IAA11_ARATH
ID IAA11_ARATH Reviewed; 246 AA.
AC Q38829; Q8LPJ8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Auxin-responsive protein IAA11;
DE AltName: Full=Indoleacetic acid-induced protein 11;
GN Name=IAA11; OrderedLocusNames=At4g28640; ORFNames=T5F17.90;
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], 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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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 Q38829; Q8RYC8: ARF19; NbExp=3; IntAct=EBI-2367923, EBI-529887;
CC Q38829; O80902: CIPK22; NbExp=4; IntAct=EBI-2367923, EBI-4453230;
CC Q38829; Q94AY3: DRIP2; NbExp=3; IntAct=EBI-2367923, EBI-1787347;
CC Q38829; P49677: IAA1; NbExp=5; IntAct=EBI-2367923, EBI-630505;
CC Q38829; Q38828: IAA10; NbExp=6; IntAct=EBI-2367923, EBI-3946434;
CC Q38829; Q38831: IAA13; NbExp=6; IntAct=EBI-2367923, EBI-1554143;
CC Q38829; A0A2H1ZEF6: IAA15; NbExp=3; IntAct=EBI-2367923, EBI-25524519;
CC Q38829; O24407: IAA16; NbExp=8; IntAct=EBI-2367923, EBI-632231;
CC Q38829; P93830: IAA17; NbExp=8; IntAct=EBI-2367923, EBI-632243;
CC Q38829; O24409: IAA19; NbExp=7; IntAct=EBI-2367923, EBI-632257;
CC Q38829; P49678: IAA2; NbExp=6; IntAct=EBI-2367923, EBI-632343;
CC Q38829; O24410: IAA20; NbExp=3; IntAct=EBI-2367923, EBI-632272;
CC Q38829; Q8LAL2: IAA26; NbExp=8; IntAct=EBI-2367923, EBI-3947418;
CC Q38829; Q9ZSY8: IAA27; NbExp=7; IntAct=EBI-2367923, EBI-3946677;
CC Q38829; Q9XFM0: IAA28; NbExp=9; IntAct=EBI-2367923, EBI-3133404;
CC Q38829; Q38822: IAA3; NbExp=7; IntAct=EBI-2367923, EBI-307174;
CC Q38829; Q8H174: IAA31; NbExp=8; IntAct=EBI-2367923, EBI-3946408;
CC Q38829; P33077: IAA4; NbExp=7; IntAct=EBI-2367923, EBI-632187;
CC Q38829; Q38824: IAA6; NbExp=7; IntAct=EBI-2367923, EBI-1554124;
CC Q38829; Q38825: IAA7; NbExp=3; IntAct=EBI-2367923, EBI-602959;
CC Q38829; Q38826: IAA8; NbExp=6; IntAct=EBI-2367923, EBI-632200;
CC Q38829; O22179: MYB70; NbExp=3; IntAct=EBI-2367923, EBI-1238013;
CC Q38829; Q9C8Y3: RGL1; NbExp=3; IntAct=EBI-2367923, EBI-963647;
CC Q38829; Q05153: SSRP1; NbExp=3; IntAct=EBI-2367923, EBI-15191543;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q38829-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in stems and flowers.
CC {ECO:0000269|PubMed:7658471}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:7658471}.
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; U18413; AAC49052.1; -; mRNA.
DR EMBL; AL161573; CAB81452.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85515.1; -; Genomic_DNA.
DR EMBL; AK118377; BAC42989.1; -; mRNA.
DR EMBL; AF332397; AAG48761.1; -; mRNA.
DR EMBL; AY099670; AAM20521.1; -; mRNA.
DR EMBL; BT000261; AAN15580.1; -; mRNA.
DR PIR; S58497; S58497.
DR RefSeq; NP_194593.1; NM_119006.3. [Q38829-1]
DR AlphaFoldDB; Q38829; -.
DR SMR; Q38829; -.
DR BioGRID; 14269; 69.
DR ELM; Q38829; -.
DR IntAct; Q38829; 64.
DR STRING; 3702.AT4G28640.2; -.
DR PaxDb; Q38829; -.
DR EnsemblPlants; AT4G28640.1; AT4G28640.1; AT4G28640. [Q38829-1]
DR GeneID; 828982; -.
DR Gramene; AT4G28640.1; AT4G28640.1; AT4G28640. [Q38829-1]
DR KEGG; ath:AT4G28640; -.
DR Araport; AT4G28640; -.
DR eggNOG; ENOG502R053; Eukaryota.
DR HOGENOM; CLU_049393_3_0_1; -.
DR InParanoid; Q38829; -.
DR OMA; MRTHEAN; -.
DR PhylomeDB; Q38829; -.
DR PRO; PR:Q38829; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38829; baseline and differential.
DR Genevisible; Q38829; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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 Alternative splicing; Auxin signaling pathway; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..246
FT /note="Auxin-responsive protein IAA11"
FT /id="PRO_0000112842"
FT DOMAIN 136..235
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT MOTIF 36..40
FT /note="EAR-like (transcriptional repression)"
FT CONFLICT 21
FT /note="V -> I (in Ref. 5; AAM20521/AAN15580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26516 MW; 449054E312FBBDAD CRC64;
MEGGSASGSA SALSNDENLV VSCEDSSSPI GNELELGLTL SLGRKGYRDC RVYADDSSSS
SSSSSLSRAS VIAGIKRTAD SMAATSGQVV GWPPIRTYRM NSMVNQAKAS ATEDPNLEIS
QAVNKNRSDS TKMRNSMFVK VTMDGIPIGR KIDLNAHKCY ESLSNTLEEM FLKPKLGSRT
LETDGHMETP VKILPDGSSG LVLTYEDKEG DWMLVGDVPW GMFIGSVRRL RIMKTSEATG
KAQMIL
