ARR20_ARATH
ID ARR20_ARATH Reviewed; 426 AA.
AC Q9LZJ8; F4IYC9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative two-component response regulator ARR20;
GN Name=ARR20; OrderedLocusNames=At3g62670; ORFNames=F26K9_100;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 TISSUE SPECIFICITY.
RX PubMed=15173562; DOI=10.1104/pp.103.038109;
RA Mason M.G., Li J., Mathews D.E., Kieber J.J., Schaller G.E.;
RT "Type-B response regulators display overlapping expression patterns in
RT Arabidopsis.";
RL Plant Physiol. 135:927-937(2004).
CC -!- FUNCTION: Putative transcriptional activator that binds specifically to
CC the DNA sequence 5'-[AG]GATT-3'. Functions as response regulator
CC involved in His-to-Asp phosphorelay signal transduction system.
CC Phosphorylation of the Asp residue in the receiver domain activates the
CC ability of the protein to promote the transcription of target genes.
CC Could directly activate some type-A response regulators in response to
CC cytokinins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds the target DNA as a monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in mature pistil tip. Also
CC detected in the shoot apical meristem as well as vascular tissue and
CC hydathodes of the leaves. {ECO:0000269|PubMed:15173562}.
CC -!- PTM: Two-component system major event consists of a His-to-Asp
CC phosphorelay between a sensor histidine kinase (HK) and a response
CC regulator (RR). In plants, the His-to-Asp phosphorelay involves an
CC additional intermediate named Histidine-containing phosphotransfer
CC protein (HPt). This multistep phosphorelay consists of a His-Asp-His-
CC Asp sequential transfer of a phosphate group between first an His and
CC an Asp of the HK protein, followed by the transfer to a conserved His
CC of the HPt protein and finally the transfer to an Asp in the receiver
CC domain of the RR protein.
CC -!- SIMILARITY: Belongs to the ARR family. Type-B subfamily. {ECO:0000305}.
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DR EMBL; AL162651; CAB83117.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80378.2; -; Genomic_DNA.
DR PIR; T48056; T48056.
DR RefSeq; NP_001319821.1; NM_001340168.1.
DR AlphaFoldDB; Q9LZJ8; -.
DR BioGRID; 10755; 1.
DR STRING; 3702.AT3G62670.1; -.
DR PaxDb; Q9LZJ8; -.
DR PRIDE; Q9LZJ8; -.
DR EnsemblPlants; AT3G62670.1; AT3G62670.1; AT3G62670.
DR GeneID; 825441; -.
DR Gramene; AT3G62670.1; AT3G62670.1; AT3G62670.
DR KEGG; ath:AT3G62670; -.
DR Araport; AT3G62670; -.
DR TAIR; locus:2081690; AT3G62670.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_788339_0_0_1; -.
DR InParanoid; Q9LZJ8; -.
DR OMA; FHMPDIN; -.
DR OrthoDB; 834249at2759; -.
DR PhylomeDB; Q9LZJ8; -.
DR PRO; PR:Q9LZJ8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZJ8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000156; F:phosphorelay response regulator activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR045279; ARR-like.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR017053; Response_reg_B-typ_pln.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43874; PTHR43874; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF036392; RR_ARR_type-B; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytokinin signaling pathway; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..426
FT /note="Putative two-component response regulator ARR20"
FT /id="PRO_0000132302"
FT DOMAIN 40..155
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 213..268
FT /note="Myb-like GARP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 161..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 210..213
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 174..189
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 426 AA; 48460 MW; 2A7AB6791B6E29BB CRC64;
MSVFSNILDE NSRNLRNEIP CDDGIASPIN DDDEEFLTKS NRVLLVGADS NSSLKNLMTQ
YSYQVTKYES GEEAMAFLMK NKHEIDLVIW DFHMPDINGL DALNIIGKQM DLPVVIMSHE
YKKETVMESI KYGACDFLVK PVSKEVIAVL WRHVYRKRMS KSGLDKPGES GTVESDPDEY
DDLEQDNLYE SNEEGSKNTC DHKEEKSPTK KPRMQWTPEL HHKFEVAVEK MGSLEKAFPK
TILKYMQEEL NVQGLTRNNV ASHLQKYRQS SKKTCTPQEP QEDFVWGNAG PDVTLAASKT
LLSSHATPSY LINNQAAPRG SYFMNNIPYP STSCLPVNNN NCFMTNPSTY IDQFQHQLQQ
QQQHQQYQST LNSISAMLTK QESRHVPSSA MENSEPLMIY NSNLPFGIDE CFPPAGFNIF
DQIGHN
