ARR10_ARATH
ID ARR10_ARATH Reviewed; 552 AA.
AC O49397;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Two-component response regulator ARR10;
DE AltName: Full=Receiver-like protein 4;
GN Name=ARR10; Synonyms=ARP4; OrderedLocusNames=At4g31920; ORFNames=F10N7.270;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Lohrmann J., Buchholz G., Keitel C., Sweere U., Kircher S., Baeurle I.,
RA Kudla J., Schaefer E., Harter K.;
RT "Differential expression and nuclear localization of response regulator-
RT like proteins from Arabidopsis thaliana.";
RL Plant Biol. 1:495-505(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [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.
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 [6]
RP DNA-BINDING SPECIFICITY, SUBCELLULAR LOCATION, AND STRUCTURE BY NMR OF
RP 179-242.
RX PubMed=12215502; DOI=10.1105/tpc.002733;
RA Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H.,
RA Mizuno T., Yamazaki T.;
RT "Molecular structure of the GARP family of plant Myb-related DNA binding
RT motifs of the Arabidopsis response regulators.";
RL Plant Cell 14:2015-2029(2002).
RN [7]
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: 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 {ECO:0000269|PubMed:11574878}.
CC -!- SUBUNIT: Binds the target DNA as a monomer.
CC -!- INTERACTION:
CC O49397; Q9ZNV8: AHP2; NbExp=3; IntAct=EBI-1101329, EBI-1100687;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:12215502}.
CC -!- TISSUE SPECIFICITY: Detected in the whole plant. Predominantly
CC expressed in roots and 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; AJ005195; CAA06432.1; -; mRNA.
DR EMBL; AL021636; CAA16597.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79910.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85979.1; -; Genomic_DNA.
DR EMBL; BT003158; AAO24590.1; -; mRNA.
DR PIR; T04653; T04653.
DR RefSeq; NP_194920.1; NM_119343.4.
DR PDB; 1IRZ; NMR; -; A=179-242.
DR PDBsum; 1IRZ; -.
DR AlphaFoldDB; O49397; -.
DR BMRB; O49397; -.
DR SMR; O49397; -.
DR BioGRID; 14608; 10.
DR IntAct; O49397; 7.
DR STRING; 3702.AT4G31920.1; -.
DR PaxDb; O49397; -.
DR PRIDE; O49397; -.
DR ProteomicsDB; 246926; -.
DR EnsemblPlants; AT4G31920.1; AT4G31920.1; AT4G31920.
DR GeneID; 829322; -.
DR Gramene; AT4G31920.1; AT4G31920.1; AT4G31920.
DR KEGG; ath:AT4G31920; -.
DR Araport; AT4G31920; -.
DR TAIR; locus:2116587; AT4G31920.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_024359_0_0_1; -.
DR InParanoid; O49397; -.
DR OMA; DLMNVDK; -.
DR OrthoDB; 332559at2759; -.
DR PhylomeDB; O49397; -.
DR EvolutionaryTrace; O49397; -.
DR PRO; PR:O49397; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49397; baseline and differential.
DR Genevisible; O49397; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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; IGI:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IGI: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 3D-structure; Activator; Coiled coil; Cytokinin signaling pathway;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..552
FT /note="Two-component response regulator ARR10"
FT /id="PRO_0000132295"
FT DOMAIN 18..133
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 185..235
FT /note="Myb-like GARP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 139..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 151..173
FT /evidence="ECO:0000255"
FT MOTIF 182..185
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 69
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:1IRZ"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1IRZ"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:1IRZ"
FT HELIX 224..239
FT /evidence="ECO:0007829|PDB:1IRZ"
SQ SEQUENCE 552 AA; 61652 MW; B419363AC09E9555 CRC64;
MTMEQEIEVL DQFPVGMRVL AVDDDQTCLR ILQTLLQRCQ YHVTTTNQAQ TALELLRENK
NKFDLVISDV DMPDMDGFKL LELVGLEMDL PVIMLSAHSD PKYVMKGVKH GACDYLLKPV
RIEELKNIWQ HVVRKSKLKK NKSNVSNGSG NCDKANRKRK EQYEEEEEEE RGNDNDDPTA
QKKPRVLWTH ELHNKFLAAV DHLGVERAVP KKILDLMNVD KLTRENVASH LQKFRVALKK
VSDDAIQQAN RAAIDSHFMQ MNSQKGLGGF YHHHRGIPVG SGQFHGGTTM MRHYSSNRNL
GRLNSLGAGM FQPVSSSFPR NHNDGGNILQ GLPLEELQIN NNINRAFPSF TSQQNSPMVA
PSNLLLLEGN PQSSSLPSNP GFSPHFEISK RLEHWSNAAL STNIPQSDVH SKPDTLEWNA
FCDSASPLVN PNLDTNPASL CRNTGFGSTN AAQTDFFYPL QMNQQPANNS GPVTEAQLFR
SSNPNEGLLM GQQKLQSGLM ASDAGSLDDI VNSLMTQEQS QSDFSEGDWD LDGLAHSEHA
YEKLHFPFSL SA
