ID   AX22B_VIGRR             Reviewed;         196 AA.
AC   P32294;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Auxin-induced protein 22B;
DE   AltName: Full=Indole-3-acetic acid-induced protein ARG4;
GN   Name=AUX22B; Synonyms=ARG4;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypocotyl;
RA   Yamamoto K.T., Mori H., Imaseki H.;
RT   "cDNA cloning of indole-3-acetic acid regulated genes: Aux22 and SAUR from
RT   mung bean (Vigna radiata) hypocotyl tissue.";
RL   Plant Cell Physiol. 33:93-97(1992).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Found in elongating hypocotyls.
CC   -!- INDUCTION: By auxin and cycloheximide.
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   -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D14413; BAA03309.1; -; mRNA.
DR   PIR; T10941; T10941.
DR   AlphaFoldDB; P32294; -.
DR   SMR; P32294; -.
DR   STRING; 3916.P32294; -.
DR   PRIDE; P32294; -.
DR   Proteomes; UP000087766; Genome assembly.
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   2: Evidence at transcript level;
KW   Auxin signaling pathway; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..196
FT                   /note="Auxin-induced protein 22B"
FT                   /id="PRO_0000112864"
FT   DOMAIN          99..186
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   MOTIF           18..22
FT                   /note="EAR-like (transcriptional repression)"
FT   COMPBIAS        48..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   196 AA;  22050 MW;  2BAF114D84E6E90C CRC64;
     MESRVVFESD LNLKATELRL GLPGTEEKED NNLRTHAVLR NNKRQVRETS QDSVSISKAS
     HHQQHVETVS APPPKAKIVG WPPIRSYRKN SVQEGEGDGI FVKVSMDGAP YLRKVDLKVY
     GGYPELLKAL ETMFKLAIGE YSEREGYKGS EYAPTYEDKD GDWMLVGDVP WDMFVTSCKR
     LRIMKGSEAR GLGCVV