ARFA_ARATH
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 25-MAY-2022, entry version 149.
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 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}.
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; 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.AT1G59750.1; -.
DR iPTMnet; Q8L7G0; -.
DR PaxDb; Q8L7G0; -.
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; locus:2025991; AT1G59750.
DR eggNOG; ENOG502QQSN; Eukaryota.
DR InParanoid; Q8L7G0; -.
DR PhylomeDB; Q8L7G0; -.
DR PRO; PR:Q8L7G0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7G0; baseline and differential.
DR Genevisible; Q8L7G0; AT.
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 transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR CDD; cd10017; B3_DNA; 1.
DR Gene3D; 2.40.330.10; -; 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; PTHR31384; 1.
DR Pfam; PF02309; AUX_IAA; 1.
DR Pfam; PF06507; Auxin_resp; 1.
DR Pfam; PF02362; B3; 1.
DR SMART; SM01019; B3; 1.
DR SUPFAM; SSF101936; SSF101936; 1.
DR PROSITE; PS50863; B3; 1.
DR PROSITE; PS51745; PB1; 1.
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
