AAR3_ARATH
ID AAR3_ARATH Reviewed; 295 AA.
AC Q9MBG8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Defective in cullin neddylation protein AAR3 {ECO:0000305};
DE AltName: Full=Protein ANTIAUXIN-RESISTANT 3 {ECO:0000303|PubMed:17905859};
GN Name=AAR3 {ECO:0000303|PubMed:17905859};
GN OrderedLocusNames=At3g28970 {ECO:0000312|Araport:AT3G28970};
GN ORFNames=K5K13.8 {ECO:0000312|EMBL:AAO64110.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17905859; DOI=10.1104/pp.107.104844;
RA Biswas K.K., Ooura C., Higuchi K., Miyazaki Y., Van Nguyen V., Rahman A.,
RA Uchimiya H., Kiyosue T., Koshiba T., Tanaka A., Narumi I., Oono Y.;
RT "Genetic characterization of mutants resistant to the antiauxin p-
RT chlorophenoxyisobutyric acid reveals that AAR3, a gene encoding a DCN1-like
RT protein, regulates responses to the synthetic auxin 2,4-
RT dichlorophenoxyacetic acid in Arabidopsis roots.";
RL Plant Physiol. 145:773-785(2007).
CC -!- FUNCTION: May contribute to the neddylation of all cullins by
CC transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s
CC enzyme to different cullin C-terminal domain-RBX complexes; neddylation
CC of cullins play an essential role in the regulation of SCF-type
CC complexes activity (By similarity). Regulates responses to the
CC synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D) in roots,
CC probably by modulating the SCF(TIR1) ubiquitin E3 ligase complex-
CC mediated proteolysis (PubMed:17905859). {ECO:0000250|UniProtKB:Q6PH85,
CC ECO:0000269|PubMed:17905859}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:17905859}.
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC interaction with different cullins. {ECO:0000250|UniProtKB:Q6PH85}.
CC -!- DISRUPTION PHENOTYPE: Root growth resistance to the anti-auxin p-
CC chlorophenoxyisobutyric acid (PCIB), which inhibits auxin action by
CC interfering the upstream auxin-signaling events (PubMed:17905859). Also
CC resistant to the auxin analog 2,4-dichlorophenoxyacetic acid (2,4-D)
CC herbicide (PubMed:17905859). {ECO:0000269|PubMed:17905859}.
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DR EMBL; AB025615; BAA95750.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77516.1; -; Genomic_DNA.
DR EMBL; AK118926; BAC43507.1; -; mRNA.
DR EMBL; BT005690; AAO64110.1; -; mRNA.
DR RefSeq; NP_189539.1; NM_113818.4.
DR AlphaFoldDB; Q9MBG8; -.
DR SMR; Q9MBG8; -.
DR STRING; 3702.AT3G28970.1; -.
DR PaxDb; Q9MBG8; -.
DR PRIDE; Q9MBG8; -.
DR ProteomicsDB; 187124; -.
DR EnsemblPlants; AT3G28970.1; AT3G28970.1; AT3G28970.
DR GeneID; 822537; -.
DR Gramene; AT3G28970.1; AT3G28970.1; AT3G28970.
DR KEGG; ath:AT3G28970; -.
DR Araport; AT3G28970; -.
DR TAIR; locus:2087022; AT3G28970.
DR eggNOG; KOG3077; Eukaryota.
DR HOGENOM; CLU_071720_0_0_1; -.
DR InParanoid; Q9MBG8; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q9MBG8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MBG8; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR Gene3D; 1.10.238.200; -; 1.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR042460; DCN1-like_PONY.
DR InterPro; IPR005176; PONY_dom.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 2: Evidence at transcript level;
KW Auxin signaling pathway; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..295
FT /note="Defective in cullin neddylation protein AAR3"
FT /id="PRO_0000452736"
FT DOMAIN 1..180
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 214..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..221
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
SQ SEQUENCE 295 AA; 34372 MW; AF5F27C863388D4C CRC64;
MDSSPVSARF DIFEIYRRFC AIRSGQQLCN KKPCDGEESQ RFNLSKEAIT QLLYLVENKF
QARNSIFDEL FKLMSRLDLM VDFTEFTCFY DFVFFMCREN GQKNITISRA ITAWKLVLAG
RFRLLNRWCD FIEKNQRHNI SEDTWQQVLA FSRCVHENLE GYDSEGAWPV LIDDFVEHMY
SILGPNKDTS LFCKCGDTES ESCLYQEDEH HKDYRRPHTG LRNIPGLKRK TSKKNDEEEE
DEDEEVLETQ NSSSLLNFKR IKTSNSPRCS SKSPCSIERS LSQGFASLLS TGDKP
