ARF1_ARATH
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 03-AUG-2022, entry version 162.
DE RecName: Full=ADP-ribosylation factor 1 {ECO:0000303|PubMed:11090220};
DE Short=AtARF1 {ECO:0000303|PubMed:11090220};
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},
GN BEX1 {ECO:0000303|PubMed:24369434};
GN OrderedLocusNames=At2g47170 {ECO:0000312|Araport:AT2G47170};
GN ORFNames=T3D7.2 {ECO:0000312|EMBL:AAM15469.1},
GN T8I13.1 {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=10.2307/3871116;
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 -!- 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}.
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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.AT2G47170.1; -.
DR iPTMnet; P36397; -.
DR PaxDb; P36397; -.
DR PRIDE; P36397; -.
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; locus:2065114; AT2G47170.
DR eggNOG; KOG0070; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR OMA; CETISIS; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P36397; -.
DR PRO; PR:P36397; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P36397; baseline and differential.
DR Genevisible; P36397; AT.
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:0006886; P:intracellular protein transport; IBA:GO_Central.
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:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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; -; 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 3D-structure; Auxin signaling pathway; Endosome; ER-Golgi transport;
KW Golgi apparatus; GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW 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 confering
FT abnormal auxin response gradient. Normal subcellular
FT 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
