21555-21560(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21976699; DOI=10.1091/mbc.e11-04-0305;
RA Johnson R.I., Sedgwick A., D'Souza-Schorey C., Cagan R.L.;
RT "Role for a Cindr-Arf6 axis in patterning emerging epithelia.";
RL Mol. Biol. Cell 22:4513-4526(2011).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28607459; DOI=10.1038/mp.2017.112;
RG IMAGEN Consortium;
RA Gonzalez D.A., Jia T., Pinzon J.H., Acevedo S.F., Ojelade S.A., Xu B.,
RA Tay N., Desrivieres S., Hernandez J.L., Banaschewski T., Buechel C.,
RA Bokde A.L.W., Conrod P.J., Flor H., Frouin V., Gallinat J., Garavan H.,
RA Gowland P.A., Heinz A., Ittermann B., Lathrop M., Martinot J.L., Paus T.,
RA Smolka M.N., Rodan A.R., Schumann G., Rothenfluh A.;
RT "The Arf6 activator Efa6/PSD3 confers regional specificity and modulates
RT ethanol consumption in Drosophila and humans.";
RL Mol. Psychiatry 23:621-628(2018).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus (By
CC similarity). Promotes cell movement and remodeling of the actin
CC cytoskeleton during compound eye morphogenesis (PubMed:21976699).
CC Required for normal ethanol-induced tolerance and preference
CC (PubMed:28607459). Probably after Efa6-mediated activation, counteracts
CC ethanol-induced sedation (PubMed:28607459).
CC {ECO:0000250|UniProtKB:P40945, ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:28607459}.
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) (By similarity).
CC May be activated by Efa6 (PubMed:28607459).
CC {ECO:0000250|UniProtKB:P62330, ECO:0000269|PubMed:28607459}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC -!- TISSUE SPECIFICITY: Expressed in the head (at protein level).
CC {ECO:0000269|PubMed:28607459}.
CC -!- DISRUPTION PHENOTYPE: Results in enhances preference and sensitivity to
CC alcohol (PubMed:28607459). Fails to develop tolerance to repeated
CC ethanol exposures (PubMed:28607459). Conditional RNAi-mediated
CC knockdown in the eye results in aberrant compound eye morphogenesis,
CC with defective cell intercalation patterns associated with altered
CC actin dynamics (PubMed:21976699). {ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:28607459}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; L25063; AAA28378.1; -; mRNA.
DR EMBL; L25064; AAA53668.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58148.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68533.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68534.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68535.1; -; Genomic_DNA.
DR EMBL; AY071116; AAL48738.1; -; mRNA.
DR PIR; B53859; B53859.
DR RefSeq; NP_523751.2; NM_079027.3.
DR RefSeq; NP_725452.1; NM_166088.2.
DR RefSeq; NP_725453.1; NM_166089.2.
DR RefSeq; NP_725454.1; NM_166090.2.
DR RefSeq; NP_725455.1; NM_166091.2.
DR AlphaFoldDB; P40946; -.
DR SMR; P40946; -.
DR BioGRID; 62436; 28.
DR IntAct; P40946; 1.
DR STRING; 7227.FBpp0086507; -.
DR PaxDb; P40946; -.
DR PRIDE; P40946; -.
DR DNASU; 36699; -.
DR EnsemblMetazoa; FBtr0087375; FBpp0086507; FBgn0013750.
DR EnsemblMetazoa; FBtr0087376; FBpp0086508; FBgn0013750.
DR EnsemblMetazoa; FBtr0087377; FBpp0086509; FBgn0013750.
DR EnsemblMetazoa; FBtr0087378; FBpp0086510; FBgn0013750.
DR EnsemblMetazoa; FBtr0087379; FBpp0086511; FBgn0013750.
DR GeneID; 36699; -.
DR KEGG; dme:Dmel_CG8156; -.
DR UCSC; CG8156-RC; d. melanogaster.
DR CTD; 36699; -.
DR FlyBase; FBgn0013750; Arf51F.
DR VEuPathDB; VectorBase:FBgn0013750; -.
DR eggNOG; KOG0071; Eukaryota.
DR GeneTree; ENSGT00940000156593; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P40946; -.
DR OMA; WSVIPTI; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P40946; -.
DR Reactome; R-DME-8854214; TBC/RABGAPs.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 36699; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36699; -.
DR PRO; PR:P40946; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013750; Expressed in cleaving embryo and 48 other tissues.
DR Genevisible; P40946; DM.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0008047; F:enzyme activator activity; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:FlyBase.
DR GO; GO:0097305; P:response to alcohol; IGI:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; TAS:FlyBase.
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 ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..175
FT /note="ADP-ribosylation factor 6"
FT /id="PRO_0000207444"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 43
FT /note="P -> G (in Ref. 1; AAA28378/AAA53668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 20005 MW; ED2B466B6156EC5A CRC64;
MGKLLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR TELHRIINDR EMRDAIILIF
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLSEGLIWLT SNHKL
