IAA18_ARATH
ID IAA18_ARATH Reviewed; 267 AA.
AC O24408; Q8L9I9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Auxin-responsive protein IAA18;
DE AltName: Full=Indoleacetic acid-induced protein 18;
GN Name=IAA18; OrderedLocusNames=At1g51950; ORFNames=T14L22.14;
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-267.
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 [6]
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 [7]
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 [8]
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).
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 (By similarity). Interacts with
CC TPL. {ECO:0000250, ECO:0000269|PubMed:18258861}.
CC -!- INTERACTION:
CC O24408; Q9C5W9: ARF18; NbExp=8; IntAct=EBI-2295525, EBI-3946783;
CC O24408; Q8RYC8: ARF19; NbExp=5; IntAct=EBI-2295525, EBI-529887;
CC O24408; Q94JM3: ARF2; NbExp=3; IntAct=EBI-2295525, EBI-1799262;
CC O24408; P93022: ARF7; NbExp=3; IntAct=EBI-2295525, EBI-632284;
CC O24408; Q9SQI2: GI; NbExp=3; IntAct=EBI-2295525, EBI-446380;
CC O24408; Q9LV52: HSFC1; NbExp=3; IntAct=EBI-2295525, EBI-4457746;
CC O24408; P49677: IAA1; NbExp=6; IntAct=EBI-2295525, EBI-630505;
CC O24408; Q38828: IAA10; NbExp=5; IntAct=EBI-2295525, EBI-3946434;
CC O24408; Q38830: IAA12; NbExp=5; IntAct=EBI-2295525, EBI-617608;
CC O24408; Q38831: IAA13; NbExp=3; IntAct=EBI-2295525, EBI-1554143;
CC O24408; A0A2H1ZEF6: IAA15; NbExp=3; IntAct=EBI-2295525, EBI-25524519;
CC O24408; O24407: IAA16; NbExp=4; IntAct=EBI-2295525, EBI-632231;
CC O24408; P93830: IAA17; NbExp=7; IntAct=EBI-2295525, EBI-632243;
CC O24408; O24409: IAA19; NbExp=3; IntAct=EBI-2295525, EBI-632257;
CC O24408; P49678: IAA2; NbExp=4; IntAct=EBI-2295525, EBI-632343;
CC O24408; O24410: IAA20; NbExp=4; IntAct=EBI-2295525, EBI-632272;
CC O24408; Q8LAL2: IAA26; NbExp=3; IntAct=EBI-2295525, EBI-3947418;
CC O24408; Q9ZSY8: IAA27; NbExp=4; IntAct=EBI-2295525, EBI-3946677;
CC O24408; Q9XFM0: IAA28; NbExp=7; IntAct=EBI-2295525, EBI-3133404;
CC O24408; Q38822: IAA3; NbExp=7; IntAct=EBI-2295525, EBI-307174;
CC O24408; Q8H174: IAA31; NbExp=5; IntAct=EBI-2295525, EBI-3946408;
CC O24408; P33077: IAA4; NbExp=4; IntAct=EBI-2295525, EBI-632187;
CC O24408; Q38824: IAA6; NbExp=3; IntAct=EBI-2295525, EBI-1554124;
CC O24408; Q38825: IAA7; NbExp=5; IntAct=EBI-2295525, EBI-602959;
CC O24408; Q38826: IAA8; NbExp=6; IntAct=EBI-2295525, EBI-632200;
CC O24408; Q39023: MPK3; NbExp=3; IntAct=EBI-2295525, EBI-349526;
CC O24408; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2295525, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
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DR EMBL; AC015448; AAF99863.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32738.1; -; Genomic_DNA.
DR EMBL; AF367263; AAK56252.1; -; mRNA.
DR EMBL; AY056062; AAL06962.1; -; mRNA.
DR EMBL; AY088406; AAM65943.1; -; mRNA.
DR EMBL; U49074; AAB84355.1; -; mRNA.
DR PIR; H96558; H96558.
DR RefSeq; NP_175607.1; NM_104076.4.
DR AlphaFoldDB; O24408; -.
DR SMR; O24408; -.
DR BioGRID; 26848; 44.
DR DIP; DIP-54845N; -.
DR ELM; O24408; -.
DR IntAct; O24408; 43.
DR STRING; 3702.AT1G51950.1; -.
DR PaxDb; O24408; -.
DR PRIDE; O24408; -.
DR ProteomicsDB; 228811; -.
DR EnsemblPlants; AT1G51950.1; AT1G51950.1; AT1G51950.
DR GeneID; 841623; -.
DR Gramene; AT1G51950.1; AT1G51950.1; AT1G51950.
DR KEGG; ath:AT1G51950; -.
DR Araport; AT1G51950; -.
DR TAIR; locus:2195820; AT1G51950.
DR eggNOG; ENOG502QPYY; Eukaryota.
DR HOGENOM; CLU_049393_2_2_1; -.
DR InParanoid; O24408; -.
DR OMA; QTAGCIK; -.
DR OrthoDB; 1210341at2759; -.
DR PhylomeDB; O24408; -.
DR PRO; PR:O24408; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O24408; baseline and differential.
DR Genevisible; O24408; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; TAS: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 Auxin signaling pathway; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..267
FT /note="Auxin-responsive protein IAA18"
FT /id="PRO_0000112849"
FT DOMAIN 149..248
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 81..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..46
FT /note="EAR-like (transcriptional repression)"
FT CONFLICT 26
FT /note="W -> S (in Ref. 4; AAM65943)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="M -> I (in Ref. 4; AAM65943)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="Y -> H (in Ref. 4; AAM65943)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> D (in Ref. 4; AAM65943)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Missing (in Ref. 5; AAB84355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29898 MW; F1DC7E50172B7B10 CRC64;
MEGYSRNGEI SPKLLDLMIP QERRNWFHDE KNSVFKTEEK KLELKLGPPG EEDDDESMIR
HMKKEPKDKS ILSLAGKYFS PSSTKTTSHK RTAPGPVVGW PPVRSFRKNL ASGSSSKLGN
DSTTSNGVTL KNQKCDAAAK TTEPKRQGGM FVKINMYGVP IGRKVDLSAH NSYEQLSFTV
DKLFRGLLAA QRDFPSSIED EKPITGLLDG NGEYTLTYED NEGDKMLVGD VPWQMFVSSV
KRLRVIKTSE ISSALTYGNG KQEKMRR
