ARF1_DROME
ID ARF1_DROME Reviewed; 182 AA.
AC P61209; A4V2B1; A8JNX4; P35676; Q9VNQ2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ADP-ribosylation factor 1;
GN Name=Arf79F; Synonyms=ARF1; ORFNames=CG8385;
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].
RX PubMed=8507638; DOI=10.1021/bi00074a012;
RA Murtagh J.J. Jr., Lee F.-J.S., Deak P., Hall L.M., Monaco L., Lee C.M.,
RA Stevens L.A., Moss J., Vaughan M.;
RT "Molecular characterization of a conserved, guanine nucleotide-dependent
RT ADP-ribosylation factor in Drosophila melanogaster.";
RL Biochemistry 32:6011-6018(1993).
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, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ILE-46 AND ASN-52.
RX PubMed=27535433; DOI=10.1091/mbc.e16-05-0272;
RA Rodrigues F.F., Shao W., Harris T.J.;
RT "The Arf GAP Asap promotes Arf1 function at the Golgi for cleavage furrow
RT biosynthesis in Drosophila.";
RL Mol. Biol. Cell 27:3143-3155(2016).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; has a
CC role in Golgi organization and may modulate vesicle budding and
CC uncoating within the Golgi apparatus (Probable). Has a role in eye
CC development (PubMed:21976699). Required for cleavage furrow ingression
CC in embryonic cells (PubMed:27535433). {ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:27535433, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:27535433}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:27535433}. Note=Localization to
CC the Golgi is dependent on Asap. {ECO:0000269|PubMed:27535433}.
CC -!- DISRUPTION PHENOTYPE: Conditional RNAi-mediated knockdown in the eye
CC results in aberrant compound eye morphogenesis (PubMed:21976699).
CC Maternal RNAi-mediated knockdown results in abnormal aggregation of
CC Golgi apparatus and disrupted cleavage furrow ingression in early
CC embryos (PubMed:27535433). {ECO:0000269|PubMed:21976699,
CC ECO:0000269|PubMed:27535433}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; S62079; AAB27066.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51871.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51872.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51873.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51874.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12207.1; -; Genomic_DNA.
DR EMBL; AE014296; ABW08583.1; -; Genomic_DNA.
DR EMBL; AE014296; ABW08584.2; -; Genomic_DNA.
DR EMBL; AY060375; AAL25414.1; -; mRNA.
DR PIR; A49520; A49520.
DR RefSeq; NP_001097667.1; NM_001104197.3.
DR RefSeq; NP_001097668.2; NM_001104198.2.
DR RefSeq; NP_001262225.1; NM_001275296.1.
DR RefSeq; NP_476955.1; NM_057607.6.
DR RefSeq; NP_730757.1; NM_168970.4.
DR RefSeq; NP_730758.1; NM_168971.4.
DR RefSeq; NP_730759.1; NM_168972.5.
DR RefSeq; NP_730760.1; NM_168973.3.
DR AlphaFoldDB; P61209; -.
DR SMR; P61209; -.
DR BioGRID; 65734; 74.
DR IntAct; P61209; 9.
DR STRING; 7227.FBpp0289184; -.
DR PaxDb; P61209; -.
DR PRIDE; P61209; -.
DR DNASU; 40506; -.
DR EnsemblMetazoa; FBtr0078571; FBpp0078222; FBgn0010348.
DR EnsemblMetazoa; FBtr0078573; FBpp0078224; FBgn0010348.
DR EnsemblMetazoa; FBtr0078574; FBpp0078225; FBgn0010348.
DR EnsemblMetazoa; FBtr0078575; FBpp0078226; FBgn0010348.
DR EnsemblMetazoa; FBtr0112858; FBpp0111771; FBgn0010348.
DR EnsemblMetazoa; FBtr0299906; FBpp0289184; FBgn0010348.
DR EnsemblMetazoa; FBtr0299907; FBpp0289185; FBgn0010348.
DR EnsemblMetazoa; FBtr0332054; FBpp0304364; FBgn0010348.
DR GeneID; 40506; -.
DR KEGG; dme:Dmel_CG8385; -.
DR UCSC; CG8385-RB; d. melanogaster.
DR CTD; 40506; -.
DR FlyBase; FBgn0010348; Arf79F.
DR VEuPathDB; VectorBase:FBgn0010348; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P61209; -.
DR OMA; VEYRNIQ; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P61209; -.
DR Reactome; R-DME-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-DME-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-6811438; Intra-Golgi traffic.
DR SignaLink; P61209; -.
DR BioGRID-ORCS; 40506; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Arf79F; fly.
DR GenomeRNAi; 40506; -.
DR PRO; PR:P61209; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010348; Expressed in brain and 9 other tissues.
DR ExpressionAtlas; P61209; baseline and differential.
DR Genevisible; P61209; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:FlyBase.
DR GO; GO:0005764; C:lysosome; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IMP:FlyBase.
DR GO; GO:0032011; P:ARF protein signal transduction; IGI:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:FlyBase.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:1990386; P:mitotic cleavage furrow ingression; IMP:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; TAS:FlyBase.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:FlyBase.
DR GO; GO:0002786; P:regulation of antibacterial peptide production; IMP:FlyBase.
DR GO; GO:0010883; P:regulation of lipid storage; IDA:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; TAS:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04150; Arf1_5_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
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 Cytoplasm; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW Myristate; Nucleotide-binding; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..182
FT /note="ADP-ribosylation factor 1"
FT /id="PRO_0000207441"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
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 MUTAGEN 46
FT /note="I->D: Abnormal aggregation of Golgi apparatus and
FT disrupted cleavage furrow ingression in early embryos. May
FT be insensitive to Asap activation."
FT /evidence="ECO:0000269|PubMed:27535433"
FT MUTAGEN 52
FT /note="N->A: No defect in Golgi apparatus and cleavage
FT furrow ingression in early embryos."
FT /evidence="ECO:0000269|PubMed:27535433"
SQ SEQUENCE 182 AA; 20688 MW; 9E87E24DFAEA3674 CRC64;
MGNVFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERI GEAREELMRM LAEDELRDAV
LLIFANKQDL PNAMNAAEIT DKLGLHSLRN RNWYIQATCA TSGDGLYEGL DWLSNQLKNA
NR
