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IAA32_ARATH
ID   IAA32_ARATH             Reviewed;         191 AA.
AC   Q8RYC6; F4IM94; Q2VW97; Q9ZU47;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Auxin-responsive protein IAA32 {ECO:0000303|PubMed:12036262};
DE   AltName: Full=Indoleacetic acid-induced protein 32 {ECO:0000303|PubMed:12036262};
GN   Name=IAA32 {ECO:0000303|PubMed:12036262};
GN   OrderedLocusNames=At2g01200 {ECO:0000312|Araport:AT2G01200};
GN   ORFNames=F10A8.8 {ECO:0000312|EMBL:AAD14520.1};
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], AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=16284307; DOI=10.1105/tpc.105.036723;
RA   Overvoorde P.J., Okushima Y., Alonso J.M., Chan A., Chang C., Ecker J.R.,
RA   Hughes B., Liu A., Onodera C., Quach H., Smith A., Yu G., Theologis A.;
RT   "Functional genomic analysis of the AUXIN/INDOLE-3-ACETIC ACID gene family
RT   members in Arabidopsis thaliana.";
RL   Plant Cell 17:3282-3300(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Bor-4;
RX   PubMed=20622145; DOI=10.1105/tpc.110.073957;
RA   Delker C., Poschl Y., Raschke A., Ullrich K., Ettingshausen S.,
RA   Hauptmann V., Grosse I., Quint M.;
RT   "Natural variation of transcriptional auxin response networks in
RT   Arabidopsis thaliana.";
RL   Plant Cell 22:2184-2200(2010).
RN   [3]
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   [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-170.
RC   STRAIN=cv. Columbia;
RA   Sessa G., Carabelli M., Ciarbelli A.R., Ruzza V., Steindler C., Ruberti I.;
RT   "Nucleotide sequence of the Arabidopsis IAA31.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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).
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|UniProtKB:P49677}.
CC   -!- INTERACTION:
CC       Q8RYC6; Q8RYC8: ARF19; NbExp=4; IntAct=EBI-3946448, EBI-529887;
CC       Q8RYC6; Q94JM3: ARF2; NbExp=6; IntAct=EBI-3946448, EBI-1799262;
CC       Q8RYC6; P49677: IAA1; NbExp=3; IntAct=EBI-3946448, EBI-630505;
CC       Q8RYC6; Q38828: IAA10; NbExp=5; IntAct=EBI-3946448, EBI-3946434;
CC       Q8RYC6; Q38831: IAA13; NbExp=5; IntAct=EBI-3946448, EBI-1554143;
CC       Q8RYC6; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-3946448, EBI-25524519;
CC       Q8RYC6; P93830: IAA17; NbExp=7; IntAct=EBI-3946448, EBI-632243;
CC       Q8RYC6; O24409: IAA19; NbExp=3; IntAct=EBI-3946448, EBI-632257;
CC       Q8RYC6; P49678: IAA2; NbExp=3; IntAct=EBI-3946448, EBI-632343;
CC       Q8RYC6; O24410: IAA20; NbExp=4; IntAct=EBI-3946448, EBI-632272;
CC       Q8RYC6; Q8LAL2: IAA26; NbExp=5; IntAct=EBI-3946448, EBI-3947418;
CC       Q8RYC6; Q9ZSY8: IAA27; NbExp=3; IntAct=EBI-3946448, EBI-3946677;
CC       Q8RYC6; Q9XFM0: IAA28; NbExp=5; IntAct=EBI-3946448, EBI-3133404;
CC       Q8RYC6; Q38822: IAA3; NbExp=5; IntAct=EBI-3946448, EBI-307174;
CC       Q8RYC6; Q8H174: IAA31; NbExp=3; IntAct=EBI-3946448, EBI-3946408;
CC       Q8RYC6; Q9FKM7: IAA33; NbExp=3; IntAct=EBI-3946448, EBI-3946739;
CC       Q8RYC6; P33077: IAA4; NbExp=5; IntAct=EBI-3946448, EBI-632187;
CC       Q8RYC6; Q38824: IAA6; NbExp=3; IntAct=EBI-3946448, EBI-1554124;
CC       Q8RYC6; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-3946448, EBI-4426144;
CC       Q8RYC6; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-3946448, EBI-25522447;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=Q8RYC6-1; Sequence=Displayed;
CC   -!- INDUCTION: By auxin. {ECO:0000250|UniProtKB:P49677}.
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   -!- CAUTION: Was originally (Ref.6) erroneously named IAA31. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD14520.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY669803; AAT67087.1; -; mRNA.
DR   EMBL; HM487929; ADL70814.1; -; Genomic_DNA.
DR   EMBL; AC006200; AAD14520.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC05414.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05415.1; -; Genomic_DNA.
DR   EMBL; DQ446449; ABE65790.1; -; mRNA.
DR   EMBL; AJ458329; CAD30211.1; -; mRNA.
DR   PIR; G84421; G84421.
DR   RefSeq; NP_001318172.1; NM_001335044.1. [Q8RYC6-1]
DR   RefSeq; NP_973390.1; NM_201661.2. [Q8RYC6-1]
DR   AlphaFoldDB; Q8RYC6; -.
DR   SMR; Q8RYC6; -.
DR   BioGRID; 52; 43.
DR   IntAct; Q8RYC6; 41.
DR   STRING; 3702.AT2G01200.2; -.
DR   PaxDb; Q8RYC6; -.
DR   PRIDE; Q8RYC6; -.
DR   EnsemblPlants; AT2G01200.1; AT2G01200.1; AT2G01200. [Q8RYC6-1]
DR   EnsemblPlants; AT2G01200.2; AT2G01200.2; AT2G01200. [Q8RYC6-1]
DR   GeneID; 814648; -.
DR   Gramene; AT2G01200.1; AT2G01200.1; AT2G01200. [Q8RYC6-1]
DR   Gramene; AT2G01200.2; AT2G01200.2; AT2G01200. [Q8RYC6-1]
DR   KEGG; ath:AT2G01200; -.
DR   Araport; AT2G01200; -.
DR   TAIR; locus:2038701; AT2G01200.
DR   eggNOG; ENOG502RZE6; Eukaryota.
DR   HOGENOM; CLU_117411_0_0_1; -.
DR   InParanoid; Q8RYC6; -.
DR   OMA; QHETYLP; -.
DR   OrthoDB; 1314275at2759; -.
DR   PhylomeDB; Q8RYC6; -.
DR   PRO; PR:Q8RYC6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8RYC6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
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..191
FT                   /note="Auxin-responsive protein IAA32"
FT                   /id="PRO_0000112858"
FT   DOMAIN          98..184
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   MOTIF           32..36
FT                   /note="EAR-like (transcriptional repression)"
SQ   SEQUENCE   191 AA;  21662 MW;  343D84427290F5F1 CRC64;
     MDPNTPADFF KGSSKFHTYY SQTKKGGGVI DLGLSLRTIQ HETYLPPARM IGLDGYGELI
     DWSQPSYNSI TQLKSEDTGH QRLAQGYYNN EGESRGKYAY VKVNLDGLVV GRKVCLVDQG
     AYATLALQLN DMFGMQTVSG LRLFQTESEF SLVYRDREGI WRNVGDVPWK EFVESVDRMR
     IARRNDALLP F
 
 
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