ARR4_ARATH
ID ARR4_ARATH Reviewed; 259 AA.
AC O82798;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Two-component response regulator ARR4;
DE AltName: Full=Response regulator 1;
GN Name=ARR4; Synonyms=ATRR1, IBC7; OrderedLocusNames=At1g10470;
GN ORFNames=T10O24.8;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9482949; DOI=10.1073/pnas.95.5.2691;
RA Imamura A., Hanaki N., Umeda H., Nakamura A., Suzuki T., Ueguchi C.,
RA Mizuno T.;
RT "Response regulators implicated in His-to-Asp phosphotransfer signaling in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2691-2696(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9607306; DOI=10.1016/s0014-5793(98)00418-9;
RA Urao T., Yakubov B., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Stress-responsive expression of genes for two-component response
RT regulator-like proteins in Arabidopsis thaliana.";
RL FEBS Lett. 427:175-178(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9634588; DOI=10.2307/3870686;
RA Brandstatter I., Kieber J.J.;
RT "Two genes with similarity to bacterial response regulators are rapidly and
RT specifically induced by cytokinin in Arabidopsis.";
RL Plant Cell 10:1009-1019(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=9662428; DOI=10.1016/s0014-5793(98)00611-5;
RA Taniguchi M., Kiba T., Sakakibara H., Ueguchi C., Mizuno T., Sugiyama T.;
RT "Expression of Arabidopsis response regulator homologs is induced by
RT cytokinins and nitrate.";
RL FEBS Lett. 429:259-262(1998).
RN [7]
RP INTERACTION WITH AHP1.
RX PubMed=10930573; DOI=10.1016/s0014-5793(00)01860-3;
RA Urao T., Miyata S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Possible His to Asp phosphorelay signaling in an Arabidopsis two-component
RT system.";
RL FEBS Lett. 478:227-232(2000).
RN [8]
RP INDUCTION.
RX PubMed=11115887; DOI=10.1104/pp.124.4.1706;
RA D'Agostino I.B., Deruere J., Kieber J.J.;
RT "Characterization of the response of the Arabidopsis response regulator
RT gene family to cytokinin.";
RL Plant Physiol. 124:1706-1717(2000).
RN [9]
RP FUNCTION, AND INTERACTION WITH PHYTOCHROME B.
RX PubMed=11691995; DOI=10.1126/science.1065022;
RA Sweere U., Eichenberg K., Lohrmann J., Mira-Rodado V., Baeurle I.,
RA Kudla J., Nagy F., Schaefer E., Harter K.;
RT "Interaction of the response regulator ARR4 with phytochrome B in
RT modulating red light signaling.";
RL Science 294:1108-1111(2001).
RN [10]
RP FUNCTION.
RX PubMed=14973166; DOI=10.1105/tpc.018978;
RA To J.P.C., Haberer G., Ferreira F.J., Deruere J., Mason M.G.,
RA Schaller G.E., Alonso J.M., Ecker J.R., Kieber J.J.;
RT "Type-A Arabidopsis response regulators are partially redundant negative
RT regulators of cytokinin signaling.";
RL Plant Cell 16:658-671(2004).
RN [11]
RP INTERACTION WITH DEGP9, SUBCELLULAR LOCATION, AND INDUCTION BY
RP TRANS-ZEATIN.
RX PubMed=27274065; DOI=10.1073/pnas.1601724113;
RA Chi W., Li J., He B., Chai X., Xu X., Sun X., Jiang J., Feng P., Zuo J.,
RA Lin R., Rochaix J.D., Zhang L.;
RT "DEG9, a serine protease, modulates cytokinin and light signaling by
RT regulating the level of ARABIDOPSIS RESPONSE REGULATOR 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E3568-E3576(2016).
CC -!- FUNCTION: Functions as response regulator involved in His-to-Asp
CC phosphorelay signal transduction system. Phosphorylation of the Asp
CC residue in the receiver domain activates the ability of the protein to
CC promote the transcription of target genes. Type-A response regulators
CC seem to act as negative regulators of the cytokinin signaling.
CC Modulates red light signaling through its interaction with the
CC phytochrome B photoreceptor. {ECO:0000269|PubMed:11691995,
CC ECO:0000269|PubMed:14973166, ECO:0000269|PubMed:9482949}.
CC -!- SUBUNIT: Interacts with the phytochrome B photoreceptor
CC (PubMed:11691995). Binds to AHP1 (PubMed:10930573). Interacts with
CC DEGP9 (PubMed:27274065). {ECO:0000269|PubMed:10930573,
CC ECO:0000269|PubMed:11691995, ECO:0000269|PubMed:27274065}.
CC -!- INTERACTION:
CC O82798; O80837: DBP; NbExp=3; IntAct=EBI-625213, EBI-1788073;
CC O82798; P14713: PHYB; NbExp=3; IntAct=EBI-625213, EBI-300727;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27274065}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots, and stems of
CC young inflorescences. {ECO:0000269|PubMed:9482949,
CC ECO:0000269|PubMed:9607306, ECO:0000269|PubMed:9634588}.
CC -!- INDUCTION: By low temperature, dehydration, abscisic acid (ABA),
CC cytokinins (BA and zeatin), nitrate and high salinity. Induced by
CC trans-zeatin (PubMed:27274065). {ECO:0000269|PubMed:11115887,
CC ECO:0000269|PubMed:27274065, ECO:0000269|PubMed:9607306,
CC ECO:0000269|PubMed:9634588, ECO:0000269|PubMed:9662428}.
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-A subfamily. {ECO:0000305}.
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DR EMBL; AB008487; BAA34726.1; -; mRNA.
DR EMBL; AB010915; BAA31143.1; -; mRNA.
DR EMBL; AF057282; AAC26636.1; -; mRNA.
DR EMBL; AC007067; AAD39568.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28583.1; -; Genomic_DNA.
DR PIR; T48851; T48851.
DR RefSeq; NP_172517.1; NM_100921.3.
DR AlphaFoldDB; O82798; -.
DR SMR; O82798; -.
DR BioGRID; 22827; 9.
DR IntAct; O82798; 10.
DR STRING; 3702.AT1G10470.1; -.
DR PaxDb; O82798; -.
DR PRIDE; O82798; -.
DR ProteomicsDB; 246672; -.
DR EnsemblPlants; AT1G10470.1; AT1G10470.1; AT1G10470.
DR GeneID; 837587; -.
DR Gramene; AT1G10470.1; AT1G10470.1; AT1G10470.
DR KEGG; ath:AT1G10470; -.
DR Araport; AT1G10470; -.
DR TAIR; locus:2194584; AT1G10470.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_000445_69_5_1; -.
DR InParanoid; O82798; -.
DR OrthoDB; 1311174at2759; -.
DR PhylomeDB; O82798; -.
DR PRO; PR:O82798; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O82798; baseline and differential.
DR Genevisible; O82798; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000156; F:phosphorelay response regulator activity; ISS:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR GO; GO:0010114; P:response to red light; IMP:TAIR.
DR InterPro; IPR045279; ARR-like.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43874; PTHR43874; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Cytokinin signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..259
FT /note="Two-component response regulator ARR4"
FT /id="PRO_0000081425"
FT DOMAIN 35..162
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 165..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 259 AA; 28297 MW; 557A4E2DA51948F5 CRC64;
MARDGGVSCL RRSEMMSVGG IGGIESAPLD LDEVHVLAVD DSLVDRIVIE RLLRITSCKV
TAVDSGWRAL EFLGLDNEKA SAEFDRLKVD LIITDYCMPG MTGYELLKKI KESSNFREVP
VVIMSSENVL TRIDRCLEEG AQDFLLKPVK LADVKRLRSH LTKDVKLSNG NKRKLPEDSS
SVNSSLPPPS PPLTISPESS PPLTVSTESS DSSPPLSPVE IFSTSPLSSP IDDEDDDVLT
SSSEESPIRR QKMRSPGLD
