IAA3_ARATH
ID IAA3_ARATH Reviewed; 189 AA.
AC Q38822; O04741;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Auxin-responsive protein IAA3;
DE AltName: Full=Indoleacetic acid-induced protein 3;
DE AltName: Full=Short hypocotyl;
DE AltName: Full=Suppressor of HY2;
GN Name=IAA3; Synonyms=SHY2; OrderedLocusNames=At1g04240; ORFNames=F19P19.32;
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 FUNCTION, AND MUTAGENESIS OF GLY-67 AND PRO-69.
RX PubMed=9895319; DOI=10.1242/dev.126.4.711;
RA Tian Q., Reed J.W.;
RT "Control of auxin-regulated root development by the Arabidopsis thaliana
RT SHY2/IAA3 gene.";
RL Development 126:711-721(1999).
RN [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=11884676; DOI=10.1105/tpc.010283;
RA Tian Q., Uhlir N.J., Reed J.W.;
RT "Arabidopsis SHY2/IAA3 inhibits auxin-regulated gene expression.";
RL Plant Cell 14:301-319(2002).
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 TISSUE SPECIFICITY.
RX PubMed=14534134; DOI=10.1242/dev.00659;
RA Knox K., Grierson C.S., Leyser O.;
RT "AXR3 and SHY2 interact to regulate root hair development.";
RL Development 130:5769-5777(2003).
RN [10]
RP INTERACTION WITH TIR1.
RX PubMed=14617065; DOI=10.1046/j.1365-313x.2003.01909.x;
RA Tian Q., Nagpal P., Reed J.W.;
RT "Regulation of Arabidopsis SHY2/IAA3 protein turnover.";
RL Plant J. 36:643-651(2003).
RN [11]
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 [12]
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 [13]
RP INDUCTION BY ARR1, TISSUE SPECIFICITY, AND INDUCTION BY CYTOKININ.
RX PubMed=19039136; DOI=10.1126/science.1164147;
RA Dello Ioio R., Nakamura K., Moubayidin L., Perilli S., Taniguchi M.,
RA Morita M.T., Aoyama T., Costantino P., Sabatini S.;
RT "A genetic framework for the control of cell division and differentiation
RT in the root meristem.";
RL Science 322:1380-1384(2008).
RN [14]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20605455; DOI=10.1016/j.cub.2010.05.035;
RA Moubayidin L., Perilli S., Dello Ioio R., Di Mambro R., Costantino P.,
RA Sabatini S.;
RT "The rate of cell differentiation controls the Arabidopsis root meristem
RT growth phase.";
RL Curr. Biol. 20:1138-1143(2010).
RN [15]
RP FUNCTION.
RX PubMed=21149702; DOI=10.1073/pnas.1014716108;
RA Scacchi E., Salinas P., Gujas B., Santuari L., Krogan N., Ragni L.,
RA Berleth T., Hardtke C.S.;
RT "Spatio-temporal sequence of cross-regulatory events in root meristem
RT growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22734-22739(2010).
RN [16]
RP FUNCTION.
RX PubMed=23425316; DOI=10.1111/nph.12189;
RA Koren D., Resnick N., Mayzlish Gati E., Belausov E., Weininger S.,
RA Kapulnik Y., Koltai H.;
RT "Strigolactone signaling in the endodermis is sufficient to restore root
RT responses and involves SHORT HYPOCOTYL 2 (SHY2) activity.";
RL New Phytol. 198:866-874(2013).
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). Plays a central role in auxin
CC regulation of root growth, in gravitropism, and in lateral root
CC formation (PubMed:9895319). Regulated by an auxin-induced protein
CC turnover (PubMed:14617065). Formation of heterodimers with ARF proteins
CC may alter their ability to modulate early auxin response genes
CC expression. When activated by cytokinin, restricts the expression of
CC the PIN genes to the vascular transition zone (PubMed:19039136).
CC Induction of SHY2 in the vascular transition zone restricts BRX
CC expression to down-regulate PIN3 and thus limit meristem growth, but
CC proper SHY2 expression requires BRX (PubMed:21149702). Involved in
CC meristem growth and in determining its size (PubMed:20605455). May
CC participate in strigolactone signaling to regulate meristem size and
CC lateral root formation (PubMed:23425316). {ECO:0000269|PubMed:11884676,
CC ECO:0000269|PubMed:12036262, ECO:0000269|PubMed:14617065,
CC ECO:0000269|PubMed:19039136, ECO:0000269|PubMed:20605455,
CC ECO:0000269|PubMed:21149702, ECO:0000269|PubMed:23425316,
CC ECO:0000269|PubMed:9895319}.
CC -!- SUBUNIT: Homodimers and heterodimers (By similarity). Interacts with
CC TPL (PubMed:18258861). Interacts with TIR1, the F-box component of the
CC Skp1-Cdc53/cullin-F-box (SCFTIR1) E3 ubiquitin ligase complex
CC (PubMed:14617065). {ECO:0000250, ECO:0000269|PubMed:14617065,
CC ECO:0000269|PubMed:18258861}.
CC -!- INTERACTION:
CC Q38822; Q8RYC8: ARF19; NbExp=4; IntAct=EBI-307174, EBI-529887;
CC Q38822; P93022: ARF7; NbExp=2; IntAct=EBI-307174, EBI-632284;
CC Q38822; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-307174, EBI-1100737;
CC Q38822; O80533: At1g09500; NbExp=4; IntAct=EBI-307174, EBI-4447439;
CC Q38822; Q9LST3: At5g60142; NbExp=3; IntAct=EBI-307174, EBI-15192745;
CC Q38822; A0A384L1A6: AXX17_At5g51430; NbExp=3; IntAct=EBI-307174, EBI-25520864;
CC Q38822; P49677: IAA1; NbExp=13; IntAct=EBI-307174, EBI-630505;
CC Q38822; Q38828: IAA10; NbExp=10; IntAct=EBI-307174, EBI-3946434;
CC Q38822; Q38829: IAA11; NbExp=7; IntAct=EBI-307174, EBI-2367923;
CC Q38822; Q38830: IAA12; NbExp=8; IntAct=EBI-307174, EBI-617608;
CC Q38822; Q38831: IAA13; NbExp=9; IntAct=EBI-307174, EBI-1554143;
CC Q38822; Q38832: IAA14; NbExp=4; IntAct=EBI-307174, EBI-2295562;
CC Q38822; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-307174, EBI-25524519;
CC Q38822; O24407: IAA16; NbExp=12; IntAct=EBI-307174, EBI-632231;
CC Q38822; P93830: IAA17; NbExp=14; IntAct=EBI-307174, EBI-632243;
CC Q38822; O24408: IAA18; NbExp=7; IntAct=EBI-307174, EBI-2295525;
CC Q38822; O24409: IAA19; NbExp=11; IntAct=EBI-307174, EBI-632257;
CC Q38822; P49678: IAA2; NbExp=12; IntAct=EBI-307174, EBI-632343;
CC Q38822; O24410: IAA20; NbExp=6; IntAct=EBI-307174, EBI-632272;
CC Q38822; Q8LAL2: IAA26; NbExp=9; IntAct=EBI-307174, EBI-3947418;
CC Q38822; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-307174, EBI-3946677;
CC Q38822; Q9XFM0: IAA28; NbExp=10; IntAct=EBI-307174, EBI-3133404;
CC Q38822; Q38822: IAA3; NbExp=4; IntAct=EBI-307174, EBI-307174;
CC Q38822; Q8H174: IAA31; NbExp=10; IntAct=EBI-307174, EBI-3946408;
CC Q38822; Q8RYC6: IAA32; NbExp=5; IntAct=EBI-307174, EBI-3946448;
CC Q38822; Q9FKM7: IAA33; NbExp=3; IntAct=EBI-307174, EBI-3946739;
CC Q38822; Q9C5X0: IAA34; NbExp=9; IntAct=EBI-307174, EBI-3946459;
CC Q38822; P33077: IAA4; NbExp=9; IntAct=EBI-307174, EBI-632187;
CC Q38822; P33078: IAA5; NbExp=6; IntAct=EBI-307174, EBI-3946487;
CC Q38822; Q38824: IAA6; NbExp=8; IntAct=EBI-307174, EBI-1554124;
CC Q38822; Q38825: IAA7; NbExp=6; IntAct=EBI-307174, EBI-602959;
CC Q38822; Q38826: IAA8; NbExp=7; IntAct=EBI-307174, EBI-632200;
CC Q38822; Q38827: IAA9; NbExp=4; IntAct=EBI-307174, EBI-632216;
CC Q38822; O04294: IMPA3; NbExp=3; IntAct=EBI-307174, EBI-1644689;
CC Q38822; O22179: MYB70; NbExp=3; IntAct=EBI-307174, EBI-1238013;
CC Q38822; O23160: MYB73; NbExp=3; IntAct=EBI-307174, EBI-25506855;
CC Q38822; Q9C8Y3: RGL1; NbExp=3; IntAct=EBI-307174, EBI-963647;
CC Q38822; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-307174, EBI-4426144;
CC Q38822; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-307174, EBI-25522447;
CC Q38822; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-307174, EBI-4426557;
CC Q38822; Q570C0: TIR1; NbExp=3; IntAct=EBI-307174, EBI-307183;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems and flowers
CC (PubMed:7658471). Expressed in hypocotyls, cotyledons and leaves, but
CC barely detected in roots (PubMed:11884676). Expressed in root tips
CC (PubMed:14534134). In the root meristem, specifically detected at the
CC vascular tissue transition zone (PubMed:19039136).
CC {ECO:0000269|PubMed:11884676, ECO:0000269|PubMed:14534134,
CC ECO:0000269|PubMed:19039136, ECO:0000269|PubMed:7658471}.
CC -!- DEVELOPMENTAL STAGE: The level of expression increases during meristem
CC growth, reaches a maximum at 5 days post germination and subsequently
CC remaines constant in time. {ECO:0000269|PubMed:20605455}.
CC -!- INDUCTION: By auxin (PubMed:7658471). Up-regulated by cytokinin
CC treatment through the primary cytokinin-response transcription factor
CC ARR1 (PubMed:19039136). Down-regulated by light in the presence of
CC sucrose, but up-regulated in the absence of sucrose (PubMed:11884676).
CC {ECO:0000269|PubMed:11884676, ECO:0000269|PubMed:19039136,
CC 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 -!- PTM: Phosphorylated by phytochrome A in vitro.
CC {ECO:0000269|PubMed:11115889}.
CC -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
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DR EMBL; U18406; AAC49045.1; -; mRNA.
DR EMBL; AC000104; AAB70452.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27673.1; -; Genomic_DNA.
DR EMBL; AF332393; AAG48757.1; -; mRNA.
DR EMBL; AY064007; AAL36363.1; -; mRNA.
DR PIR; S58491; S58491.
DR RefSeq; NP_171920.1; NM_100305.4.
DR AlphaFoldDB; Q38822; -.
DR SMR; Q38822; -.
DR BioGRID; 24805; 65.
DR DIP; DIP-31741N; -.
DR ELM; Q38822; -.
DR IntAct; Q38822; 74.
DR STRING; 3702.AT1G04240.1; -.
DR PaxDb; Q38822; -.
DR PRIDE; Q38822; -.
DR DNASU; 839570; -.
DR EnsemblPlants; AT1G04240.1; AT1G04240.1; AT1G04240.
DR GeneID; 839570; -.
DR Gramene; AT1G04240.1; AT1G04240.1; AT1G04240.
DR KEGG; ath:AT1G04240; -.
DR Araport; AT1G04240; -.
DR TAIR; locus:2018379; AT1G04240.
DR eggNOG; ENOG502QU81; Eukaryota.
DR HOGENOM; CLU_049393_0_1_1; -.
DR InParanoid; Q38822; -.
DR PhylomeDB; Q38822; -.
DR PRO; PR:Q38822; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38822; baseline and differential.
DR Genevisible; Q38822; 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: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: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; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..189
FT /note="Auxin-responsive protein IAA3"
FT /id="PRO_0000112834"
FT DOMAIN 92..179
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 42..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..16
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 67
FT /note="G->E: In shy2-3; gain of function. Affects auxin-
FT related developmental processes. Affects
FT photomorphogenesis."
FT /evidence="ECO:0000269|PubMed:9895319"
FT MUTAGEN 69
FT /note="P->S: In shy2-2; gain of function. Affects auxin-
FT related developmental processes. Affects
FT photomorphogenesis."
FT /evidence="ECO:0000269|PubMed:9895319"
SQ SEQUENCE 189 AA; 21520 MW; 8627A4173363EF27 CRC64;
MDEFVNLKET ELRLGLPGTD NVCEAKERVS CCNNNNKRVL STDTEKEIES SSRKTETSPP
RKAQIVGWPP VRSYRKNNIQ SKKNESEHEG QGIYVKVSMD GAPYLRKIDL SCYKGYSELL
KALEVMFKFS VGEYFERDGY KGSDFVPTYE DKDGDWMLIG DVPWEMFICT CKRLRIMKGS
EAKGLGCGV
