ID ARF1_ARATH Reviewed; 181 AA. AC P36397; Q7G9L3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 171. DE RecName: Full=ADP-ribosylation factor 1 {ECO:0000303|PubMed:11090220}; DE Short=AtARF1 {ECO:0000303|PubMed:11090220}; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P84077}; DE AltName: Full=Protein BFA-VISUALIZED EXOCYTIC TRAFFICKING DEFECTIVE 1 {ECO:0000303|PubMed:24369434}; GN Name=ARF1 {ECO:0000303|PubMed:11090220}; GN Synonyms=ARF1A1C {ECO:0000303|PubMed:21156810}, BEX1 GN {ECO:0000303|PubMed:24369434}; GN OrderedLocusNames=At2g47170 {ECO:0000312|Araport:AT2G47170}; GN ORFNames=T3D7.2 {ECO:0000312|EMBL:AAM15469.1}, T8I13.1 GN {ECO:0000312|EMBL:AAB63817.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX PubMed=8420798; DOI=10.1016/0014-5793(93)81201-a; RA Regad F., Bardet C., Tremousaygue D., Moisan A., Lescure B., Axelos M.; RT "cDNA cloning and expression of an Arabidopsis GTP-binding protein of the RT ARF family."; RL FEBS Lett. 316:133-136(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP SUBCELLULAR LOCATION. RX PubMed=11090220; DOI=10.1105/tpc.12.11.2219; RA Pimpl P., Movafeghi A., Coughlan S., Denecke J., Hillmer S., Robinson D.G.; RT "In situ localization and in vitro induction of plant COPI-coated RT vesicles."; RL Plant Cell 12:2219-2236(2000). RN [7] RP MUTAGENESIS OF THR-31, AND FUNCTION. RX PubMed=12177464; DOI=10.1104/pp.003624; RA Lee M.H., Min M.K., Lee Y.J., Jin J.B., Shin D.H., Kim D.H., Lee K.-H., RA Hwang I.; RT "ADP-ribosylation factor 1 of Arabidopsis plays a critical role in RT intracellular trafficking and maintenance of endoplasmic reticulum RT morphology in Arabidopsis."; RL Plant Physiol. 129:1507-1520(2002). RN [8] RP MUTAGENESIS OF THR-31 AND GLN-71, AND FUNCTION. RX PubMed=12182707; DOI=10.1046/j.1365-313x.2002.01372.x; RA Takeuchi M., Ueda T., Yahara N., Nakano A.; RT "Arf1 GTPase plays roles in the protein traffic between the endoplasmic RT reticulum and the Golgi apparatus in tobacco and Arabidopsis cultured RT cells."; RL Plant J. 31:499-515(2002). RN [9] RP MUTAGENESIS OF THR-31 AND GLN-71, AND FUNCTION. RX PubMed=12724547; DOI=10.1105/tpc.010140; RA Pimpl P., Hanton S.L., Taylor J.P., Pinto-daSilva L.L., Denecke J.; RT "The GTPase ARF1p controls the sequence-specific vacuolar sorting route to RT the lytic vacuole."; RL Plant Cell 15:1242-1256(2003). RN [10] RP INTERACTION WITH P24 PROTEINS. RX PubMed=15125774; DOI=10.1111/j.1365-313x.2004.02075.x; RA Contreras I., Ortiz-Zapater E., Aniento F.; RT "Sorting signals in the cytosolic tail of membrane proteins involved in the RT interaction with plant ARF1 and coatomer."; RL Plant J. 38:685-698(2004). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15659621; DOI=10.1105/tpc.104.028449; RA Xu J., Scheres B.; RT "Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal RT cell polarity."; RL Plant Cell 17:525-536(2005). RN [12] RP ACTIVITY REGULATION. RX PubMed=16731582; DOI=10.1104/pp.106.077818; RA Song X.-F., Yang C.-Y., Liu J., Yang W.-C.; RT "RPA, a class II ARFGAP protein, activates ARF1 and U5 and plays a role in RT root hair development in Arabidopsis."; RL Plant Physiol. 141:966-976(2006). RN [13] RP INTERACTION WITH AGD7, AND ACTIVITY REGULATION. RX PubMed=17307897; DOI=10.1104/pp.106.095091; RA Min M.K., Kim S.J., Miao Y., Shin J., Jiang L., Hwang I.; RT "Overexpression of Arabidopsis AGD7 causes relocation of Golgi-localized RT proteins to the endoplasmic reticulum and inhibits protein trafficking in RT plant cells."; RL Plant Physiol. 143:1601-1614(2007). RN [14] RP INTERACTION WITH GDAP1, AND FUNCTION. RX PubMed=17307898; DOI=10.1104/pp.106.094953; RA Matheson L.A., Hanton S.L., Rossi M., Latijnhouwers M., Stefano G., RA Renna L., Brandizzi F.; RT "Multiple roles of ADP-ribosylation factor 1 in plant cells include RT spatially regulated recruitment of coatomer and elements of the Golgi RT matrix."; RL Plant Physiol. 143:1615-1627(2007). RN [15] RP SUBCELLULAR LOCATION, AND INTERACTION WITH AGD5. RC STRAIN=cv. Columbia; RX PubMed=21105926; DOI=10.1111/j.1365-313x.2010.04369.x; RA Stefano G., Renna L., Rossi M., Azzarello E., Pollastri S., Brandizzi F., RA Baluska F., Mancuso S.; RT "AGD5 is a GTPase-activating protein at the trans-Golgi network."; RL Plant J. 64:790-799(2010). RN [16] RP FUNCTION, MUTAGENESIS OF LEU-34, AND SUBCELLULAR LOCATION. RC STRAIN=cv. Columbia; RX PubMed=24369434; DOI=10.1093/pcp/pct196; RA Tanaka H., Nodzylski T., Kitakura S., Feraru M.I., Sasabe M., Ishikawa T., RA Kleine-Vehn J., Kakimoto T., Friml J.; RT "BEX1/ARF1A1C is required for BFA-sensitive recycling of PIN auxin RT transporters and auxin-mediated development in Arabidopsis."; RL Plant Cell Physiol. 55:737-749(2014). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP, AND INTERACTION RP WITH A.TUMEFACIENS AK6B. RC STRAIN=cv. Columbia; RX PubMed=21156810; DOI=10.1101/gad.1985511; RA Wang M., Soyano T., Machida S., Yang J.-Y., Jung C., Chua N.-H., Yuan Y.A.; RT "Molecular insights into plant cell proliferation disturbance by RT Agrobacterium protein 6b."; RL Genes Dev. 25:64-76(2011). CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; required CC for the sequence-specific vacuolar sorting route to the lytic vacuole, CC for the ER-to-Golgi transport and for the Golgi-derived transport to CC the plasma membrane (PubMed:24369434). Involved in the recruitment of CC COPI and GDAP1 to membranes. Required for recycling of PIN auxin CC transporters (e.g. PIN1 and PIN2) in a fungal toxin brefeldin A (BFA)- CC dependent manner. Involved in various auxin-dependent developmental CC processes (PubMed:24369434). {ECO:0000269|PubMed:12177464, CC ECO:0000269|PubMed:12182707, ECO:0000269|PubMed:12724547, CC ECO:0000269|PubMed:15659621, ECO:0000269|PubMed:17307898, CC ECO:0000269|PubMed:24369434}. 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:0000250|UniProtKB:P84077}; CC -!- ACTIVITY REGULATION: Activated by AGD7 and AGD10. CC {ECO:0000269|PubMed:16731582, ECO:0000269|PubMed:17307897}. CC -!- SUBUNIT: Interacts with AGD7 and GDAP1. GDP-locked form interacts with CC cytosolic tail of p24 proteins. Interacts with AGD5 at trans-Golgi CC network (PubMed:21105926). Interacts with A.tumefaciens AK6b CC (PubMed:21156810). {ECO:0000269|PubMed:15125774, CC ECO:0000269|PubMed:17307897, ECO:0000269|PubMed:17307898, CC ECO:0000269|PubMed:21105926, ECO:0000269|PubMed:21156810}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11090220, CC ECO:0000269|PubMed:15659621, ECO:0000269|PubMed:24369434}. Endosome CC {ECO:0000269|PubMed:11090220, ECO:0000269|PubMed:15659621}. Golgi CC apparatus, trans-Golgi network {ECO:0000269|PubMed:21105926, CC ECO:0000269|PubMed:24369434}. Early endosome CC {ECO:0000269|PubMed:24369434}. Note=Colocalizes with AGD5 at trans- CC Golgi network. {ECO:0000269|PubMed:21105926}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M95166; AAA32729.1; -; mRNA. DR EMBL; AC002337; AAB63817.1; -; Genomic_DNA. DR EMBL; AC007236; AAM15469.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10810.1; -; Genomic_DNA. DR EMBL; CP002685; ANM62132.1; -; Genomic_DNA. DR EMBL; CP002685; ANM62133.1; -; Genomic_DNA. DR EMBL; AY074859; AAL75910.1; -; mRNA. DR EMBL; AY142032; AAM98296.1; -; mRNA. DR EMBL; AY087342; AAM64892.1; -; mRNA. DR PIR; S28875; S28875. DR RefSeq; NP_001324310.1; NM_001337250.1. DR RefSeq; NP_001324311.1; NM_001337251.1. DR RefSeq; NP_182239.1; NM_130285.3. DR PDB; 3AQ4; X-ray; 1.80 A; A/B=1-181. DR PDBsum; 3AQ4; -. DR AlphaFoldDB; P36397; -. DR SMR; P36397; -. DR BioGRID; 4665; 1. DR IntAct; P36397; 1. DR MINT; P36397; -. DR STRING; 3702.P36397; -. DR iPTMnet; P36397; -. DR PaxDb; 3702-AT2G47170-1; -. DR ProteomicsDB; 240326; -. DR EnsemblPlants; AT2G47170.1; AT2G47170.1; AT2G47170. DR EnsemblPlants; AT2G47170.2; AT2G47170.2; AT2G47170. DR EnsemblPlants; AT2G47170.3; AT2G47170.3; AT2G47170. DR GeneID; 819330; -. DR Gramene; AT2G47170.1; AT2G47170.1; AT2G47170. DR Gramene; AT2G47170.2; AT2G47170.2; AT2G47170. DR Gramene; AT2G47170.3; AT2G47170.3; AT2G47170. DR KEGG; ath:AT2G47170; -. DR Araport; AT2G47170; -. DR TAIR; AT2G47170; ARF1A1C. DR eggNOG; KOG0070; Eukaryota. DR HOGENOM; CLU_040729_9_3_1; -. DR InParanoid; P36397; -. DR OMA; TIRFNVE; -. DR OrthoDB; 641961at2759; -. DR PhylomeDB; P36397; -. DR PRO; PR:P36397; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; P36397; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISS:TAIR. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:0016004; F:phospholipase activator activity; TAS:TAIR. DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0090354; P:regulation of auxin metabolic process; IMP:UniProtKB. DR GO; GO:0031001; P:response to brefeldin A; IMP:UniProtKB. DR GO; GO:0098876; P:vesicle-mediated transport to the plasma membrane; IMP:UniProtKB. DR CDD; cd04150; Arf1_5_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR045872; Arf1-5-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1. DR PANTHER; PTHR11711:SF30; ADP-RIBOSYLATION FACTOR 1; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51417; ARF; 1. DR Genevisible; P36397; AT. PE 1: Evidence at protein level; KW 3D-structure; Auxin signaling pathway; Endosome; ER-Golgi transport; KW Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein; Myristate; KW Nucleotide-binding; Protein transport; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255" FT CHAIN 2..181 FT /note="ADP-ribosylation factor 1" FT /id="PRO_0000207426" FT BINDING 24..31 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:21156810, FT ECO:0007744|PDB:3AQ4" 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:0000269|PubMed:21156810, FT ECO:0007744|PDB:3AQ4" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT MUTAGEN 31 FT /note="T->N: Constitutively inactive form (GDP-locked FT form); loss of intracellular protein trafficking." FT /evidence="ECO:0000269|PubMed:12177464, FT ECO:0000269|PubMed:12182707, ECO:0000269|PubMed:12724547" FT MUTAGEN 34 FT /note="L->F: In bex1; hypersensitivity to the fungal toxin FT brefeldin A (BFA) leading to developmental defects FT (including embryonic patterning defects, root bending and FT growth arrest) and impaired plasma membrane localization of FT PIN auxin transporters (e.g. PIN1 and PIN2), thus FT conferring abnormal auxin response gradient. Normal FT subcellular localization." FT /evidence="ECO:0000269|PubMed:24369434" FT MUTAGEN 71 FT /note="Q->L: Constitutively active form (GTP-locked form)." FT /evidence="ECO:0000269|PubMed:12182707, FT ECO:0000269|PubMed:12724547" FT HELIX 5..9 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 10..12 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 17..25 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 30..37 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 61..68 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 79..84 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 85..93 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 100..111 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 136..142 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:3AQ4" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:3AQ4" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:3AQ4" FT HELIX 166..178 FT /evidence="ECO:0007829|PDB:3AQ4" SQ SEQUENCE 181 AA; 20609 MW; 7EDDEC87B7B29592 CRC64; MGLSFGKLFS RLFAKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRDRV VEARDELHRM LNEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRQ RHWYIQSTCA TSGEGLYEGL DWLSNNIASK A //