ID   IAA4_PEA                Reviewed;         189 AA.
AC   P49679;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Auxin-induced protein IAA4;
GN   Name=IAA4/5;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Alaska;
RX   PubMed=8411182; DOI=10.1006/jmbi.1993.1555;
RA   Oeller P.W., Keller J.A., Parks J.E., Silbert J.E., Theologis A.;
RT   "Structural characterization of the early indoleacetic acid-inducible
RT   genes, PS-IAA4/5 and PS-IAA6, of pea (Pisum sativum L.).";
RL   J. Mol. Biol. 233:789-798(1993).
RN   [2]
RP   PHOSPHORYLATION BY PHYTOCHROME A.
RX   PubMed=11115889; DOI=10.1104/pp.124.4.1728;
RA   Colon-Carmona A., Chen D.L., Yeh K.-C., Abel S.;
RT   "Aux/IAA proteins are phosphorylated by phytochrome in vitro.";
RL   Plant Physiol. 124:1728-1738(2000).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimers and heterodimers. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P49679; P49677: IAA1; Xeno; NbExp=3; IntAct=EBI-632357, EBI-630505;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: By auxin.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by phytochrome A in vitro.
CC       {ECO:0000269|PubMed:11115889}.
CC   -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA48298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X68215; CAA48297.1; -; mRNA.
DR   EMBL; X68216; CAA48298.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S39075; S39075.
DR   PDB; 2M1M; NMR; -; A=86-189.
DR   PDBsum; 2M1M; -.
DR   AlphaFoldDB; P49679; -.
DR   BMRB; P49679; -.
DR   SMR; P49679; -.
DR   ELM; P49679; -.
DR   IntAct; P49679; 1.
DR   EnsemblPlants; Psat6g102800.3; Psat6g102800.3.cds; Psat6g102800.
DR   Gramene; Psat6g102800.3; Psat6g102800.3.cds; Psat6g102800.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..189
FT                   /note="Auxin-induced protein IAA4"
FT                   /id="PRO_0000112861"
FT   DOMAIN          92..179
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   MOTIF           8..12
FT                   /note="EAR-like (transcriptional repression)"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   HELIX           116..126
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   STRAND          156..162
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   HELIX           164..170
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:2M1M"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:2M1M"
SQ   SEQUENCE   189 AA;  21036 MW;  BC699EF97443E580 CRC64;
     MEFKATELRL GLPGITEEEE KKIIHGSSVV KNNNKRQLPQ TSEESVSISK VTNDEHIVES
     SSAAPPAKAK IVGWPPIRSY RKNSLHEADV GGIFVKVSMD GAPYLRKIDL RVYGGYSELL
     KALETMFKLT IGEYSEREGY KGSEYAPTYE DKDGDWMLVG DVPWDMFVTS CKRLRIMKGT
     EAKGLGCGV