IAA34_ARATH
ID IAA34_ARATH Reviewed; 185 AA.
AC Q9C5X0; Q9M9Q0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Auxin-responsive protein IAA34;
DE AltName: Full=Indoleacetic acid-induced protein 34;
GN Name=IAA34; OrderedLocusNames=At1g15050; ORFNames=T15D22.10;
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].
RC STRAIN=cv. Columbia;
RA Sessa G., Carabelli M., Ciarbelli A.R., Ruzza V., Steindler C., Ruberti I.;
RT "Nucleotide sequence of the Arabidopsis IAA29.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
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).
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. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9C5X0; Q9FIW5: ANAC094; NbExp=3; IntAct=EBI-3946459, EBI-25522986;
CC Q9C5X0; Q8L7G0: ARF1; NbExp=4; IntAct=EBI-3946459, EBI-2324259;
CC Q9C5X0; Q9C5W9: ARF18; NbExp=4; IntAct=EBI-3946459, EBI-3946783;
CC Q9C5X0; Q8RYC8: ARF19; NbExp=4; IntAct=EBI-3946459, EBI-529887;
CC Q9C5X0; Q94JM3: ARF2; NbExp=6; IntAct=EBI-3946459, EBI-1799262;
CC Q9C5X0; Q9XED8: ARF9; NbExp=4; IntAct=EBI-3946459, EBI-3946762;
CC Q9C5X0; Q9FIK2: At5g47790; NbExp=3; IntAct=EBI-3946459, EBI-25523851;
CC Q9C5X0; Q9LST3: At5g60142; NbExp=3; IntAct=EBI-3946459, EBI-15192745;
CC Q9C5X0; Q38897: BEL1; NbExp=3; IntAct=EBI-3946459, EBI-1153783;
CC Q9C5X0; Q8S3D2: BHLH87; NbExp=3; IntAct=EBI-3946459, EBI-15194565;
CC Q9C5X0; Q9SKT1: ERF053; NbExp=6; IntAct=EBI-3946459, EBI-25511859;
CC Q9C5X0; Q6J9Q2: ERF086; NbExp=3; IntAct=EBI-3946459, EBI-15202888;
CC Q9C5X0; Q9FYK5: ESR2; NbExp=3; IntAct=EBI-3946459, EBI-1536925;
CC Q9C5X0; Q8L8A6: GRF5; NbExp=3; IntAct=EBI-3946459, EBI-1396652;
CC Q9C5X0; P49677: IAA1; NbExp=6; IntAct=EBI-3946459, EBI-630505;
CC Q9C5X0; Q38828: IAA10; NbExp=11; IntAct=EBI-3946459, EBI-3946434;
CC Q9C5X0; Q38831: IAA13; NbExp=6; IntAct=EBI-3946459, EBI-1554143;
CC Q9C5X0; Q38832: IAA14; NbExp=3; IntAct=EBI-3946459, EBI-2295562;
CC Q9C5X0; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-3946459, EBI-25524519;
CC Q9C5X0; O24407: IAA16; NbExp=6; IntAct=EBI-3946459, EBI-632231;
CC Q9C5X0; P93830: IAA17; NbExp=11; IntAct=EBI-3946459, EBI-632243;
CC Q9C5X0; O24409: IAA19; NbExp=8; IntAct=EBI-3946459, EBI-632257;
CC Q9C5X0; P49678: IAA2; NbExp=6; IntAct=EBI-3946459, EBI-632343;
CC Q9C5X0; O24410: IAA20; NbExp=6; IntAct=EBI-3946459, EBI-632272;
CC Q9C5X0; Q8LAL2: IAA26; NbExp=7; IntAct=EBI-3946459, EBI-3947418;
CC Q9C5X0; Q9ZSY8: IAA27; NbExp=8; IntAct=EBI-3946459, EBI-3946677;
CC Q9C5X0; Q9XFM0: IAA28; NbExp=8; IntAct=EBI-3946459, EBI-3133404;
CC Q9C5X0; Q38822: IAA3; NbExp=9; IntAct=EBI-3946459, EBI-307174;
CC Q9C5X0; Q8H174: IAA31; NbExp=8; IntAct=EBI-3946459, EBI-3946408;
CC Q9C5X0; Q9FKM7: IAA33; NbExp=9; IntAct=EBI-3946459, EBI-3946739;
CC Q9C5X0; P33077: IAA4; NbExp=6; IntAct=EBI-3946459, EBI-632187;
CC Q9C5X0; P33078: IAA5; NbExp=6; IntAct=EBI-3946459, EBI-3946487;
CC Q9C5X0; Q38824: IAA6; NbExp=8; IntAct=EBI-3946459, EBI-1554124;
CC Q9C5X0; Q38825: IAA7; NbExp=10; IntAct=EBI-3946459, EBI-602959;
CC Q9C5X0; Q38826: IAA8; NbExp=6; IntAct=EBI-3946459, EBI-632200;
CC Q9C5X0; Q38827: IAA9; NbExp=4; IntAct=EBI-3946459, EBI-632216;
CC Q9C5X0; O65154: KIWI; NbExp=3; IntAct=EBI-3946459, EBI-2112286;
CC Q9C5X0; Q9LTC4: MYB15; NbExp=3; IntAct=EBI-3946459, EBI-21497119;
CC Q9C5X0; O22179: MYB70; NbExp=3; IntAct=EBI-3946459, EBI-1238013;
CC Q9C5X0; O23160: MYB73; NbExp=3; IntAct=EBI-3946459, EBI-25506855;
CC Q9C5X0; Q9SFD8: NFYB9; NbExp=3; IntAct=EBI-3946459, EBI-2475789;
CC Q9C5X0; O82239: RFI2; NbExp=3; IntAct=EBI-3946459, EBI-4425094;
CC Q9C5X0; Q9XGX0: SHI; NbExp=3; IntAct=EBI-3946459, EBI-15205274;
CC Q9C5X0; Q9FUA4: SPT; NbExp=3; IntAct=EBI-3946459, EBI-1536703;
CC Q9C5X0; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-3946459, EBI-4424877;
CC Q9C5X0; Q9C9L2: TCP15; NbExp=5; IntAct=EBI-3946459, EBI-4426144;
CC Q9C5X0; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-3946459, EBI-25522447;
CC Q9C5X0; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-3946459, EBI-15192325;
CC Q9C5X0; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-3946459, EBI-4424568;
CC Q9C5X0; O64722: ZHD3; NbExp=4; IntAct=EBI-3946459, EBI-1806244;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 -!- CAUTION: Was originally (Ref.1) erroneously named IAA29. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31028.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ458327; CAD30209.1; -; mRNA.
DR EMBL; AC012189; AAF31028.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29261.1; -; Genomic_DNA.
DR EMBL; AF334713; AAG50091.1; -; mRNA.
DR PIR; B86284; B86284.
DR RefSeq; NP_172959.2; NM_101375.3.
DR AlphaFoldDB; Q9C5X0; -.
DR SMR; Q9C5X0; -.
DR BioGRID; 23310; 70.
DR IntAct; Q9C5X0; 67.
DR STRING; 3702.AT1G15050.1; -.
DR PaxDb; Q9C5X0; -.
DR PRIDE; Q9C5X0; -.
DR DNASU; 838070; -.
DR EnsemblPlants; AT1G15050.1; AT1G15050.1; AT1G15050.
DR GeneID; 838070; -.
DR Gramene; AT1G15050.1; AT1G15050.1; AT1G15050.
DR KEGG; ath:AT1G15050; -.
DR Araport; AT1G15050; -.
DR TAIR; locus:2196184; AT1G15050.
DR eggNOG; ENOG502RZE6; Eukaryota.
DR HOGENOM; CLU_117411_0_0_1; -.
DR InParanoid; Q9C5X0; -.
DR OrthoDB; 1314275at2759; -.
DR PhylomeDB; Q9C5X0; -.
DR PRO; PR:Q9C5X0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5X0; baseline and differential.
DR Genevisible; Q9C5X0; 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; 2.
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..185
FT /note="Auxin-responsive protein IAA34"
FT /id="PRO_0000112860"
FT DOMAIN 92..180
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT MOTIF 63..67
FT /note="EAR-like (transcriptional repression)"
SQ SEQUENCE 185 AA; 21405 MW; 83D4F89CFC657BB7 CRC64;
MYCSDPPHPL HLVASDKQQK DHKLILSWKK PTMDSDPLGV FPNSPKYHPY YSQTTEFGGV
IDLGLSLRTI QHEIYHSSGQ RYCSNEGYRR KWGYVKVTMD GLVVGRKVCV LDHGSYSTLA
HQLEDMFGMQ SVSGLRLFQM ESEFCLVYRD EEGLWRNAGD VPWNEFIESV ERLRITRRND
AVLPF
