IAA10_ARATH
ID IAA10_ARATH Reviewed; 261 AA.
AC Q38828;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Auxin-responsive protein IAA10;
DE AltName: Full=Indoleacetic acid-induced protein 10;
GN Name=IAA10; OrderedLocusNames=At1g04100; ORFNames=F20D22.13;
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], 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 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 Q38828; Q9C5W9: ARF18; NbExp=8; IntAct=EBI-3946434, EBI-3946783;
CC Q38828; Q8RYC8: ARF19; NbExp=7; IntAct=EBI-3946434, EBI-529887;
CC Q38828; Q94JM3: ARF2; NbExp=6; IntAct=EBI-3946434, EBI-1799262;
CC Q38828; Q9XED8: ARF9; NbExp=3; IntAct=EBI-3946434, EBI-3946762;
CC Q38828; Q9LST3: At5g60142; NbExp=3; IntAct=EBI-3946434, EBI-15192745;
CC Q38828; Q9FPE8: HHO3; NbExp=3; IntAct=EBI-3946434, EBI-2298866;
CC Q38828; P49677: IAA1; NbExp=10; IntAct=EBI-3946434, EBI-630505;
CC Q38828; Q38828: IAA10; NbExp=5; IntAct=EBI-3946434, EBI-3946434;
CC Q38828; Q38829: IAA11; NbExp=6; IntAct=EBI-3946434, EBI-2367923;
CC Q38828; Q38830: IAA12; NbExp=5; IntAct=EBI-3946434, EBI-617608;
CC Q38828; Q38831: IAA13; NbExp=10; IntAct=EBI-3946434, EBI-1554143;
CC Q38828; Q38832: IAA14; NbExp=3; IntAct=EBI-3946434, EBI-2295562;
CC Q38828; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-3946434, EBI-25524519;
CC Q38828; O24407: IAA16; NbExp=11; IntAct=EBI-3946434, EBI-632231;
CC Q38828; P93830: IAA17; NbExp=9; IntAct=EBI-3946434, EBI-632243;
CC Q38828; O24408: IAA18; NbExp=5; IntAct=EBI-3946434, EBI-2295525;
CC Q38828; O24409: IAA19; NbExp=9; IntAct=EBI-3946434, EBI-632257;
CC Q38828; P49678: IAA2; NbExp=12; IntAct=EBI-3946434, EBI-632343;
CC Q38828; O24410: IAA20; NbExp=5; IntAct=EBI-3946434, EBI-632272;
CC Q38828; Q8LAL2: IAA26; NbExp=10; IntAct=EBI-3946434, EBI-3947418;
CC Q38828; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-3946434, EBI-3946677;
CC Q38828; Q9XFM0: IAA28; NbExp=10; IntAct=EBI-3946434, EBI-3133404;
CC Q38828; Q38822: IAA3; NbExp=10; IntAct=EBI-3946434, EBI-307174;
CC Q38828; Q8H174: IAA31; NbExp=8; IntAct=EBI-3946434, EBI-3946408;
CC Q38828; Q8RYC6: IAA32; NbExp=5; IntAct=EBI-3946434, EBI-3946448;
CC Q38828; Q9FKM7: IAA33; NbExp=6; IntAct=EBI-3946434, EBI-3946739;
CC Q38828; Q9C5X0: IAA34; NbExp=11; IntAct=EBI-3946434, EBI-3946459;
CC Q38828; P33077: IAA4; NbExp=10; IntAct=EBI-3946434, EBI-632187;
CC Q38828; P33078: IAA5; NbExp=6; IntAct=EBI-3946434, EBI-3946487;
CC Q38828; Q38824: IAA6; NbExp=9; IntAct=EBI-3946434, EBI-1554124;
CC Q38828; Q38825: IAA7; NbExp=4; IntAct=EBI-3946434, EBI-602959;
CC Q38828; Q38826: IAA8; NbExp=7; IntAct=EBI-3946434, EBI-632200;
CC Q38828; Q38827: IAA9; NbExp=4; IntAct=EBI-3946434, EBI-632216;
CC Q38828; Q8LA53: MBD2; NbExp=4; IntAct=EBI-3946434, EBI-4425826;
CC Q38828; O23160: MYB73; NbExp=3; IntAct=EBI-3946434, EBI-25506855;
CC Q38828; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-3946434, EBI-4426144;
CC Q38828; Q9FTA2: TCP21; NbExp=3; IntAct=EBI-3946434, EBI-4426168;
CC Q38828; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-3946434, EBI-25522447;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in vegetative organs.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18412; AAC49051.1; -; mRNA.
DR EMBL; AC002411; AAC16750.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27656.1; -; Genomic_DNA.
DR EMBL; AF332396; AAG48760.1; -; mRNA.
DR PIR; S58496; S58496.
DR RefSeq; NP_171906.1; NM_100291.3.
DR PDB; 5C7E; X-ray; 3.10 A; G/H/I/J/K/L=41-51.
DR PDBsum; 5C7E; -.
DR AlphaFoldDB; Q38828; -.
DR SMR; Q38828; -.
DR BioGRID; 24525; 59.
DR ELM; Q38828; -.
DR IntAct; Q38828; 56.
DR STRING; 3702.AT1G04100.1; -.
DR PaxDb; Q38828; -.
DR PRIDE; Q38828; -.
DR EnsemblPlants; AT1G04100.1; AT1G04100.1; AT1G04100.
DR GeneID; 839290; -.
DR Gramene; AT1G04100.1; AT1G04100.1; AT1G04100.
DR KEGG; ath:AT1G04100; -.
DR Araport; AT1G04100; -.
DR TAIR; locus:2020255; AT1G04100.
DR eggNOG; ENOG502R053; Eukaryota.
DR HOGENOM; CLU_049393_3_0_1; -.
DR InParanoid; Q38828; -.
DR OMA; FRDVCSS; -.
DR OrthoDB; 1104776at2759; -.
DR PhylomeDB; Q38828; -.
DR PRO; PR:Q38828; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38828; baseline and differential.
DR Genevisible; Q38828; 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; 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 3D-structure; Auxin signaling pathway; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..261
FT /note="Auxin-responsive protein IAA10"
FT /id="PRO_0000112841"
FT DOMAIN 151..253
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..49
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 62..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 27878 MW; DE99194344815A14 CRC64;
MNGLQEVCSS SGSVMIGLPA EEDENAAHSS EDSSCPDESV SETELDLALG LSIGRRKVRS
SLSSSSSSLT RESGTKRSAD SSPAAASNAT RQVAVGWPPL RTYRINSLVN QAKSLATEGG
LSSGIQKETT KSVVVAAKND DACFIKSSRT SMLVKVTMDG VIIGRKVDLN ALDSYAALEK
TLDLMFFQIP SPVTRSNTQG YKTIKETCTS KLLDGSSEYI ITYQDKDGDW MLVGDVPWQM
FLGSVTRLRI MKTSIGAGVG K
