ARR11_ARATH
ID ARR11_ARATH Reviewed; 521 AA.
AC Q9FXD6; O81712; Q9MAY2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Two-component response regulator ARR11;
DE AltName: Full=Receiver-like protein 3;
GN Name=ARR11; Synonyms=ARP3; OrderedLocusNames=At1g67710; ORFNames=F12A21.15;
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=Hypocotyl;
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=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 [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 NUCLEOTIDE SEQUENCE OF 1-462.
RC STRAIN=cv. Columbia;
RA Mizuno T.;
RT "ARR11: a member of the type-B family of response regulators of Arabidopsis
RT thaliana.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CHARACTERIZATION, AND FUNCTION.
RX PubMed=12610214; DOI=10.1093/pcp/pcg014;
RA Imamura A., Kiba T., Tajima Y., Yamashino T., Mizuno T.;
RT "In vivo and in vitro characterization of the ARR11 response regulator
RT implicated in the His-to-Asp phosphorelay signal transduction in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:122-131(2003).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12610214}.
CC -!- SUBUNIT: Binds the target DNA as a monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9FXD6; Q67XQ1: At1g03430; NbExp=2; IntAct=EBI-1101048, EBI-1100725;
CC Q9FXD6; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-1101048, EBI-15193025;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Detected in the whole plant. Predominantly
CC expressed in roots and stems. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA94549.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA06431.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ005194; CAA06431.1; ALT_FRAME; mRNA.
DR EMBL; AC008113; AAG28891.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34686.1; -; Genomic_DNA.
DR EMBL; BT008768; AAP68207.1; -; mRNA.
DR EMBL; AB041532; BAA94549.1; ALT_FRAME; mRNA.
DR PIR; C96700; C96700.
DR PIR; T52034; T52034.
DR PIR; T52074; T52074.
DR RefSeq; NP_176938.1; NM_105439.3.
DR AlphaFoldDB; Q9FXD6; -.
DR SMR; Q9FXD6; -.
DR BioGRID; 28317; 8.
DR IntAct; Q9FXD6; 6.
DR STRING; 3702.AT1G67710.1; -.
DR PaxDb; Q9FXD6; -.
DR PRIDE; Q9FXD6; -.
DR ProteomicsDB; 246927; -.
DR EnsemblPlants; AT1G67710.1; AT1G67710.1; AT1G67710.
DR GeneID; 843096; -.
DR Gramene; AT1G67710.1; AT1G67710.1; AT1G67710.
DR KEGG; ath:AT1G67710; -.
DR Araport; AT1G67710; -.
DR TAIR; locus:2008585; AT1G67710.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_024359_3_0_1; -.
DR InParanoid; Q9FXD6; -.
DR OrthoDB; 609085at2759; -.
DR PhylomeDB; Q9FXD6; -.
DR PRO; PR:Q9FXD6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXD6; baseline and differential.
DR Genevisible; Q9FXD6; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:CACAO.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Cytokinin signaling pathway; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..521
FT /note="Two-component response regulator ARR11"
FT /id="PRO_0000132296"
FT DOMAIN 12..127
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 195..246
FT /note="Myb-like GARP"
FT MOTIF 192..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 63
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 103..104
FT /note="QH -> HT (in Ref. 1; CAA06431)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="L -> P (in Ref. 1; CAA06431)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="N -> I (in Ref. 1; CAA06431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58579 MW; D0727FCAB617F102 CRC64;
MEKSGFSPVG LRVLVVDDDP TWLKILEKML KKCSYEVTTC GLAREALRLL RERKDGYDIV
ISDVNMPDMD GFKLLEHVGL ELDLPVIMMS VDGETSRVMK GVQHGACDYL LKPIRMKELK
IIWQHVLRKK LQEVRDIEGC GYEGGADWIT RYDEAHFLGG GEDVSFGKKR KDFDFEKKLL
QDESDPSSSS SKKARVVWSF ELHHKFVNAV NQIGCDHKAG PKKILDLMNV PWLTRENVAS
HLQKYRLYLS RLEKGKELKC YSGGVKNADS SPKDVEVNSG YQSPGRSSYV FSGGNSLIQK
ATEIDPKPLA SASLSDLNTD VIMPPKTKKT RIGFDPPISS SAFDSLLPWN DVPEVLESKP
VLYENSFLQQ QPLPSQSSYV ANSAPSLMEE EMKPPYETPA GGSSVNADEF LMPQDKIPTV
TLQDLDPSAM KLQEFNTEAI LRSLNWELPE SHHSVSLDTD LDLTWLQGER FLANTGLQFQ
DYSSSPSLLS ELPAHLNWYG NERLPDPDEY SFMVDQGLFI S
