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}.
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; 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