ID   AX22A_VIGRR             Reviewed;         194 AA.
AC   P32293;
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 22A;
DE   AltName: Full=Indole-3-acetic acid-induced protein ARG3;
GN   Name=AUX22A; Synonyms=ARG3;
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}.
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DR   EMBL; D14412; BAA03308.1; -; mRNA.
DR   PIR; T10939; T10939.
DR   AlphaFoldDB; P32293; -.
DR   SMR; P32293; -.
DR   STRING; 3916.P32293; -.
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..194
FT                   /note="Auxin-induced protein 22A"
FT                   /id="PRO_0000112863"
FT   DOMAIN          85..173
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   REGION          40..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           13..17
FT                   /note="EAR-like (transcriptional repression)"
SQ   SEQUENCE   194 AA;  21514 MW;  B8E3BC6D925FC88C CRC64;
     MAKEGLGLEI TELRLGLPDA EHVAVANKNG EKKNKRVFSE IDDVGDENSS SGGGGDRKME
     NKNQVVGWPP VCSYRKKNSV NEASKMYVKV SMDGAPFLRK MDLGMHKGYS DLAFALEKLF
     GCYGMVEALK NVENGEHVPI YEDKDGDWML VGDVPWEMFM ESCKRLRIMK RADAKGFGLQ
     PKGSLKGFIE SVGK