RH47_ARATH
ID RH47_ARATH Reviewed; 551 AA.
AC Q8W4E1; Q0WLV2; Q9LN70; Q9LPX3;
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 47, mitochondrial;
DE EC=3.6.4.13;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1586;
DE AltName: Full=Protein INCREASED SIZE EXCLUSION LIMIT 1;
DE Flags: Precursor;
GN Name=RH47; Synonyms=EMB1586, ISE1; OrderedLocusNames=At1g12770;
GN ORFNames=F13K23.1, T12C24.30;
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=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 [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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11779812; DOI=10.1093/genetics/159.4.1751;
RA McElver J., Tzafrir I., Aux G., Rogers R., Ashby C., Smith K., Thomas C.,
RA Schetter A., Zhou Q., Cushman M.A., Tossberg J., Nickle T., Levin J.Z.,
RA Law M., Meinke D., Patton D.;
RT "Insertional mutagenesis of genes required for seed development in
RT Arabidopsis thaliana.";
RL Genetics 159:1751-1763(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11874921; DOI=10.1242/dev.129.5.1261;
RA Kim I., Hempel F.D., Sha K., Pfluger J., Zambryski P.C.;
RT "Identification of a developmental transition in plasmodesmatal function
RT during embryogenesis in Arabidopsis thaliana.";
RL Development 129:1261-1272(2002).
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 FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-228, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19805190; DOI=10.1073/pnas.0909229106;
RA Stonebloom S., Burch-Smith T., Kim I., Meinke D., Mindrinos M.,
RA Zambryski P.;
RT "Loss of the plant DEAD-box protein ISE1 leads to defective mitochondria
RT and increased cell-to-cell transport via plasmodesmata.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17229-17234(2009).
RN [9]
RP REVIEW.
RX PubMed=20541498; DOI=10.1016/j.cub.2010.03.047;
RA Lee D.K., Sieburth L.E.;
RT "Plasmodesmata formation: poking holes in walls with ise.";
RL Curr. Biol. 20:R488-R490(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20434343; DOI=10.1016/j.cub.2010.03.064;
RA Burch-Smith T.-M., Zambryski P.C.;
RT "Loss of INCREASED SIZE EXCLUSION LIMIT (ISE)1 or ISE2 increases the
RT formation of secondary plasmodesmata.";
RL Curr. Biol. 20:989-993(2010).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=22106293; DOI=10.1073/pnas.1117226108;
RA Burch-Smith T.M., Brunkard J.O., Choi Y.G., Zambryski P.C.;
RT "Organelle-nucleus cross-talk regulates plant intercellular communication
RT via plasmodesmata.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E1451-E1460(2011).
RN [12]
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).
CC -!- FUNCTION: Essential protein required during embryogenesis. Required for
CC mitochondrial metabolism. Necessary for normal plasmodesmata (PD)
CC development and aperture regulation. {ECO:0000269|PubMed:11779812,
CC ECO:0000269|PubMed:11874921, ECO:0000269|PubMed:19805190,
CC ECO:0000269|PubMed:20434343}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19805190}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and, to a
CC lower extent, in roots, seedlings and siliques, especially in
CC meristematic regions. {ECO:0000269|PubMed:19805190}.
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: Embryogenesis mostly arrested at globular stage
CC and cotyledon stage. Altered size exclusion limit of PD; abnormally
CC maintained dilated PD at the torpedo stage and increased formation of
CC secondary branched PD. Chlorosis (PubMed:11779812, PubMed:11874921,
CC PubMed:19805190, PubMed:20434343). Altered plastid development
CC (PubMed:22106293). {ECO:0000269|PubMed:11779812,
CC ECO:0000269|PubMed:11874921, ECO:0000269|PubMed:19805190,
CC ECO:0000269|PubMed:20434343, ECO:0000269|PubMed:22106293}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AC012187; AAF78481.1; -; Genomic_DNA.
DR EMBL; AC025417; AAF88089.2; -; Genomic_DNA.
DR EMBL; CP002684; AEE28926.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60164.1; -; Genomic_DNA.
DR EMBL; AY062618; AAL32696.1; -; mRNA.
DR EMBL; AY114691; AAM48010.1; -; mRNA.
DR EMBL; AK175587; BAD43350.1; -; mRNA.
DR EMBL; AK175711; BAD43474.1; -; mRNA.
DR EMBL; AK175751; BAD43514.1; -; mRNA.
DR EMBL; AK175793; BAD43556.1; -; mRNA.
DR EMBL; AK176044; BAD43807.1; -; mRNA.
DR EMBL; AK176194; BAD43957.1; -; mRNA.
DR EMBL; AK226229; BAE98393.1; -; mRNA.
DR EMBL; AK229878; BAF01707.1; -; mRNA.
DR EMBL; AK230085; BAF01905.1; -; mRNA.
DR PIR; H86260; H86260.
DR RefSeq; NP_001322468.1; NM_001332052.1.
DR RefSeq; NP_172737.2; NM_101147.3.
DR AlphaFoldDB; Q8W4E1; -.
DR SMR; Q8W4E1; -.
DR STRING; 3702.AT1G12770.1; -.
DR PaxDb; Q8W4E1; -.
DR PRIDE; Q8W4E1; -.
DR ProteomicsDB; 236247; -.
DR EnsemblPlants; AT1G12770.1; AT1G12770.1; AT1G12770.
DR EnsemblPlants; AT1G12770.2; AT1G12770.2; AT1G12770.
DR GeneID; 837833; -.
DR Gramene; AT1G12770.1; AT1G12770.1; AT1G12770.
DR Gramene; AT1G12770.2; AT1G12770.2; AT1G12770.
DR KEGG; ath:AT1G12770; -.
DR Araport; AT1G12770; -.
DR TAIR; locus:2010306; AT1G12770.
DR eggNOG; KOG0327; Eukaryota.
DR HOGENOM; CLU_003041_1_3_1; -.
DR InParanoid; Q8W4E1; -.
DR OMA; CVTKLQH; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q8W4E1; -.
DR PRO; PR:Q8W4E1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4E1; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0009663; P:plasmodesma organization; IMP:TAIR.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 2.
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; 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; 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; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..551
FT /note="DEAD-box ATP-dependent RNA helicase 47,
FT mitochondrial"
FT /id="PRO_0000239187"
FT DOMAIN 141..340
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 397..548
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 110..138
FT /note="Q motif"
FT MOTIF 274..277
FT /note="DEAD box"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 228
FT /note="G->E: In ise1-1; increased PD-mediated transport,
FT with higher frequency of branched and twinned PD, and
FT impaired mitochondrial metabolism accompanied by a
FT disrupted mitochondrial proton gradient and an increased
FT production of reactive oxygen species."
FT /evidence="ECO:0000269|PubMed:19805190"
FT CONFLICT 238
FT /note="A -> P (in Ref. 3; AAL32696/AAM48010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 60718 MW; 4301AB0F877EEFD8 CRC64;
MAASTSTRFL VLLKDFSAFR KISWTCAATN FHRQSRFLCH VAKEDGSLTL ASLDLGNKPR
KFGKGKAMKL EGSFVTEMGQ GKVRAVKNDK MKVVKEKKPA EIVSPLFSAK SFEELGLPDS
LLDSLEREGF SVPTDVQSAA VPAIIKGHDA VIQSYTGSGK TLAYLLPILS EIGPLAEKSR
SSHSENDKRT EIQAMIVAPS RELGMQIVRE VEKLLGPVHR RMVQQLVGGA NRMRQEEALK
KNKPAIVVGT PGRIAEISKG GKLHTHGCRF LVLDEVDELL SFNFREDIHR ILEHVGKRSG
AGPKGEVDER ANRQTILVSA TVPFSVIRAA KSWSHEPVLV QANKVTPLDT VQPSAPVMSL
TPTTSEADGQ IQTTIQSLPP ALKHYYCISK HQHKVDTLRR CVHALDAQSV IAFMNHSRQL
KDVVYKLEAR GMNSAEMHGD LGKLGRSTVL KKFKNGEIKV LVTNELSARG LDVAECDLVV
NLELPTDAVH YAHRAGRTGR LGRKGTVVTV CEESQVFIVK KMEKQLGLPF LYCEFVDGEL
VVTEEDKAII R
