IAA6_ARATH
ID IAA6_ARATH Reviewed; 189 AA.
AC Q38824; Q8LEM1; Q9C539;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Auxin-responsive protein IAA6;
DE AltName: Full=Indoleacetic acid-induced protein 6;
GN Name=IAA6; Synonyms=SHY1; OrderedLocusNames=At1g52830; ORFNames=F14G24.10;
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=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].
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 [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 [6]
RP MUTANT SHY1-1.
RX PubMed=8624510; DOI=10.1046/j.1365-313x.1996.09040441.x;
RA Kim B.C., Soh M.S., Kang B.J., Furuya M., Nam H.G.;
RT "Two dominant photomorphogenic mutations of Arabidopsis thaliana identified
RT as suppressor mutations of hy2.";
RL Plant J. 9:441-456(1996).
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 Q38824; Q9C5W9: ARF18; NbExp=3; IntAct=EBI-1554124, EBI-3946783;
CC Q38824; Q9FIK2: At5g47790; NbExp=3; IntAct=EBI-1554124, EBI-25523851;
CC Q38824; P49677: IAA1; NbExp=9; IntAct=EBI-1554124, EBI-630505;
CC Q38824; Q38828: IAA10; NbExp=9; IntAct=EBI-1554124, EBI-3946434;
CC Q38824; Q38829: IAA11; NbExp=7; IntAct=EBI-1554124, EBI-2367923;
CC Q38824; Q38830: IAA12; NbExp=5; IntAct=EBI-1554124, EBI-617608;
CC Q38824; Q38831: IAA13; NbExp=8; IntAct=EBI-1554124, EBI-1554143;
CC Q38824; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-1554124, EBI-25524519;
CC Q38824; O24407: IAA16; NbExp=8; IntAct=EBI-1554124, EBI-632231;
CC Q38824; P93830: IAA17; NbExp=8; IntAct=EBI-1554124, EBI-632243;
CC Q38824; O24408: IAA18; NbExp=3; IntAct=EBI-1554124, EBI-2295525;
CC Q38824; O24409: IAA19; NbExp=8; IntAct=EBI-1554124, EBI-632257;
CC Q38824; P49678: IAA2; NbExp=7; IntAct=EBI-1554124, EBI-632343;
CC Q38824; O24410: IAA20; NbExp=5; IntAct=EBI-1554124, EBI-632272;
CC Q38824; Q8LAL2: IAA26; NbExp=8; IntAct=EBI-1554124, EBI-3947418;
CC Q38824; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-1554124, EBI-3946677;
CC Q38824; Q9XFM0: IAA28; NbExp=9; IntAct=EBI-1554124, EBI-3133404;
CC Q38824; Q38822: IAA3; NbExp=8; IntAct=EBI-1554124, EBI-307174;
CC Q38824; Q8H174: IAA31; NbExp=9; IntAct=EBI-1554124, EBI-3946408;
CC Q38824; Q8RYC6: IAA32; NbExp=3; IntAct=EBI-1554124, EBI-3946448;
CC Q38824; Q9FKM7: IAA33; NbExp=5; IntAct=EBI-1554124, EBI-3946739;
CC Q38824; Q9C5X0: IAA34; NbExp=8; IntAct=EBI-1554124, EBI-3946459;
CC Q38824; P33077: IAA4; NbExp=10; IntAct=EBI-1554124, EBI-632187;
CC Q38824; P33078: IAA5; NbExp=5; IntAct=EBI-1554124, EBI-3946487;
CC Q38824; Q38824: IAA6; NbExp=4; IntAct=EBI-1554124, EBI-1554124;
CC Q38824; Q38826: IAA8; NbExp=5; IntAct=EBI-1554124, EBI-632200;
CC Q38824; Q38827: IAA9; NbExp=3; IntAct=EBI-1554124, EBI-632216;
CC Q38824; Q9XI84: LSMT-L; NbExp=3; IntAct=EBI-1554124, EBI-15192835;
CC Q38824; O22179: MYB70; NbExp=3; IntAct=EBI-1554124, EBI-1238013;
CC Q38824; O23160: MYB73; NbExp=3; IntAct=EBI-1554124, EBI-25506855;
CC Q38824; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1554124, EBI-4426144;
CC Q38824; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-1554124, EBI-25522447;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly 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; U18408; AAC49047.1; -; mRNA.
DR EMBL; AC019018; AAG52268.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32858.1; -; Genomic_DNA.
DR EMBL; AF336915; AAG53996.1; -; mRNA.
DR EMBL; AY085353; AAM62583.1; -; mRNA.
DR PIR; E96569; E96569.
DR PIR; S58493; S58493.
DR RefSeq; NP_175692.1; NM_104161.3.
DR AlphaFoldDB; Q38824; -.
DR SMR; Q38824; -.
DR BioGRID; 26942; 41.
DR ELM; Q38824; -.
DR IntAct; Q38824; 41.
DR STRING; 3702.AT1G52830.1; -.
DR PaxDb; Q38824; -.
DR PRIDE; Q38824; -.
DR EnsemblPlants; AT1G52830.1; AT1G52830.1; AT1G52830.
DR GeneID; 841717; -.
DR Gramene; AT1G52830.1; AT1G52830.1; AT1G52830.
DR KEGG; ath:AT1G52830; -.
DR Araport; AT1G52830; -.
DR TAIR; locus:2011461; AT1G52830.
DR eggNOG; ENOG502RXTN; Eukaryota.
DR HOGENOM; CLU_049393_0_1_1; -.
DR InParanoid; Q38824; -.
DR OMA; WEMFKES; -.
DR OrthoDB; 1208467at2759; -.
DR PhylomeDB; Q38824; -.
DR PRO; PR:Q38824; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38824; baseline and differential.
DR Genevisible; Q38824; AT.
DR GO; GO:0005634; C:nucleus; ISS: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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009704; P:de-etiolation; 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 Auxin signaling pathway; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..189
FT /note="Auxin-responsive protein IAA6"
FT /id="PRO_0000112837"
FT DOMAIN 93..178
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT MOTIF 13..17
FT /note="EAR-like (transcriptional repression)"
FT MUTAGEN 78
FT /note="C->R: In shy1-1; gain of function. Affects auxin-
FT related developmental processes. Affects
FT photomorphogenesis."
FT CONFLICT 17
FT /note="L -> I (in Ref. 5; AAM62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="V -> I (in Ref. 5; AAM62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="K -> N (in Ref. 1; AAC49047)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="A -> S (in Ref. 5; AAM62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> N (in Ref. 5; AAM62583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21031 MW; 5E9B130584A75465 CRC64;
MAKEGLALEI TELRLGLPGD NYSEISVCGS SKKKKRVLSD MMTSSALDTE NENSVVSSVE
DESLPVVKSQ AVGWPPVCSY RRKKNNEEAS KAIGYVKVSM DGVPYMRKID LGSSNSYINL
VTVLENLFGC LGIGVAKEGK KCEYIIIYED KDRDWMLVGD VPWQMFKESC KRLRIVKRSD
ATGFGLQQD
