IAA26_ARATH
ID IAA26_ARATH Reviewed; 269 AA.
AC Q8LAL2; Q9LK75; Q9ZSY7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Auxin-responsive protein IAA26;
DE AltName: Full=Indoleacetic acid-induced protein 26;
DE AltName: Full=Phytochrome-associated protein 1;
GN Name=IAA26; Synonyms=PAP1; OrderedLocusNames=At3g16500; ORFNames=MDC8.13;
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 Lee J., Yi H., Shin B., Song P.-S., Choi G.;
RT "Identification and characterization of three phytochrome-associated
RT proteins.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 phytochrome A. Interacts with TPL. {ECO:0000250,
CC ECO:0000269|PubMed:18258861}.
CC -!- INTERACTION:
CC Q8LAL2; Q9C5W9: ARF18; NbExp=7; IntAct=EBI-3947418, EBI-3946783;
CC Q8LAL2; Q94JM3: ARF2; NbExp=7; IntAct=EBI-3947418, EBI-1799262;
CC Q8LAL2; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-3947418, EBI-1100737;
CC Q8LAL2; Q501D3: At1g01920; NbExp=3; IntAct=EBI-3947418, EBI-15194159;
CC Q8LAL2; Q9FIK2: At5g47790; NbExp=3; IntAct=EBI-3947418, EBI-25523851;
CC Q8LAL2; O04292: ATHB-9; NbExp=4; IntAct=EBI-3947418, EBI-1536772;
CC Q8LAL2; Q9SQI2: GI; NbExp=3; IntAct=EBI-3947418, EBI-446380;
CC Q8LAL2; P49677: IAA1; NbExp=14; IntAct=EBI-3947418, EBI-630505;
CC Q8LAL2; Q38828: IAA10; NbExp=10; IntAct=EBI-3947418, EBI-3946434;
CC Q8LAL2; Q38829: IAA11; NbExp=8; IntAct=EBI-3947418, EBI-2367923;
CC Q8LAL2; Q38830: IAA12; NbExp=3; IntAct=EBI-3947418, EBI-617608;
CC Q8LAL2; Q38831: IAA13; NbExp=8; IntAct=EBI-3947418, EBI-1554143;
CC Q8LAL2; Q38832: IAA14; NbExp=4; IntAct=EBI-3947418, EBI-2295562;
CC Q8LAL2; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-3947418, EBI-25524519;
CC Q8LAL2; O24407: IAA16; NbExp=9; IntAct=EBI-3947418, EBI-632231;
CC Q8LAL2; P93830: IAA17; NbExp=9; IntAct=EBI-3947418, EBI-632243;
CC Q8LAL2; O24408: IAA18; NbExp=3; IntAct=EBI-3947418, EBI-2295525;
CC Q8LAL2; O24409: IAA19; NbExp=9; IntAct=EBI-3947418, EBI-632257;
CC Q8LAL2; P49678: IAA2; NbExp=10; IntAct=EBI-3947418, EBI-632343;
CC Q8LAL2; O24410: IAA20; NbExp=5; IntAct=EBI-3947418, EBI-632272;
CC Q8LAL2; Q8LAL2: IAA26; NbExp=3; IntAct=EBI-3947418, EBI-3947418;
CC Q8LAL2; Q9ZSY8: IAA27; NbExp=8; IntAct=EBI-3947418, EBI-3946677;
CC Q8LAL2; Q9XFM0: IAA28; NbExp=8; IntAct=EBI-3947418, EBI-3133404;
CC Q8LAL2; Q38822: IAA3; NbExp=9; IntAct=EBI-3947418, EBI-307174;
CC Q8LAL2; Q8H174: IAA31; NbExp=5; IntAct=EBI-3947418, EBI-3946408;
CC Q8LAL2; Q8RYC6: IAA32; NbExp=5; IntAct=EBI-3947418, EBI-3946448;
CC Q8LAL2; Q9FKM7: IAA33; NbExp=5; IntAct=EBI-3947418, EBI-3946739;
CC Q8LAL2; Q9C5X0: IAA34; NbExp=7; IntAct=EBI-3947418, EBI-3946459;
CC Q8LAL2; P33077: IAA4; NbExp=8; IntAct=EBI-3947418, EBI-632187;
CC Q8LAL2; P33078: IAA5; NbExp=5; IntAct=EBI-3947418, EBI-3946487;
CC Q8LAL2; Q38824: IAA6; NbExp=8; IntAct=EBI-3947418, EBI-1554124;
CC Q8LAL2; Q38825: IAA7; NbExp=6; IntAct=EBI-3947418, EBI-602959;
CC Q8LAL2; Q38826: IAA8; NbExp=5; IntAct=EBI-3947418, EBI-632200;
CC Q8LAL2; Q38827: IAA9; NbExp=4; IntAct=EBI-3947418, EBI-632216;
CC Q8LAL2; Q946J8: LHP1; NbExp=3; IntAct=EBI-3947418, EBI-2309089;
CC Q8LAL2; Q9LTC4: MYB15; NbExp=3; IntAct=EBI-3947418, EBI-21497119;
CC Q8LAL2; O23160: MYB73; NbExp=3; IntAct=EBI-3947418, EBI-25506855;
CC Q8LAL2; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-3947418, EBI-15193025;
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}.
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DR EMBL; AF088281; AAC99772.1; -; mRNA.
DR EMBL; AP000373; BAB01149.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75827.1; -; Genomic_DNA.
DR EMBL; AF332394; AAG48758.2; -; mRNA.
DR EMBL; AF332401; AAG48765.1; -; mRNA.
DR EMBL; AF386948; AAK62393.1; -; mRNA.
DR EMBL; AY072502; AAL66917.1; -; mRNA.
DR EMBL; AY087745; AAM65282.1; -; mRNA.
DR RefSeq; NP_188271.1; NM_112521.4.
DR AlphaFoldDB; Q8LAL2; -.
DR SMR; Q8LAL2; -.
DR BioGRID; 6232; 61.
DR ELM; Q8LAL2; -.
DR IntAct; Q8LAL2; 52.
DR STRING; 3702.AT3G16500.1; -.
DR PaxDb; Q8LAL2; -.
DR PRIDE; Q8LAL2; -.
DR ProteomicsDB; 232159; -.
DR EnsemblPlants; AT3G16500.1; AT3G16500.1; AT3G16500.
DR GeneID; 820898; -.
DR Gramene; AT3G16500.1; AT3G16500.1; AT3G16500.
DR KEGG; ath:AT3G16500; -.
DR Araport; AT3G16500; -.
DR TAIR; locus:2088324; AT3G16500.
DR eggNOG; ENOG502QPYY; Eukaryota.
DR HOGENOM; CLU_049393_2_1_1; -.
DR InParanoid; Q8LAL2; -.
DR OMA; TASWAKN; -.
DR OrthoDB; 1210341at2759; -.
DR PhylomeDB; Q8LAL2; -.
DR PRO; PR:Q8LAL2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LAL2; baseline and differential.
DR Genevisible; Q8LAL2; 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: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; 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..269
FT /note="Auxin-responsive protein IAA26"
FT /id="PRO_0000112852"
FT DOMAIN 151..250
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 25..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..42
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 76..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 43..46
FT /note="GPPG -> HR (in Ref. 1; AAC99772)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> H (in Ref. 5; AAM65282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30124 MW; 70CA1CECBD77CD0E CRC64;
MEGCPRNREI GPKLLDLIPQ GRKWYQEDKN NTDQEKKLEL RLGPPGGDEE DHSAIKKKNT
EIRNIKKETE DKSFHCFNGN HFSPSNKTTS VPHISQKRTA PGPVVGWPPV RSFRKNLAST
SSSKLGNESS HGGQINKSDD GEKQVETKKE GMFVKINMDG VPIGRKVDLN AYNSYEQLSF
VVDKLFRGLL AAQRDISDGQ GEEKPIIGLL DGKGEFTLTY EDNEGDKMLV GDVPWQMFVS
SVKRLRVIKS SEISSALTFG CSKQEKMMH
