ARR1_ARATH
ID ARR1_ARATH Reviewed; 690 AA.
AC Q940D0; B9DFS4; Q9LIB7; Q9ZWK0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Two-component response regulator ARR1;
GN Name=ARR1; OrderedLocusNames=At3g16857; ORFNames=K20I9.9, MUH15.1;
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 [GENOMIC DNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9891419; DOI=10.1093/oxfordjournals.pcp.a029325;
RA Sakai H., Aoyama T., Bono H., Oka A.;
RT "Two-component response regulators from Arabidopsis thaliana contain a
RT putative DNA-binding motif.";
RL Plant Cell Physiol. 39:1232-1239(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP DNA-BINDING SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11135105; DOI=10.1046/j.1365-313x.2000.00909.x;
RA Sakai H., Aoyama T., Oka A.;
RT "Arabidopsis ARR1 and ARR2 response regulators operate as transcriptional
RT activators.";
RL Plant J. 24:703-711(2000).
RN [8]
RP FUNCTION.
RX PubMed=11691951; DOI=10.1126/science.1065201;
RA Sakai H., Honma T., Aoyama T., Sato S., Kato T., Tabata S., Oka A.;
RT "ARR1, a transcription factor for genes immediately responsive to
RT cytokinins.";
RL Science 294:1519-1521(2001).
RN [9]
RP FUNCTION.
RX PubMed=11574878; DOI=10.1038/35096500;
RA Hwang I., Sheen J.;
RT "Two-component circuitry in Arabidopsis cytokinin signal transduction.";
RL Nature 413:383-389(2001).
RN [10]
RP INTERACTION.
RX PubMed=14981318; DOI=10.1271/bbb.68.462;
RA Tanaka Y., Suzuki T., Yamashino T., Mizuno T.;
RT "Comparative studies of the AHP histidine-containing phosphotransmitters
RT implicated in His-to-Asp phosphorelay in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 68:462-465(2004).
RN [11]
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).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17363254; DOI=10.1016/j.cub.2007.02.047;
RA Dello Ioio R., Linhares F.S., Scacchi E., Casamitjana-Martinez E.,
RA Heidstra R., Costantino P., Sabatini S.;
RT "Cytokinins determine Arabidopsis root-meristem size by controlling cell
RT differentiation.";
RL Curr. Biol. 17:678-682(2007).
RN [13]
RP FUNCTION.
RX PubMed=19039136; DOI=10.1126/science.1164147;
RA Dello Ioio R., Nakamura K., Moubayidin L., Perilli S., Taniguchi M.,
RA Morita M.T., Aoyama T., Costantino P., Sabatini S.;
RT "A genetic framework for the control of cell division and differentiation
RT in the root meristem.";
RL Science 322:1380-1384(2008).
RN [14]
RP INDUCTION BY GIBBERELLIN.
RX PubMed=20605455; DOI=10.1016/j.cub.2010.05.035;
RA Moubayidin L., Perilli S., Dello Ioio R., Di Mambro R., Costantino P.,
RA Sabatini S.;
RT "The rate of cell differentiation controls the Arabidopsis root meristem
RT growth phase.";
RL Curr. Biol. 20:1138-1143(2010).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in
CC His-to-Asp phosphorelay signal transduction system. Phosphorylation of
CC the Asp residue in the receiver domain activates the ability of the
CC protein to promote the transcription of target genes. Could directly
CC activate some type-A response regulators in response to cytokinins.
CC Regulates SHY2 by binding to its promoter (PubMed:19039136). Involved
CC in the root-meristem size determination through the regulation of cell
CC differentiation (PubMed:17363254). {ECO:0000269|PubMed:11574878,
CC ECO:0000269|PubMed:11691951, ECO:0000269|PubMed:17363254,
CC ECO:0000269|PubMed:19039136}.
CC -!- SUBUNIT: Binds the target DNA as a monomer (By similarity). Interacts
CC with histidine-containing phosphotransfer proteins. {ECO:0000250,
CC ECO:0000269|PubMed:14981318}.
CC -!- INTERACTION:
CC Q940D0; Q9ZNV9: AHP1; NbExp=3; IntAct=EBI-1100998, EBI-1100673;
CC Q940D0; Q9SAZ5: AHP3; NbExp=3; IntAct=EBI-1100998, EBI-1100711;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:11135105}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q940D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q940D0-2; Sequence=VSP_010853, VSP_010854;
CC -!- TISSUE SPECIFICITY: Detected in the whole plant. Expressed at the root
CC transition zone (PubMed:17363254). {ECO:0000269|PubMed:15173562,
CC ECO:0000269|PubMed:17363254, ECO:0000269|PubMed:9891419}.
CC -!- DEVELOPMENTAL STAGE: Expressed only from 5 days post germination
CC onward, when the fixed meristem cell number is established.
CC {ECO:0000269|PubMed:17363254}.
CC -!- INDUCTION: Down-regulated by gibberellin.
CC {ECO:0000269|PubMed:20605455}.
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ARR family. Type-B subfamily. {ECO:0000305}.
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DR EMBL; AB016471; BAA74528.1; -; Genomic_DNA.
DR EMBL; AP001308; BAB03073.1; -; Genomic_DNA.
DR EMBL; AB028608; BAB03073.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE75875.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75876.1; -; Genomic_DNA.
DR EMBL; AY056099; AAL06987.1; -; mRNA.
DR EMBL; AK316883; BAH19591.1; -; mRNA.
DR PIR; T51246; T51246.
DR RefSeq; NP_566561.2; NM_112561.5. [Q940D0-1]
DR RefSeq; NP_850600.2; NM_180269.3. [Q940D0-2]
DR AlphaFoldDB; Q940D0; -.
DR SMR; Q940D0; -.
DR BioGRID; 6273; 16.
DR IntAct; Q940D0; 18.
DR STRING; 3702.AT3G16857.2; -.
DR iPTMnet; Q940D0; -.
DR PaxDb; Q940D0; -.
DR PRIDE; Q940D0; -.
DR ProteomicsDB; 246933; -. [Q940D0-1]
DR EnsemblPlants; AT3G16857.1; AT3G16857.1; AT3G16857. [Q940D0-2]
DR EnsemblPlants; AT3G16857.2; AT3G16857.2; AT3G16857. [Q940D0-1]
DR GeneID; 820940; -.
DR Gramene; AT3G16857.1; AT3G16857.1; AT3G16857. [Q940D0-2]
DR Gramene; AT3G16857.2; AT3G16857.2; AT3G16857. [Q940D0-1]
DR KEGG; ath:AT3G16857; -.
DR Araport; AT3G16857; -.
DR TAIR; locus:2093668; AT3G16857.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_024359_0_1_1; -.
DR InParanoid; Q940D0; -.
DR PhylomeDB; Q940D0; -.
DR PRO; PR:Q940D0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940D0; baseline and differential.
DR Genevisible; Q940D0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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:0090506; P:axillary shoot meristem initiation; IMP:TAIR.
DR GO; GO:1990110; P:callus formation; IGI:TAIR.
DR GO; GO:0071368; P:cellular response to cytokinin stimulus; IMP:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IGI:TAIR.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IGI:TAIR.
DR GO; GO:0080022; P:primary root development; IGI:TAIR.
DR GO; GO:0031537; P:regulation of anthocyanin metabolic process; IGI:TAIR.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IGI:TAIR.
DR GO; GO:0080036; P:regulation of cytokinin-activated signaling pathway; IMP:CACAO.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:CACAO.
DR GO; GO:0080113; P:regulation of seed growth; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IGI: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 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytokinin signaling pathway; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..690
FT /note="Two-component response regulator ARR1"
FT /id="PRO_0000132293"
FT DOMAIN 38..153
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 239..289
FT /note="Myb-like GARP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 236..239
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT VAR_SEQ 669
FT /note="E -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_010853"
FT VAR_SEQ 670..690
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_010854"
FT CONFLICT 528
FT /note="P -> T (in Ref. 5; AAL06987)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="T -> I (in Ref. 1; BAA74528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 75177 MW; 8AB6D05DEA94EC4F CRC64;
MMNPSHGRGL GSAGGSSSGR NQGGGGETVV EMFPSGLRVL VVDDDPTCLM ILERMLRTCL
YEVTKCNRAE MALSLLRKNK HGFDIVISDV HMPDMDGFKL LEHVGLEMDL PVIMMSADDS
KSVVLKGVTH GAVDYLIKPV RMEALKNIWQ HVVRKRRSEW SVPEHSGSIE ETGERQQQQH
RGGGGGAAVS GGEDAVDDNS SSVNEGNNWR SSSRKRKDEE GEEQGDDKDE DASNLKKPRV
VWSVELHQQF VAAVNQLGVE KAVPKKILEL MNVPGLTREN VASHLQKYRI YLRRLGGVSQ
HQGNLNNSFM TGQDASFGPL STLNGFDLQA LAVTGQLPAQ SLAQLQAAGL GRPAMVSKSG
LPVSSIVDER SIFSFDNTKT RFGEGLGHHG QQPQQQPQMN LLHGVPTGLQ QQLPMGNRMS
IQQQIAAVRA GNSVQNNGML MPLAGQQSLP RGPPPMLTSS QSSIRQPMLS NRISERSGFS
GRNNIPESSR VLPTSYTNLT TQHSSSSMPY NNFQPELPVN SFPLASAPGI SVPVRKATSY
QEEVNSSEAG FTTPSYDMFT TRQNDWDLRN IGIAFDSHQD SESAAFSASE AYSSSSMSRH
NTTVAATEHG RNHQQPPSGM VQHHQVYADG NGGSVRVKSE RVATDTATMA FHEQYSNQED
LMSALLKQEG IAPVDGEFDF DAYSIDNIPV
