ID   ARFA_ARATH              Reviewed;         665 AA.
AC   Q8L7G0; O23664;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Auxin response factor 1 {ECO:0000303|PubMed:9188533};
GN   Name=ARF1 {ECO:0000303|PubMed:9188533};
GN   OrderedLocusNames=At1g59750 {ECO:0000312|Araport:AT1G59750};
GN   ORFNames=F23H11.7 {ECO:0000312|EMBL:AAD39318.1};
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=9188533; DOI=10.1126/science.276.5320.1865;
RA   Ulmasov T., Hagen G., Guilfoyle T.J.;
RT   "ARF1, a transcription factor that binds to auxin response elements.";
RL   Science 276:1865-1868(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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] (ISOFORMS 1 AND 2).
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   DIMERIZATION, AND TISSUE SPECIFICITY.
RX   PubMed=10476078; DOI=10.1046/j.1365-313x.1999.00538.x;
RA   Ulmasov T., Hagen G., Guilfoyle T.J.;
RT   "Dimerization and DNA binding of auxin response factors.";
RL   Plant J. 19:309-319(1999).
RN   [6]
RP   TRANSCRIPTIONAL REPRESSOR.
RX   PubMed=10318972; DOI=10.1073/pnas.96.10.5844;
RA   Ulmasov T., Hagen G., Guilfoyle T.J.;
RT   "Activation and repression of transcription by auxin-response factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:5844-5849(1999).
RN   [7]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=12036261; DOI=10.1023/a:1015207114117;
RA   Hagen G., Guilfoyle T.J.;
RT   "Auxin-responsive gene expression: genes, promoters and regulatory
RT   factors.";
RL   Plant Mol. Biol. 49:373-385(2002).
RN   [8]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16176952; DOI=10.1242/dev.02012;
RA   Ellis C.M., Nagpal P., Young J.C., Hagen G., Guilfoyle T.J., Reed J.W.;
RT   "AUXIN RESPONSE FACTOR1 and AUXIN RESPONSE FACTOR2 regulate senescence and
RT   floral organ abscission in Arabidopsis thaliana.";
RL   Development 132:4563-4574(2005).
RN   [9]
RP   GENE FAMILY.
RX   PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006;
RA   Swaminathan K., Peterson K., Jack T.;
RT   "The plant B3 superfamily.";
RL   Trends Plant Sci. 13:647-655(2008).
RN   [10]
RP   FUNCTION, INTERACTION WITH RIN13, AND SUBCELLULAR LOCATION.
RX   PubMed=32446355; DOI=10.1016/j.bbrc.2020.04.082;
RA   Liu X., Liu H., Liu W.-C., Gao Z.;
RT   "The nuclear localized RIN13 induces cell death through interacting with
RT   ARF1.";
RL   Biochem. Biophys. Res. Commun. 527:124-130(2020).
CC   -!- FUNCTION: Auxin response factors (ARFs) are transcriptional factors
CC       that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the
CC       auxin-responsive promoter elements (AuxREs). Seems to act as
CC       transcriptional repressor. Formation of heterodimers with Aux/IAA
CC       proteins may alter their ability to modulate early auxin response genes
CC       expression. Promotes flowering, stamen development, floral organ
CC       abscission and fruit dehiscence. Acts as a repressor of IAA2, IAA3 and
CC       IAA7. Together with RIN13, promotes leaf senescence and cell death
CC       (PubMed:32446355). {ECO:0000269|PubMed:12036261,
CC       ECO:0000269|PubMed:16176952, ECO:0000269|PubMed:32446355}.
CC   -!- SUBUNIT: Homodimers and heterodimers. Interacts with the auxin-
CC       responsive proteins IAA12, IAA13, IAA17 and with ARF2. Binds to RIN13
CC       in the nucleus (PubMed:32446355). {ECO:0000269|PubMed:32446355}.
CC   -!- INTERACTION:
CC       Q8L7G0; Q8L7G0: ARF1; NbExp=4; IntAct=EBI-2324259, EBI-2324259;
CC       Q8L7G0; Q9C5W9: ARF18; NbExp=4; IntAct=EBI-2324259, EBI-3946783;
CC       Q8L7G0; Q94JM3: ARF2; NbExp=4; IntAct=EBI-2324259, EBI-1799262;
CC       Q8L7G0; Q9XED8: ARF9; NbExp=3; IntAct=EBI-2324259, EBI-3946762;
CC       Q8L7G0; Q9C5X0: IAA34; NbExp=4; IntAct=EBI-2324259, EBI-3946459;
CC       Q8L7G0; Q9SN12: MYB77; NbExp=2; IntAct=EBI-2324259, EBI-2324225;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32446355}. Cytoplasm
CC       {ECO:0000269|PubMed:32446355}. Note=Translocates to the nucleus in the
CC       presence of RIN13. {ECO:0000269|PubMed:32446355}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8L7G0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8L7G0-2; Sequence=VSP_010077;
CC   -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC       {ECO:0000269|PubMed:10476078}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the sepals and carpels of young
CC       flower buds. At stage 10 of flower development, expression in the
CC       carpels becomes restricted to the style. Also expressed in anthers and
CC       filaments. At stage 13, expressed in the region at the top of the
CC       pedicel, including the abscission zone. {ECO:0000269|PubMed:16176952}.
CC   -!- DOMAIN: Interactions between auxin response factors (ARFs) and Aux/IAA
CC       proteins occur through their C-terminal dimerization domains III and
CC       IV.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ARF family. {ECO:0000305}.
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DR   EMBL; U83245; AAC49751.1; -; mRNA.
DR   EMBL; AC007258; AAD39318.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33612.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33613.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33614.1; -; Genomic_DNA.
DR   EMBL; AY133723; AAM91657.1; -; mRNA.
DR   EMBL; BT002748; AAO22577.1; -; mRNA.
DR   PIR; D96621; D96621.
DR   RefSeq; NP_001031208.1; NM_001036131.3. [Q8L7G0-1]
DR   RefSeq; NP_176184.1; NM_104668.4. [Q8L7G0-1]
DR   RefSeq; NP_849830.1; NM_179499.2. [Q8L7G0-2]
DR   PDB; 4LDV; X-ray; 1.45 A; A=1-355.
DR   PDB; 4LDW; X-ray; 2.67 A; A/B=1-355.
DR   PDB; 4LDX; X-ray; 2.90 A; A/B=1-355.
DR   PDB; 4LDY; X-ray; 2.30 A; A/B=1-355.
DR   PDB; 6YCQ; X-ray; 1.65 A; A/B=1-355.
DR   PDBsum; 4LDV; -.
DR   PDBsum; 4LDW; -.
DR   PDBsum; 4LDX; -.
DR   PDBsum; 4LDY; -.
DR   PDBsum; 6YCQ; -.
DR   AlphaFoldDB; Q8L7G0; -.
DR   SMR; Q8L7G0; -.
DR   BioGRID; 27493; 17.
DR   IntAct; Q8L7G0; 21.
DR   MINT; Q8L7G0; -.
DR   STRING; 3702.Q8L7G0; -.
DR   iPTMnet; Q8L7G0; -.
DR   PaxDb; 3702-AT1G59750-1; -.
DR   ProteomicsDB; 240612; -. [Q8L7G0-1]
DR   EnsemblPlants; AT1G59750.1; AT1G59750.1; AT1G59750. [Q8L7G0-1]
DR   EnsemblPlants; AT1G59750.2; AT1G59750.2; AT1G59750. [Q8L7G0-2]
DR   EnsemblPlants; AT1G59750.3; AT1G59750.3; AT1G59750. [Q8L7G0-1]
DR   GeneID; 842268; -.
DR   Gramene; AT1G59750.1; AT1G59750.1; AT1G59750. [Q8L7G0-1]
DR   Gramene; AT1G59750.2; AT1G59750.2; AT1G59750. [Q8L7G0-2]
DR   Gramene; AT1G59750.3; AT1G59750.3; AT1G59750. [Q8L7G0-1]
DR   KEGG; ath:AT1G59750; -.
DR   Araport; AT1G59750; -.
DR   TAIR; AT1G59750; ARF1.
DR   eggNOG; ENOG502QQSN; Eukaryota.
DR   InParanoid; Q8L7G0; -.
DR   OrthoDB; 447839at2759; -.
DR   PhylomeDB; Q8L7G0; -.
DR   PRO; PR:Q8L7G0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L7G0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR   GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEP:TAIR.
DR   GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR   CDD; cd10017; B3_DNA; 1.
DR   Gene3D; 2.30.30.1040; -; 1.
DR   Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 1.
DR   InterPro; IPR010525; ARF_dom.
DR   InterPro; IPR044835; ARF_plant.
DR   InterPro; IPR033389; AUX/IAA_dom.
DR   InterPro; IPR003340; B3_DNA-bd.
DR   InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR   InterPro; IPR000270; PB1_dom.
DR   PANTHER; PTHR31384:SF96; AUXIN RESPONSE FACTOR 1; 1.
DR   PANTHER; PTHR31384; AUXIN RESPONSE FACTOR 4-RELATED; 1.
DR   Pfam; PF02309; AUX_IAA; 2.
DR   Pfam; PF06507; Auxin_resp; 1.
DR   Pfam; PF02362; B3; 1.
DR   SMART; SM01019; B3; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF101936; DNA-binding pseudobarrel domain; 1.
DR   PROSITE; PS50863; B3; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   Genevisible; Q8L7G0; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Auxin signaling pathway; Cytoplasm;
KW   DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..665
FT                   /note="Auxin response factor 1"
FT                   /id="PRO_0000111505"
FT   DOMAIN          542..635
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   DNA_BIND        124..226
FT                   /note="TF-B3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT   REGION          356..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..387
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         390..392
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_010077"
FT   CONFLICT        136
FT                   /note="H -> Q (in Ref. 4; AAM91657)"
FT                   /evidence="ECO:0000305"
FT   HELIX           17..28
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           45..52
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          71..84
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:6YCQ"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           130..133
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           143..149
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          161..167
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          173..181
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   TURN            182..185
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          186..189
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           193..199
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          207..213
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   TURN            214..216
FT                   /evidence="ECO:0007829|PDB:6YCQ"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           239..256
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          260..264
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           277..285
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          293..297
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:4LDY"
FT   STRAND          307..316
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          331..337
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:4LDV"
FT   HELIX           349..351
FT                   /evidence="ECO:0007829|PDB:4LDV"
SQ   SEQUENCE   665 AA;  73668 MW;  79DD3180C2091401 CRC64;
     MAASNHSSGK PGGVLSDALC RELWHACAGP LVTLPREGER VYYFPEGHME QLEASMHQGL
     EQQMPSFNLP SKILCKVINI QRRAEPETDE VYAQITLLPE LDQSEPTSPD APVQEPEKCT
     VHSFCKTLTA SDTSTHGGFS VLRRHADDCL PPLDMSQQPP WQELVATDLH NSEWHFRHIF
     RGQPRRHLLT TGWSVFVSSK KLVAGDAFIF LRGENEELRV GVRRHMRQQT NIPSSVISSH
     SMHIGVLATA AHAITTGTIF SVFYKPRTSR SEFIVSVNRY LEAKTQKLSV GMRFKMRFEG
     EEAPEKRFSG TIVGVQENKS SVWHDSEWRS LKVQWDEPSS VFRPERVSPW ELEPLVANST
     PSSQPQPPQR NKRPRPPGLP SPATGPSGPV TPDGVWKSPA DTPSSVPLFS PPAKAATFGH
     GGNKSFGVSI GSAFWPTNAD SAAESFASAF NNESTEKKQT NGNVCRLFGF ELVENVNVDE
     CFSAASVSGA VAVDQPVPSN EFDSGQQSEP LNINQSDIPS GSGDPEKSSL RSPQESQSRQ
     IRSCTKVHMQ GSAVGRAIDL TRSECYEDLF KKLEEMFDIK GELLESTKKW QVVYTDDEDD
     MMMVGDDPWN EFCGMVRKIF IYTPEEVKKL SPKNKLAVNA RMQLKADAEE NGNTEGRSSS
     MAGSR
//