RH10_ARATH
ID RH10_ARATH Reviewed; 456 AA.
AC Q8GY84; Q8LA24; Q9FME1; Q9ZS10;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 10;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:A2XKG2};
DE AltName: Full=Protein ENHANCER OF ASYMMETRIC LEAVES TWO {ECO:0000303|PubMed:27334696};
GN Name=RH10; Synonyms=EAST2; OrderedLocusNames=At5g60990;
GN ORFNames=MSL3.13, MSL3_110;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-456.
RC STRAIN=cv. Columbia;
RX PubMed=9862990; DOI=10.1093/nar/27.2.628;
RA Aubourg S., Kreis M., Lecharny A.;
RT "The DEAD box RNA helicase family in Arabidopsis thaliana.";
RL Nucleic Acids Res. 27:628-636(1999).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17168887; DOI=10.1111/j.1467-7652.2004.00084.x;
RA Mingam A., Toffano-Nioche C., Brunaud V., Boudet N., Kreis M., Lecharny A.;
RT "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT between quantitative expression, gene structure and evolution of a family
RT of genes.";
RL Plant Biotechnol. J. 2:401-415(2004).
RN [8]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF THR-273.
RC STRAIN=cv. Columbia {ECO:0000303|PubMed:27334696}, and
RC cv. Landsberg erecta {ECO:0000303|PubMed:27334696};
RX PubMed=27334696; DOI=10.1242/bio.019109;
RA Matsumura Y., Ohbayashi I., Takahashi H., Kojima S., Ishibashi N., Keta S.,
RA Nakagawa A., Hayashi R., Saez-Vasquez J., Echeverria M., Sugiyama M.,
RA Nakamura K., Machida C., Machida Y.;
RT "A genetic link between epigenetic repressor AS1-AS2 and a putative small
RT subunit processome in leaf polarity establishment of Arabidopsis.";
RL Biol. Open 5:942-954(2016).
CC -!- FUNCTION: Involved in leaf polarity establishment by functioning
CC cooperatively with AS2 to repress abaxial genes ARF3, ARF4, KAN1, KAN2,
CC YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM
CC to promote adaxial development in leaf primordia at shoot apical
CC meristems at high temperatures. Involved in the processing of pre-rRNA
CC intermediates at high temperatures. {ECO:0000269|PubMed:27334696}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:A2XKG2};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27334696}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:27334696}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues and organs examined
CC including root, cotyledon, first and second leaves, third and fourth
CC leaves, fifth and sixth leaves, shoot apex, flower, flower bud, cauline
CC leaf and rosette leaves. {ECO:0000269|PubMed:27334696}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- DISRUPTION PHENOTYPE: Plants are indistinguishable from that of wild-
CC type at 16 degrees Celsius, however they generate a weak phenotype of
CC pointed leaves at 22 degrees Celsius which become narrower at 26
CC degrees Celsius. In the leaves of plants grown at 26 degrees Celsius,
CC the xylems are located on the adaxial sides and the phloems are on the
CC abaxial sides, similar to those in the wild type. Plants with double
CC mutations in this protein and in AS2 or AS1 protein have abaxialized
CC filamentous and trumpet-like leaves with loss of the adaxial domain at
CC high temperatures. In double mutants, shapes of epidermal cells of the
CC filamentous leaves are simple and rectangular, similar to those of a
CC petiole, but different from those of flat leaves of wild-type plants.
CC The filamentous leaves of the double mutant at 26 degrees Celsius show
CC primitive or no vascular tissue without apparent xylem cells inside the
CC bundle sheath, suggesting defects in differentiation of xylem cells on
CC the adaxial side. {ECO:0000269|PubMed:27334696}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB008269; BAB10648.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97408.1; -; Genomic_DNA.
DR EMBL; AK117799; BAC42444.1; -; mRNA.
DR EMBL; BT005375; AAO63439.1; -; mRNA.
DR EMBL; AY088068; AAM65614.1; -; mRNA.
DR EMBL; AJ010462; CAA09201.1; -; mRNA.
DR PIR; T51342; T51342.
DR RefSeq; NP_568931.1; NM_125492.5.
DR AlphaFoldDB; Q8GY84; -.
DR SMR; Q8GY84; -.
DR STRING; 3702.AT5G60990.1; -.
DR iPTMnet; Q8GY84; -.
DR PaxDb; Q8GY84; -.
DR PRIDE; Q8GY84; -.
DR ProteomicsDB; 236906; -.
DR EnsemblPlants; AT5G60990.1; AT5G60990.1; AT5G60990.
DR GeneID; 836220; -.
DR Gramene; AT5G60990.1; AT5G60990.1; AT5G60990.
DR KEGG; ath:AT5G60990; -.
DR Araport; AT5G60990; -.
DR TAIR; locus:2173517; AT5G60990.
DR eggNOG; KOG0330; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q8GY84; -.
DR OMA; YDIELYQ; -.
DR OrthoDB; 744428at2759; -.
DR PhylomeDB; Q8GY84; -.
DR PRO; PR:Q8GY84; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GY84; baseline and differential.
DR Genevisible; Q8GY84; AT.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd17954; DEADc_DDX47; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044765; DDX47/Rrp3_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repressor; RNA-binding; rRNA processing;
KW Stress response.
FT CHAIN 1..456
FT /note="DEAD-box ATP-dependent RNA helicase 10"
FT /id="PRO_0000239152"
FT DOMAIN 40..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 250..394
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 407..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..37
FT /note="Q motif"
FT MOTIF 171..174
FT /note="DEAD box"
FT COMPBIAS 411..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 273
FT /note="T->I: In rh10-1; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:27334696"
FT CONFLICT 124
FT /note="V -> F (in Ref. 5; AAM65614)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="L -> R (in Ref. 5; AAM65614)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="K -> E (in Ref. 3; BAC42444 and 4; AAO63439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 51147 MW; 6D882E48C7224FB6 CRC64;
MEEENEVVKT FAELGVREEL VKACERLGWK NPSKIQAEAL PFALEGKDVI GLAQTGSGKT
GAFAIPILQA LLEYVYDSEP KKGRRPDPAF FACVLSPTRE LAIQIAEQFE ALGADISLRC
AVLVGGIDRM QQTIALGKRP HVIVATPGRL WDHMSDTKGF SLKSLKYLVL DEADRLLNED
FEKSLNQILE EIPLERKTFL FSATMTKKVR KLQRACLRNP VKIEAASKYS TVDTLKQQYR
FVAAKYKDCY LVYILSEMPE STSMIFTRTC DGTRFLALVL RSLGFRAIPI SGQMTQSKRL
GALNKFKAGE CNILVCTDVA SRGLDIPSVD VVINYDIPTN SKDYIHRVGR TARAGRSGVG
ISLVNQYELE WYIQIEKLIG KKLPEYPAEE DEVLSLLERV AEAKKLSAMN MKESGGRKRR
GEDDEESERF LGGNKDRGNK ERGGNKDKKS SKKFKR
