IAA13_ARATH
ID IAA13_ARATH Reviewed; 247 AA.
AC Q38831; Q84TE5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Auxin-responsive protein IAA13;
DE AltName: Full=Indoleacetic acid-induced protein 13;
GN Name=IAA13; OrderedLocusNames=At2g33310; ORFNames=F4P9.8;
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] (ISOFORM 2), 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORMS 1 AND 2).
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 210-247.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
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.
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 TPL. {ECO:0000250, ECO:0000269|PubMed:18258861}.
CC -!- INTERACTION:
CC Q38831; Q9C5W9: ARF18; NbExp=3; IntAct=EBI-1554143, EBI-3946783;
CC Q38831; Q8RYC8: ARF19; NbExp=3; IntAct=EBI-1554143, EBI-529887;
CC Q38831; P93024: ARF5; NbExp=3; IntAct=EBI-1554143, EBI-629519;
CC Q38831; P49677: IAA1; NbExp=8; IntAct=EBI-1554143, EBI-630505;
CC Q38831; Q38828: IAA10; NbExp=10; IntAct=EBI-1554143, EBI-3946434;
CC Q38831; Q38829: IAA11; NbExp=6; IntAct=EBI-1554143, EBI-2367923;
CC Q38831; Q38830: IAA12; NbExp=8; IntAct=EBI-1554143, EBI-617608;
CC Q38831; Q38831: IAA13; NbExp=4; IntAct=EBI-1554143, EBI-1554143;
CC Q38831; Q38832: IAA14; NbExp=4; IntAct=EBI-1554143, EBI-2295562;
CC Q38831; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-1554143, EBI-25524519;
CC Q38831; O24407: IAA16; NbExp=9; IntAct=EBI-1554143, EBI-632231;
CC Q38831; P93830: IAA17; NbExp=9; IntAct=EBI-1554143, EBI-632243;
CC Q38831; O24408: IAA18; NbExp=3; IntAct=EBI-1554143, EBI-2295525;
CC Q38831; O24409: IAA19; NbExp=11; IntAct=EBI-1554143, EBI-632257;
CC Q38831; P49678: IAA2; NbExp=8; IntAct=EBI-1554143, EBI-632343;
CC Q38831; O24410: IAA20; NbExp=5; IntAct=EBI-1554143, EBI-632272;
CC Q38831; Q8LAL2: IAA26; NbExp=8; IntAct=EBI-1554143, EBI-3947418;
CC Q38831; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-1554143, EBI-3946677;
CC Q38831; Q9XFM0: IAA28; NbExp=8; IntAct=EBI-1554143, EBI-3133404;
CC Q38831; Q38822: IAA3; NbExp=9; IntAct=EBI-1554143, EBI-307174;
CC Q38831; Q8H174: IAA31; NbExp=9; IntAct=EBI-1554143, EBI-3946408;
CC Q38831; Q8RYC6: IAA32; NbExp=5; IntAct=EBI-1554143, EBI-3946448;
CC Q38831; Q9FKM7: IAA33; NbExp=6; IntAct=EBI-1554143, EBI-3946739;
CC Q38831; Q9C5X0: IAA34; NbExp=6; IntAct=EBI-1554143, EBI-3946459;
CC Q38831; P33077: IAA4; NbExp=9; IntAct=EBI-1554143, EBI-632187;
CC Q38831; P33078: IAA5; NbExp=6; IntAct=EBI-1554143, EBI-3946487;
CC Q38831; Q38824: IAA6; NbExp=8; IntAct=EBI-1554143, EBI-1554124;
CC Q38831; Q38825: IAA7; NbExp=7; IntAct=EBI-1554143, EBI-602959;
CC Q38831; Q38826: IAA8; NbExp=6; IntAct=EBI-1554143, EBI-632200;
CC Q38831; Q38827: IAA9; NbExp=4; IntAct=EBI-1554143, EBI-632216;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38831-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38831-2; Sequence=VSP_008997;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in stems.
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 -!- MISCELLANEOUS: [Isoform 1]: May be due to a competing acceptor splice
CC site.
CC -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
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DR EMBL; U18415; AAC49054.1; -; mRNA.
DR EMBL; AC002332; AAB80649.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08812.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08813.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08814.1; -; Genomic_DNA.
DR EMBL; AF332399; AAG48763.1; -; mRNA.
DR EMBL; BT005874; AAO64809.1; -; mRNA.
DR EMBL; AY085194; AAM61745.1; -; mRNA.
DR EMBL; Z26543; CAA81314.1; -; mRNA.
DR PIR; S58499; S58499.
DR RefSeq; NP_001118434.1; NM_001124962.1. [Q38831-2]
DR RefSeq; NP_180889.1; NM_128891.4. [Q38831-2]
DR RefSeq; NP_850205.1; NM_179874.2. [Q38831-1]
DR AlphaFoldDB; Q38831; -.
DR SMR; Q38831; -.
DR BioGRID; 3241; 44.
DR ELM; Q38831; -.
DR IntAct; Q38831; 38.
DR STRING; 3702.AT2G33310.2; -.
DR iPTMnet; Q38831; -.
DR PaxDb; Q38831; -.
DR PRIDE; Q38831; -.
DR ProteomicsDB; 232114; -. [Q38831-1]
DR EnsemblPlants; AT2G33310.1; AT2G33310.1; AT2G33310. [Q38831-2]
DR EnsemblPlants; AT2G33310.2; AT2G33310.2; AT2G33310. [Q38831-1]
DR EnsemblPlants; AT2G33310.3; AT2G33310.3; AT2G33310. [Q38831-2]
DR GeneID; 817894; -.
DR Gramene; AT2G33310.1; AT2G33310.1; AT2G33310. [Q38831-2]
DR Gramene; AT2G33310.2; AT2G33310.2; AT2G33310. [Q38831-1]
DR Gramene; AT2G33310.3; AT2G33310.3; AT2G33310. [Q38831-2]
DR KEGG; ath:AT2G33310; -.
DR Araport; AT2G33310; -.
DR TAIR; locus:2051154; AT2G33310.
DR eggNOG; ENOG502R8MA; Eukaryota.
DR HOGENOM; CLU_049393_3_0_1; -.
DR InParanoid; Q38831; -.
DR OMA; KASAWGE; -.
DR PhylomeDB; Q38831; -.
DR PRO; PR:Q38831; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38831; baseline and differential.
DR Genevisible; Q38831; 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 Alternative splicing; Auxin signaling pathway; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..247
FT /note="Auxin-responsive protein IAA13"
FT /id="PRO_0000112844"
FT DOMAIN 129..225
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..18
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:7658471, ECO:0000303|Ref.5"
FT /id="VSP_008997"
SQ SEQUENCE 247 AA; 26729 MW; 5B57E065DA786CD4 CRC64;
MITELEMGKG ESELELGLGL SLGGGTAAKI GKSGGGGAWG ERGRLLTAKD FPSVGSKRAA
DSASHAGSSP PRSSSQVVGW PPIGSHRMNS LVNNQATKSA REEEEAGKKK VKDDEPKDVT
KKVNGKVQVG FIKVNMDGVA IGRKVDLNAH SSYENLAQTL EDMFFRTNPG TVGLTSQFTK
PLRLLDGSSE FVLTYEDKEG DWMLVGDVPW RMFINSVKRL RVMKTSEANG LAARNQEPNE
RQRKQPV
