IAA14_ARATH
ID IAA14_ARATH Reviewed; 228 AA.
AC Q38832; O23311; Q9C5W8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Auxin-responsive protein IAA14;
DE AltName: Full=Indoleacetic acid-induced protein 14;
DE AltName: Full=Protein SOLITARY ROOT;
GN Name=IAA14; Synonyms=SLR1; OrderedLocusNames=At4g14550;
GN ORFNames=dl3315c, FCAALL.254;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 [MRNA] OF 65-228, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7658471; DOI=10.1006/jmbi.1995.0454;
RA Abel S., Nguyen M.D., Theologis A.;
RT "The PS-IAA4/5-like family of early auxin-inducible mRNAs in Arabidopsis
RT thaliana.";
RL J. Mol. Biol. 251:533-549(1995).
RN [6]
RP MUTANT SLR1-1.
RX PubMed=11862947; DOI=10.1046/j.0960-7412.2001.01201.x;
RA Fukaki H., Tameda S., Masuda H., Tasaka M.;
RT "Lateral root formation is blocked by a gain-of-function mutation in the
RT SOLITARY-ROOT/IAA14 gene of Arabidopsis.";
RL Plant J. 29:153-168(2002).
RN [7]
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 [8]
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 [9]
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 Q38832; Q8RYC8: ARF19; NbExp=4; IntAct=EBI-2295562, EBI-529887;
CC Q38832; P93024: ARF5; NbExp=3; IntAct=EBI-2295562, EBI-629519;
CC Q38832; P93022: ARF7; NbExp=3; IntAct=EBI-2295562, EBI-632284;
CC Q38832; P49677: IAA1; NbExp=3; IntAct=EBI-2295562, EBI-630505;
CC Q38832; Q38828: IAA10; NbExp=3; IntAct=EBI-2295562, EBI-3946434;
CC Q38832; Q38830: IAA12; NbExp=4; IntAct=EBI-2295562, EBI-617608;
CC Q38832; Q38831: IAA13; NbExp=4; IntAct=EBI-2295562, EBI-1554143;
CC Q38832; P93830: IAA17; NbExp=4; IntAct=EBI-2295562, EBI-632243;
CC Q38832; O24409: IAA19; NbExp=4; IntAct=EBI-2295562, EBI-632257;
CC Q38832; P49678: IAA2; NbExp=4; IntAct=EBI-2295562, EBI-632343;
CC Q38832; Q8LAL2: IAA26; NbExp=4; IntAct=EBI-2295562, EBI-3947418;
CC Q38832; Q9ZSY8: IAA27; NbExp=3; IntAct=EBI-2295562, EBI-3946677;
CC Q38832; Q9XFM0: IAA28; NbExp=4; IntAct=EBI-2295562, EBI-3133404;
CC Q38832; Q38822: IAA3; NbExp=4; IntAct=EBI-2295562, EBI-307174;
CC Q38832; Q8H174: IAA31; NbExp=3; IntAct=EBI-2295562, EBI-3946408;
CC Q38832; Q9C5X0: IAA34; NbExp=3; IntAct=EBI-2295562, EBI-3946459;
CC Q38832; P33077: IAA4; NbExp=4; IntAct=EBI-2295562, EBI-632187;
CC Q38832; P33078: IAA5; NbExp=4; IntAct=EBI-2295562, EBI-3946487;
CC Q38832; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2295562, EBI-4426144;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in roots and flowers.
CC {ECO:0000269|PubMed:7658471}.
CC -!- INDUCTION: By auxin. {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB46059.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78497.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97336; CAB46059.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161539; CAB78497.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83459.1; -; Genomic_DNA.
DR EMBL; AF334718; AAG50096.1; -; mRNA.
DR EMBL; U18416; AAC49055.1; -; mRNA.
DR PIR; C85159; C85159.
DR PIR; H71407; H71407.
DR PIR; S58501; S58501.
DR RefSeq; NP_001329483.1; NM_001340945.1.
DR RefSeq; NP_193191.2; NM_117535.5.
DR AlphaFoldDB; Q38832; -.
DR SMR; Q38832; -.
DR BioGRID; 12399; 38.
DR DIP; DIP-53499N; -.
DR ELM; Q38832; -.
DR IntAct; Q38832; 32.
DR STRING; 3702.AT4G14550.1; -.
DR PaxDb; Q38832; -.
DR PRIDE; Q38832; -.
DR EnsemblPlants; AT4G14550.1; AT4G14550.1; AT4G14550.
DR GeneID; 827102; -.
DR Gramene; AT4G14550.1; AT4G14550.1; AT4G14550.
DR KEGG; ath:AT4G14550; -.
DR Araport; AT4G14550; -.
DR TAIR; locus:2129900; AT4G14550.
DR eggNOG; ENOG502QPNB; Eukaryota.
DR HOGENOM; CLU_049393_1_5_1; -.
DR InParanoid; Q38832; -.
DR OMA; PARMEPS; -.
DR OrthoDB; 1203639at2759; -.
DR PhylomeDB; Q38832; -.
DR PRO; PR:Q38832; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38832; baseline and differential.
DR Genevisible; Q38832; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010102; P:lateral root morphogenesis; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
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..228
FT /note="Auxin-responsive protein IAA14"
FT /id="PRO_0000112845"
FT DOMAIN 110..210
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT MOTIF 8..12
FT /note="EAR-like (transcriptional repression)"
FT MUTAGEN 82
FT /note="P->S: In slr1-1; gain of function. Affects auxin-
FT related developmental processes."
SQ SEQUENCE 228 AA; 25044 MW; A76A9F733538E372 CRC64;
MNLKETELCL GLPGGTETVE SPAKSGVGNK RGFSETVDLK LNLQSNKQGH VDLNTNGAPK
EKTFLKDPSK PPAKAQVVGW PPVRNYRKNV MANQKSGEAE EAMSSGGGTV AFVKVSMDGA
PYLRKVDLKM YTSYKDLSDA LAKMFSSFTM GSYGAQGMID FMNESKVMDL LNSSEYVPSY
EDKDGDWMLV GDVPWPMFVE SCKRLRIMKG SEAIGLAPRA MEKFKNRS
