IAA17_ARATH
ID IAA17_ARATH Reviewed; 229 AA.
AC P93830; O49162;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Auxin-responsive protein IAA17;
DE AltName: Full=Auxin response 3;
DE AltName: Full=Indoleacetic acid-induced protein 17;
GN Name=IAA17; Synonyms=AXR3; OrderedLocusNames=At1g04250; ORFNames=F19P19.31;
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], AND INTERACTION WITH IAA1.
RC STRAIN=cv. Columbia;
RX PubMed=9342315; DOI=10.1073/pnas.94.22.11786;
RA Kim J., Harter K., Theologis A.;
RT "Protein-protein interactions among the Aux/IAA proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11786-11791(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS AXR3-1 AND AXR3-3, AND
RP MUTAGENESIS OF LEU-16; ASP-118 AND PRO-121.
RC STRAIN=cv. Columbia;
RX PubMed=9478901; DOI=10.1126/science.279.5355.1371;
RA Rouse D., Mackay P., Stirnberg P., Estelle M., Leyser O.;
RT "Changes in auxin response from mutations in an AUX/IAA gene.";
RL Science 279:1371-1373(1998).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION BY PHYTOCHROME A.
RX PubMed=11115889; DOI=10.1104/pp.124.4.1728;
RA Colon-Carmona A., Chen D.L., Yeh K.-C., Abel S.;
RT "Aux/IAA proteins are phosphorylated by phytochrome in vitro.";
RL Plant Physiol. 124:1728-1738(2000).
RN [8]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=12036262; DOI=10.1023/a:1015255030047;
RA Liscum E., Reed J.W.;
RT "Genetics of Aux/IAA and ARF action in plant growth and development.";
RL Plant Mol. Biol. 49:387-400(2002).
RN [9]
RP TRANSCRIPTIONAL REPRESSION DOMAIN.
RX PubMed=14742873; DOI=10.1105/tpc.017384;
RA Tiwari S.B., Hagen G., Guilfoyle T.J.;
RT "Aux/IAA proteins contain a potent transcriptional repression domain.";
RL Plant Cell 16:533-543(2004).
RN [10]
RP INTERACTION WITH TPL.
RX PubMed=18258861; DOI=10.1126/science.1151461;
RA Szemenyei H., Hannon M., Long J.A.;
RT "TOPLESS mediates auxin-dependent transcriptional repression during
RT Arabidopsis embryogenesis.";
RL Science 319:1384-1386(2008).
RN [11]
RP INTERACTION.
RX PubMed=21734647; DOI=10.1038/msb.2011.39;
RA Vernoux T., Brunoud G., Farcot E., Morin V., Van den Daele H., Legrand J.,
RA Oliva M., Das P., Larrieu A., Wells D., Guedon Y., Armitage L., Picard F.,
RA Guyomarc'h S., Cellier C., Parry G., Koumproglou R., Doonan J.H.,
RA Estelle M., Godin C., Kepinski S., Bennett M., De Veylder L., Traas J.;
RT "The auxin signalling network translates dynamic input into robust
RT patterning at the shoot apex.";
RL Mol. Syst. Biol. 7:508-508(2011).
RN [12]
RP MUTAGENESIS OF LYS-114; ASP-183 AND ASP-187, AND INTERACTION WITH ARF7.
RX PubMed=24706860; DOI=10.1073/pnas.1400074111;
RA Korasick D.A., Westfall C.S., Lee S.G., Nanao M.H., Dumas R., Hagen G.,
RA Guilfoyle T.J., Jez J.M., Strader L.C.;
RT "Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the
RT control of auxin response repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5427-5432(2014).
CC -!- FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that
CC function as repressors of early auxin response genes at low auxin
CC concentrations. Repression is thought to result from the interaction
CC with auxin response factors (ARFs), proteins that bind to the auxin-
CC responsive promoter element (AuxRE). Formation of heterodimers with ARF
CC proteins may alter their ability to modulate early auxin response genes
CC expression. {ECO:0000269|PubMed:12036262}.
CC -!- SUBUNIT: Homodimers and heterodimers (PubMed:18258861,
CC PubMed:21734647). Interacts with the auxin response factors ARF1 and
CC IAA24 (PubMed:21734647). Interacts with IAA1 (PubMed:9342315,
CC PubMed:21734647). Interacts with TPL (PubMed:18258861,
CC PubMed:21734647). Interacts (via PB1 domain) with ARF7 (via PB1 domain)
CC (PubMed:21734647, PubMed:24706860). {ECO:0000269|PubMed:18258861,
CC ECO:0000269|PubMed:21734647, ECO:0000269|PubMed:24706860,
CC ECO:0000269|PubMed:9342315}.
CC -!- INTERACTION:
CC P93830; Q9FIW5: ANAC094; NbExp=3; IntAct=EBI-632243, EBI-25522986;
CC P93830; Q9C5W9: ARF18; NbExp=16; IntAct=EBI-632243, EBI-3946783;
CC P93830; Q8RYC8: ARF19; NbExp=6; IntAct=EBI-632243, EBI-529887;
CC P93830; Q94JM3: ARF2; NbExp=3; IntAct=EBI-632243, EBI-1799262;
CC P93830; Q8RV83: ARF70; NbExp=3; IntAct=EBI-632243, EBI-15392261;
CC P93830; Q9XED8: ARF9; NbExp=5; IntAct=EBI-632243, EBI-3946762;
CC P93830; C0SUW7: ARID6; NbExp=3; IntAct=EBI-632243, EBI-15192335;
CC P93830; O80533: At1g09500; NbExp=3; IntAct=EBI-632243, EBI-4447439;
CC P93830; Q9FVU9: CSN5B; NbExp=3; IntAct=EBI-632243, EBI-697501;
CC P93830; Q8VZS3: HHO2; NbExp=3; IntAct=EBI-632243, EBI-4429217;
CC P93830; Q9FPE8: HHO3; NbExp=3; IntAct=EBI-632243, EBI-2298866;
CC P93830; P49677: IAA1; NbExp=11; IntAct=EBI-632243, EBI-630505;
CC P93830; Q38828: IAA10; NbExp=9; IntAct=EBI-632243, EBI-3946434;
CC P93830; Q38829: IAA11; NbExp=8; IntAct=EBI-632243, EBI-2367923;
CC P93830; Q38830: IAA12; NbExp=9; IntAct=EBI-632243, EBI-617608;
CC P93830; Q38831: IAA13; NbExp=9; IntAct=EBI-632243, EBI-1554143;
CC P93830; Q38832: IAA14; NbExp=4; IntAct=EBI-632243, EBI-2295562;
CC P93830; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-632243, EBI-25524519;
CC P93830; O24407: IAA16; NbExp=8; IntAct=EBI-632243, EBI-632231;
CC P93830; P93830: IAA17; NbExp=10; IntAct=EBI-632243, EBI-632243;
CC P93830; O24408: IAA18; NbExp=7; IntAct=EBI-632243, EBI-2295525;
CC P93830; O24409: IAA19; NbExp=11; IntAct=EBI-632243, EBI-632257;
CC P93830; P49678: IAA2; NbExp=10; IntAct=EBI-632243, EBI-632343;
CC P93830; O24410: IAA20; NbExp=6; IntAct=EBI-632243, EBI-632272;
CC P93830; Q8LAL2: IAA26; NbExp=9; IntAct=EBI-632243, EBI-3947418;
CC P93830; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-632243, EBI-3946677;
CC P93830; Q9XFM0: IAA28; NbExp=9; IntAct=EBI-632243, EBI-3133404;
CC P93830; Q38822: IAA3; NbExp=14; IntAct=EBI-632243, EBI-307174;
CC P93830; Q8H174: IAA31; NbExp=8; IntAct=EBI-632243, EBI-3946408;
CC P93830; Q8RYC6: IAA32; NbExp=7; IntAct=EBI-632243, EBI-3946448;
CC P93830; Q9FKM7: IAA33; NbExp=5; IntAct=EBI-632243, EBI-3946739;
CC P93830; Q9C5X0: IAA34; NbExp=11; IntAct=EBI-632243, EBI-3946459;
CC P93830; P33077: IAA4; NbExp=8; IntAct=EBI-632243, EBI-632187;
CC P93830; P33078: IAA5; NbExp=9; IntAct=EBI-632243, EBI-3946487;
CC P93830; Q38824: IAA6; NbExp=8; IntAct=EBI-632243, EBI-1554124;
CC P93830; Q38826: IAA8; NbExp=8; IntAct=EBI-632243, EBI-632200;
CC P93830; Q38827: IAA9; NbExp=4; IntAct=EBI-632243, EBI-632216;
CC P93830; F4JL11: IMPA2; NbExp=3; IntAct=EBI-632243, EBI-1253508;
CC P93830; O04294: IMPA3; NbExp=3; IntAct=EBI-632243, EBI-1644689;
CC P93830; Q9FWY7: IMPA6; NbExp=3; IntAct=EBI-632243, EBI-4431755;
CC P93830; Q5XEN5: MBD1; NbExp=7; IntAct=EBI-632243, EBI-4445335;
CC P93830; Q9LSI4: MGH6.1; NbExp=3; IntAct=EBI-632243, EBI-15198743;
CC P93830; Q9LTC4: MYB15; NbExp=3; IntAct=EBI-632243, EBI-21497119;
CC P93830; O22179: MYB70; NbExp=3; IntAct=EBI-632243, EBI-1238013;
CC P93830; Q9FK47: MYR1; NbExp=3; IntAct=EBI-632243, EBI-25523464;
CC P93830; Q8LAJ7: PHL3; NbExp=3; IntAct=EBI-632243, EBI-4443730;
CC P93830; Q9C8Y3: RGL1; NbExp=3; IntAct=EBI-632243, EBI-963647;
CC P93830; Q9S7W5: TCP13; NbExp=5; IntAct=EBI-632243, EBI-4424877;
CC P93830; Q9C9L2: TCP15; NbExp=6; IntAct=EBI-632243, EBI-4426144;
CC P93830; Q9M1U4: TCP16; NbExp=6; IntAct=EBI-632243, EBI-15198627;
CC P93830; Q9FTA2: TCP21; NbExp=3; IntAct=EBI-632243, EBI-4426168;
CC P93830; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-632243, EBI-25522447;
CC P93830; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-632243, EBI-15192325;
CC P93830; O64647: TCP9; NbExp=3; IntAct=EBI-632243, EBI-9838721;
CC P93830; Q570C0: TIR1; NbExp=2; IntAct=EBI-632243, EBI-307183;
CC P93830; Q9LQW3: ZHD14; NbExp=3; IntAct=EBI-632243, EBI-1806701;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By auxin.
CC -!- DOMAIN: The N-terminal half of the protein contains two conserved
CC domains I and II. Domain I includes a slightly degenerated ERF-
CC associated amphiphilic repression (EAR) motif which seems to be
CC involved in the activity of transcriptional repression. Domain II is
CC required for the correct degradation of the protein through the SCF-
CC mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA
CC proteins and auxin response factors (ARFs) occur through their C-
CC terminal dimerization domains III and IV.
CC -!- PTM: Phosphorylated by phytochrome A in vitro.
CC {ECO:0000269|PubMed:11115889}.
CC -!- MISCELLANEOUS: Increased auxin response of mutants axr3-1 and axr3-3
CC may result from an increased stability of AXR3.
CC -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64837.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U49073; AAB84354.1; -; mRNA.
DR EMBL; AF040631; AAC39439.1; -; Genomic_DNA.
DR EMBL; AF040632; AAC39440.1; -; Genomic_DNA.
DR EMBL; AC000104; AAB70451.2; -; Genomic_DNA.
DR EMBL; CP002684; AEE27674.1; -; Genomic_DNA.
DR EMBL; AF336916; AAG53997.1; -; mRNA.
DR EMBL; AY070094; AAL49831.1; -; mRNA.
DR EMBL; AY117183; AAM51258.1; -; mRNA.
DR EMBL; AY087284; AAM64837.1; ALT_INIT; mRNA.
DR PIR; H86173; H86173.
DR RefSeq; NP_171921.1; NM_100306.4.
DR PDB; 2MUK; NMR; -; X=105-217.
DR PDB; 6L5K; X-ray; 2.91 A; B=105-217.
DR PDBsum; 2MUK; -.
DR PDBsum; 6L5K; -.
DR AlphaFoldDB; P93830; -.
DR BMRB; P93830; -.
DR SMR; P93830; -.
DR BioGRID; 24803; 93.
DR ELM; P93830; -.
DR IntAct; P93830; 90.
DR STRING; 3702.AT1G04250.1; -.
DR PaxDb; P93830; -.
DR PRIDE; P93830; -.
DR ProteomicsDB; 250633; -.
DR DNASU; 839568; -.
DR EnsemblPlants; AT1G04250.1; AT1G04250.1; AT1G04250.
DR GeneID; 839568; -.
DR Gramene; AT1G04250.1; AT1G04250.1; AT1G04250.
DR KEGG; ath:AT1G04250; -.
DR Araport; AT1G04250; -.
DR TAIR; locus:2018374; AT1G04250.
DR eggNOG; ENOG502QPNB; Eukaryota.
DR HOGENOM; CLU_049393_1_5_1; -.
DR InParanoid; P93830; -.
DR OMA; MALVNTW; -.
DR OrthoDB; 1440216at2759; -.
DR PhylomeDB; P93830; -.
DR PRO; PR:P93830; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93830; baseline and differential.
DR Genevisible; P93830; AT.
DR GO; GO:0005634; C:nucleus; 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:0009734; P:auxin-activated signaling pathway; TAS:TAIR.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR InterPro; IPR033389; AUX/IAA_dom.
DR InterPro; IPR003311; AUX_IAA.
DR InterPro; IPR000270; PB1_dom.
DR PANTHER; PTHR31734; PTHR31734; 1.
DR Pfam; PF02309; AUX_IAA; 1.
DR PROSITE; PS51745; PB1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Auxin signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..229
FT /note="Auxin-responsive protein IAA17"
FT /id="PRO_0000112848"
FT DOMAIN 110..211
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT MOTIF 14..18
FT /note="EAR-like (transcriptional repression)"
FT MUTAGEN 16
FT /note="L->F: Suppresses the axr3-1 phenotype; when
FT associated with L-88."
FT /evidence="ECO:0000269|PubMed:9478901"
FT MUTAGEN 88
FT /note="P->L: In axr3-1; gain of function. Affects auxin-
FT related developmental processes. Affects
FT photomorphogenesis."
FT MUTAGEN 89
FT /note="V->G: In axr3-3; gain of function. Affects auxin-
FT related developmental processes. Affects
FT photomorphogenesis."
FT MUTAGEN 114
FT /note="K->A: No effect on interaction with ARF7."
FT /evidence="ECO:0000269|PubMed:24706860"
FT MUTAGEN 118
FT /note="D->N: Suppresses the axr3-1 phenotype; when
FT associated with L-88."
FT /evidence="ECO:0000269|PubMed:9478901"
FT MUTAGEN 121
FT /note="P->S: Suppresses the axr3-1 phenotype; when
FT associated with L-88."
FT /evidence="ECO:0000269|PubMed:9478901"
FT MUTAGEN 183
FT /note="D->A: No effect on interaction with ARF7; when
FT associated with A-187. Loss of interaction with ARF7; when
FT associated with A-114 and A-187."
FT /evidence="ECO:0000269|PubMed:24706860"
FT MUTAGEN 187
FT /note="D->A: No effect on interaction with ARF7; when
FT associated with A-183. Loss of interaction with ARF7; when
FT associated with A-114 and A-183."
FT /evidence="ECO:0000269|PubMed:24706860"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6L5K"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6L5K"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6L5K"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:6L5K"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6L5K"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2MUK"
FT TURN 156..162
FT /evidence="ECO:0007829|PDB:2MUK"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2MUK"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2MUK"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6L5K"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6L5K"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:6L5K"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6L5K"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2MUK"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2MUK"
SQ SEQUENCE 229 AA; 25288 MW; ECEA39207476581E CRC64;
MMGSVELNLR ETELCLGLPG GDTVAPVTGN KRGFSETVDL KLNLNNEPAN KEGSTTHDVV
TFDSKEKSAC PKDPAKPPAK AQVVGWPPVR SYRKNVMVSC QKSSGGPEAA AFVKVSMDGA
PYLRKIDLRM YKSYDELSNA LSNMFSSFTM GKHGGEEGMI DFMNERKLMD LVNSWDYVPS
YEDKDGDWML VGDVPWPMFV DTCKRLRLMK GSDAIGLAPR AMEKCKSRA
