IAA27_ARATH
ID IAA27_ARATH Reviewed; 305 AA.
AC Q9ZSY8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Auxin-responsive protein IAA27;
DE AltName: Full=Auxin-induced protein 27;
DE AltName: Full=Indoleacetic acid-induced protein 27;
DE AltName: Full=Phytochrome-associated protein 2;
GN Name=IAA27; Synonyms=PAP2; OrderedLocusNames=At4g29080;
GN ORFNames=F19B15.110;
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].
RA Yi H., Lee J., 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 [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 IAA27.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [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 Q9ZSY8; Q9C5W9: ARF18; NbExp=4; IntAct=EBI-3946677, EBI-3946783;
CC Q9ZSY8; Q9SJM4: GPL3; NbExp=3; IntAct=EBI-3946677, EBI-15199331;
CC Q9ZSY8; P49677: IAA1; NbExp=10; IntAct=EBI-3946677, EBI-630505;
CC Q9ZSY8; Q38828: IAA10; NbExp=9; IntAct=EBI-3946677, EBI-3946434;
CC Q9ZSY8; Q38829: IAA11; NbExp=7; IntAct=EBI-3946677, EBI-2367923;
CC Q9ZSY8; Q38830: IAA12; NbExp=3; IntAct=EBI-3946677, EBI-617608;
CC Q9ZSY8; Q38831: IAA13; NbExp=9; IntAct=EBI-3946677, EBI-1554143;
CC Q9ZSY8; Q38832: IAA14; NbExp=3; IntAct=EBI-3946677, EBI-2295562;
CC Q9ZSY8; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-3946677, EBI-25524519;
CC Q9ZSY8; O24407: IAA16; NbExp=9; IntAct=EBI-3946677, EBI-632231;
CC Q9ZSY8; P93830: IAA17; NbExp=9; IntAct=EBI-3946677, EBI-632243;
CC Q9ZSY8; O24408: IAA18; NbExp=4; IntAct=EBI-3946677, EBI-2295525;
CC Q9ZSY8; O24409: IAA19; NbExp=10; IntAct=EBI-3946677, EBI-632257;
CC Q9ZSY8; P49678: IAA2; NbExp=9; IntAct=EBI-3946677, EBI-632343;
CC Q9ZSY8; O24410: IAA20; NbExp=3; IntAct=EBI-3946677, EBI-632272;
CC Q9ZSY8; Q8LAL2: IAA26; NbExp=8; IntAct=EBI-3946677, EBI-3947418;
CC Q9ZSY8; Q9ZSY8: IAA27; NbExp=4; IntAct=EBI-3946677, EBI-3946677;
CC Q9ZSY8; Q9XFM0: IAA28; NbExp=8; IntAct=EBI-3946677, EBI-3133404;
CC Q9ZSY8; Q38822: IAA3; NbExp=9; IntAct=EBI-3946677, EBI-307174;
CC Q9ZSY8; Q8H174: IAA31; NbExp=9; IntAct=EBI-3946677, EBI-3946408;
CC Q9ZSY8; Q8RYC6: IAA32; NbExp=3; IntAct=EBI-3946677, EBI-3946448;
CC Q9ZSY8; Q9FKM7: IAA33; NbExp=6; IntAct=EBI-3946677, EBI-3946739;
CC Q9ZSY8; Q9C5X0: IAA34; NbExp=8; IntAct=EBI-3946677, EBI-3946459;
CC Q9ZSY8; P33077: IAA4; NbExp=9; IntAct=EBI-3946677, EBI-632187;
CC Q9ZSY8; P33078: IAA5; NbExp=6; IntAct=EBI-3946677, EBI-3946487;
CC Q9ZSY8; Q38824: IAA6; NbExp=9; IntAct=EBI-3946677, EBI-1554124;
CC Q9ZSY8; Q38826: IAA8; NbExp=6; IntAct=EBI-3946677, EBI-632200;
CC Q9ZSY8; Q38827: IAA9; NbExp=4; IntAct=EBI-3946677, EBI-632216;
CC Q9ZSY8; Q9LID0: LDL2; NbExp=3; IntAct=EBI-3946677, EBI-15195631;
CC Q9ZSY8; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-3946677, EBI-4426144;
CC Q9ZSY8; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-3946677, EBI-25522447;
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; AF087936; AAC99773.1; -; mRNA.
DR EMBL; AJ458326; CAD30208.1; -; mRNA.
DR EMBL; AL078470; CAB43922.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79666.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85584.1; -; Genomic_DNA.
DR EMBL; AF332402; AAG48766.1; -; mRNA.
DR EMBL; AY053404; AAK96634.1; -; mRNA.
DR EMBL; AY133516; AAM91346.1; -; mRNA.
DR PIR; T08963; T08963.
DR RefSeq; NP_194637.1; NM_119052.4.
DR PDB; 5NQV; X-ray; 1.95 A; E/F/G/H=43-53.
DR PDBsum; 5NQV; -.
DR AlphaFoldDB; Q9ZSY8; -.
DR SMR; Q9ZSY8; -.
DR BioGRID; 14316; 51.
DR ELM; Q9ZSY8; -.
DR IntAct; Q9ZSY8; 49.
DR STRING; 3702.AT4G29080.1; -.
DR PaxDb; Q9ZSY8; -.
DR PRIDE; Q9ZSY8; -.
DR ProteomicsDB; 232191; -.
DR EnsemblPlants; AT4G29080.1; AT4G29080.1; AT4G29080.
DR GeneID; 829029; -.
DR Gramene; AT4G29080.1; AT4G29080.1; AT4G29080.
DR KEGG; ath:AT4G29080; -.
DR Araport; AT4G29080; -.
DR TAIR; locus:2119976; AT4G29080.
DR eggNOG; ENOG502QTW8; Eukaryota.
DR HOGENOM; CLU_049393_1_2_1; -.
DR InParanoid; Q9ZSY8; -.
DR OMA; PCLYVKV; -.
DR OrthoDB; 1277419at2759; -.
DR PhylomeDB; Q9ZSY8; -.
DR PRO; PR:Q9ZSY8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSY8; baseline and differential.
DR Genevisible; Q9ZSY8; 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..305
FT /note="Auxin-responsive protein IAA27"
FT /id="PRO_0000112853"
FT DOMAIN 185..287
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 96..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..49
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 96..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 33196 MW; 18F83E199FFC0A84 CRC64;
MSVSVAAEHD YIGLSEFPTM EATTMSDKTK TRDNNNGLNF KATELRLGLP GSESPERVDS
RFLALNKSSC PVSGAKRVFS DAINDSNKWV FSPGSTTATG DVGSGSGPRT SVVKDGKSTT
FTKPAVPVKE KKSSATAPAS KAQVVGWPPI RSFRKNSMAS SQSQKPGNNS ETEEAEAKSG
PEQPCLYVKV SMEGAPYLRK IDLKTYKSYL ELSSALEKMF SCFTIGQFGS HGGCGRDGLN
ESRLTDLLRG SEYVVTYEDK DSDWMLVGDV PWEMFICSCK KLRIMKSSEA IGLAPRVMEK
CRSRN
