GenomeNet

Database: UniProt
Entry: Q8GY84
LinkDB: Q8GY84
Original site: Q8GY84 
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   16-OCT-2019, entry version 114.
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;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.
RT   Sequence features of the regions of 1,191,918 bp covered by seventeen
RT   physically 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
RT   reference 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.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Lecharny A.;
RT   "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT   between quantitative expression, gene structure and evolution of a
RT   family 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
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
RP   PHENOTYPE, 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.,
RA   Keta S., Nakagawa A., Hayashi R., Saez-Vasquez J., Echeverria M.,
RA   Sugiyama M., Nakamura K., Machida C., Machida Y.;
RT   "A genetic link between epigenetic repressor AS1-AS2 and a putative
RT   small subunit processome in leaf polarity establishment of
RT   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,
CC       KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2,
CC       KNAT6, and STM to promote adaxial development in leaf primordia at
CC       shoot apical meristems at high temperatures. Involved in the
CC       processing of pre-rRNA intermediates at high temperatures.
CC       {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}.
CC       Nucleus, 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
CC       fourth leaves, fifth and sixth leaves, shoot apex, flower, flower
CC       bud, cauline leaf and rosette leaves.
CC       {ECO:0000269|PubMed:27334696}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- DISRUPTION PHENOTYPE: Plants are indistinguishable from that of
CC       wild-type at 16 degrees Celsius, however they generate a weak
CC       phenotype of pointed leaves at 22 degrees Celsius which become
CC       narrower at 26 degrees Celsius. In the leaves of plants grown at
CC       26 degrees Celsius, the xylems are located on the adaxial sides
CC       and the phloems are on the abaxial sides, similar to those in the
CC       wild type. Plants with double mutations in this protein and in AS2
CC       or AS1 protein have abaxialized filamentous and trumpet-like
CC       leaves with loss of the adaxial domain at high temperatures. In
CC       double mutants, shapes of epidermal cells of the filamentous
CC       leaves are simple and rectangular, similar to those of a petiole,
CC       but different from those of flat leaves of wild-type plants. The
CC       filamentous leaves of the double mutant at 26 degrees Celsius show
CC       primitive or no vascular tissue without apparent xylem cells
CC       inside the bundle sheath, suggesting defects in differentiation of
CC       xylem cells on the adaxial side. {ECO:0000269|PubMed:27334696}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
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   SMR; Q8GY84; -.
DR   STRING; 3702.AT5G60990.1; -.
DR   iPTMnet; Q8GY84; -.
DR   PaxDb; Q8GY84; -.
DR   PRIDE; Q8GY84; -.
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   eggNOG; ENOG410XQU7; LUCA.
DR   HOGENOM; HOG000268802; -.
DR   InParanoid; Q8GY84; -.
DR   KO; K14777; -.
DR   OMA; KAKNRSI; -.
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:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repressor;
KW   RNA-binding; rRNA processing; Stress response.
FT   CHAIN         1    456       DEAD-box ATP-dependent RNA helicase 10.
FT                                /FTId=PRO_0000239152.
FT   DOMAIN       40    223       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      250    394       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         9     37       Q motif.
FT   MOTIF       171    174       DEAD box.
FT   MUTAGEN     273    273       T->I: In rh10-1; temperature-sensitive
FT                                mutant. {ECO:0000269|PubMed:27334696}.
FT   CONFLICT    124    124       V -> F (in Ref. 5; AAM65614).
FT                                {ECO:0000305}.
FT   CONFLICT    194    194       L -> R (in Ref. 5; AAM65614).
FT                                {ECO:0000305}.
FT   CONFLICT    197    197       K -> E (in Ref. 3; BAC42444 and 4;
FT                                AAO63439). {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
//
DBGET integrated database retrieval system