ID   AX22D_VIGRR             Reviewed;         193 AA.
AC   O24542;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Auxin-induced protein 22D;
DE   AltName: Full=Indole-3-acetic acid-induced protein ARG13;
GN   Name=AUX22D; Synonyms=ARG13;
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   Hashimoto H., Yamamoto K.T.;
RT   "Three more members of the Aux/IAA gene family from mung bean (Vigna
RT   radiata) hypocotyl.";
RL   (er) Plant Gene Register PGR97-137(1997).
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   -!- 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   -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
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DR   EMBL; AB004932; BAA20848.1; -; mRNA.
DR   PIR; T10884; T10884.
DR   AlphaFoldDB; O24542; -.
DR   SMR; O24542; -.
DR   STRING; 3916.O24542; -.
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..193
FT                   /note="Auxin-induced protein 22D"
FT                   /id="PRO_0000112866"
FT   DOMAIN          97..184
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   REGION          16..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           19..23
FT                   /note="EAR-like (transcriptional repression)"
FT   COMPBIAS        24..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   193 AA;  21699 MW;  08F738C0BD9C03F1 CRC64;
     MENSLGSYEK ELNLKATELR LGLPGSDEPE KRATARSNKR SSPEASDEES ISNGSDVTKE
     DNVVPPAKAQ VVGWPPIRSY RKNNVQQKKE EESEGNGMYV KVSMAGAPYL RKIDLKVYKS
     YPELLKALEN MFKCIFGEYS EREGYNGSEY APTYEDKDGD WMLVGDVPWN MFVSSCKRLR
     IMKGSEAKGL GCF