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AX22E_VIGRR
ID   AX22E_VIGRR             Reviewed;         203 AA.
AC   O24543;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Auxin-induced protein 22E;
DE   AltName: Full=Indole-3-acetic acid-induced protein ARG14;
GN   Name=AUX22E; Synonyms=ARG14;
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; AB004933; BAA20849.1; -; mRNA.
DR   PIR; T10885; T10885.
DR   RefSeq; NP_001304245.1; NM_001317316.1.
DR   AlphaFoldDB; O24543; -.
DR   SMR; O24543; -.
DR   STRING; 3916.O24543; -.
DR   GeneID; 106757071; -.
DR   KEGG; vra:106757071; -.
DR   Proteomes; UP000087766; Chromosome 3.
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..203
FT                   /note="Auxin-induced protein 22E"
FT                   /id="PRO_0000112867"
FT   DOMAIN          107..199
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   REGION          15..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           15..19
FT                   /note="EAR-like (transcriptional repression)"
FT   COMPBIAS        56..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   203 AA;  22695 MW;  4B13504E5A191F49 CRC64;
     MGSYETELNL RATELRLGLP GSDEPQEKRP CSGSVVRSSN KRSSPELEES RCKSNINSDS
     SDSTTTSDHN EDSVQPAKVQ VVGWPPIRSF RKNSLQQKKV EQGDGTGMYL KVSMAGAPYL
     RKIDLKVYKS YPELLKALQN LFKCTFGEYS EREGYNGSEY APTYEDKDGD WMLVGDVPWN
     MFVSSCKRLR IIKGSEAKGL GCL
 
 
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