IAA12_ARATH
ID IAA12_ARATH Reviewed; 239 AA.
AC Q38830; Q8LA42;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Auxin-responsive protein IAA12;
DE AltName: Full=Indoleacetic acid-induced protein 12;
DE AltName: Full=Protein BODENLOS;
GN Name=IAA12; Synonyms=BDL; OrderedLocusNames=At1g04550; ORFNames=T1G11.20;
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 BDL, AND INTERACTION WITH ARF5.
RX PubMed=12101120; DOI=10.1101/gad.229402;
RA Hamann T., Benkova E., Baeurle I., Kientz M., Juergens G.;
RT "The Arabidopsis BODENLOS gene encodes an auxin response protein inhibiting
RT MONOPTEROS-mediated embryo patterning.";
RL Genes Dev. 16:1610-1615(2002).
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, AND MUTAGENESIS OF LEU-20; LEU-22 AND LEU-24.
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. Interacts with the auxin response
CC factor ARF5. Interacts (via domain I) with TPL (via the LisH domain).
CC {ECO:0000269|PubMed:12101120, ECO:0000269|PubMed:18258861}.
CC -!- INTERACTION:
CC Q38830; Q9C5W9: ARF18; NbExp=4; IntAct=EBI-617608, EBI-3946783;
CC Q38830; P93024: ARF5; NbExp=4; IntAct=EBI-617608, EBI-629519;
CC Q38830; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-617608, EBI-1100737;
CC Q38830; Q67XT7: At2g36145; NbExp=3; IntAct=EBI-617608, EBI-25521975;
CC Q38830; P49677: IAA1; NbExp=5; IntAct=EBI-617608, EBI-630505;
CC Q38830; Q38828: IAA10; NbExp=5; IntAct=EBI-617608, EBI-3946434;
CC Q38830; Q38830: IAA12; NbExp=5; IntAct=EBI-617608, EBI-617608;
CC Q38830; Q38831: IAA13; NbExp=8; IntAct=EBI-617608, EBI-1554143;
CC Q38830; Q38832: IAA14; NbExp=4; IntAct=EBI-617608, EBI-2295562;
CC Q38830; A0A2H1ZEF6: IAA15; NbExp=3; IntAct=EBI-617608, EBI-25524519;
CC Q38830; O24407: IAA16; NbExp=8; IntAct=EBI-617608, EBI-632231;
CC Q38830; P93830: IAA17; NbExp=9; IntAct=EBI-617608, EBI-632243;
CC Q38830; O24408: IAA18; NbExp=5; IntAct=EBI-617608, EBI-2295525;
CC Q38830; O24409: IAA19; NbExp=8; IntAct=EBI-617608, EBI-632257;
CC Q38830; P49678: IAA2; NbExp=5; IntAct=EBI-617608, EBI-632343;
CC Q38830; O24410: IAA20; NbExp=4; IntAct=EBI-617608, EBI-632272;
CC Q38830; Q8LAL2: IAA26; NbExp=3; IntAct=EBI-617608, EBI-3947418;
CC Q38830; Q9ZSY8: IAA27; NbExp=3; IntAct=EBI-617608, EBI-3946677;
CC Q38830; Q9XFM0: IAA28; NbExp=6; IntAct=EBI-617608, EBI-3133404;
CC Q38830; Q38822: IAA3; NbExp=8; IntAct=EBI-617608, EBI-307174;
CC Q38830; Q8H174: IAA31; NbExp=8; IntAct=EBI-617608, EBI-3946408;
CC Q38830; P33077: IAA4; NbExp=6; IntAct=EBI-617608, EBI-632187;
CC Q38830; Q38824: IAA6; NbExp=5; IntAct=EBI-617608, EBI-1554124;
CC Q38830; Q38825: IAA7; NbExp=4; IntAct=EBI-617608, EBI-602959;
CC Q38830; Q38826: IAA8; NbExp=7; IntAct=EBI-617608, EBI-632200;
CC Q38830; Q9FWY7: IMPA6; NbExp=3; IntAct=EBI-617608, EBI-4431755;
CC Q38830; O22179: MYB70; NbExp=3; IntAct=EBI-617608, EBI-1238013;
CC Q38830; Q9FJJ3: SRO5; NbExp=3; IntAct=EBI-617608, EBI-4434999;
CC Q38830; Q9FEE2: TON2; NbExp=3; IntAct=EBI-617608, EBI-4452426;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q38830-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in stems, leaves and
CC flowers. {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; U18414; AAC49053.1; -; mRNA.
DR EMBL; AC002376; AAB80631.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27713.1; -; Genomic_DNA.
DR EMBL; AF332398; AAG48762.1; -; mRNA.
DR EMBL; AY065240; AAL38716.1; -; mRNA.
DR EMBL; AY096535; AAM20185.1; -; mRNA.
DR EMBL; AY088042; AAM65588.1; -; mRNA.
DR PIR; S58498; S58498.
DR RefSeq; NP_171949.1; NM_100334.4. [Q38830-1]
DR AlphaFoldDB; Q38830; -.
DR SMR; Q38830; -.
DR BioGRID; 24730; 47.
DR ELM; Q38830; -.
DR IntAct; Q38830; 48.
DR STRING; 3702.AT1G04550.2; -.
DR iPTMnet; Q38830; -.
DR PaxDb; Q38830; -.
DR PRIDE; Q38830; -.
DR DNASU; 839495; -.
DR EnsemblPlants; AT1G04550.2; AT1G04550.2; AT1G04550. [Q38830-1]
DR GeneID; 839495; -.
DR Gramene; AT1G04550.2; AT1G04550.2; AT1G04550. [Q38830-1]
DR KEGG; ath:AT1G04550; -.
DR Araport; AT1G04550; -.
DR TAIR; locus:2197838; AT1G04550.
DR eggNOG; ENOG502R8MA; Eukaryota.
DR HOGENOM; CLU_049393_3_0_1; -.
DR InParanoid; Q38830; -.
DR OMA; SVPHDSG; -.
DR OrthoDB; 1104776at2759; -.
DR PhylomeDB; Q38830; -.
DR PRO; PR:Q38830; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38830; baseline and differential.
DR Genevisible; Q38830; 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:0009880; P:embryonic pattern specification; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; 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 Alternative splicing; Auxin signaling pathway; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..239
FT /note="Auxin-responsive protein IAA12"
FT /id="PRO_0000112843"
FT DOMAIN 124..217
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 44..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 20..24
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 50..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 20
FT /note="L->A: Decreased interaction with TPL; when
FT associated with A-22 and A-24."
FT /evidence="ECO:0000269|PubMed:18258861"
FT MUTAGEN 22
FT /note="L->A: Decreased interaction with TPL; when
FT associated with A-20 and A-24."
FT /evidence="ECO:0000269|PubMed:18258861"
FT MUTAGEN 24
FT /note="L->A: Decreased interaction with TPL; when
FT associated with A-20 and A-22."
FT /evidence="ECO:0000269|PubMed:18258861"
FT MUTAGEN 74
FT /note="P->S: In bdl; gain of function. Affects auxin-
FT related developmental processes."
FT CONFLICT 119
FT /note="P -> A (in Ref. 5; AAM65588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26286 MW; BBAADA3E98B222CA CRC64;
MRGVSELEVG KSNLPAESEL ELGLGLSLGG GAWKERGRIL TAKDFPSVGS KRSAESSSHQ
GASPPRSSQV VGWPPIGLHR MNSLVNNQAM KAARAEEGDG EKKVVKNDEL KDVSMKVNPK
VQGLGFVKVN MDGVGIGRKV DMRAHSSYEN LAQTLEEMFF GMTGTTCREK VKPLRLLDGS
SDFVLTYEDK EGDWMLVGDV PWRMFINSVK RLRIMGTSEA SGLAPRRQEQ KDRQRNNPV
