RH14_ARATH
ID RH14_ARATH Reviewed; 619 AA.
AC Q8H136; O64430; Q8W4F5; Q93WJ3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 14;
DE EC=3.6.4.13;
GN Name=RH14; Synonyms=DRH1; OrderedLocusNames=At3g01540; ORFNames=F4P13.9;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9592148; DOI=10.1093/nar/26.11.2638;
RA Okanami M., Meshi T., Iwabuchi M.;
RT "Characterization of a DEAD box ATPase/RNA helicase protein of Arabidopsis
RT thaliana.";
RL Nucleic Acids Res. 26:2638-2643(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORMS 1 AND 2).
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 GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
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: ATP-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {ECO:0000250}.
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: Nucleus {ECO:0000269|PubMed:19245862}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H136-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H136-2; Sequence=VSP_019098;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in flowers and
CC roots. {ECO:0000269|PubMed:17168887, ECO:0000269|PubMed:9592148}.
CC -!- INDUCTION: Down-regulated by abscisic acid (ABA), salt and cold
CC treatments. {ECO:0000269|PubMed:9592148}.
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; AB010259; BAA28347.1; -; mRNA.
DR EMBL; AC009325; AAF01539.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73683.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73684.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73685.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73686.1; -; Genomic_DNA.
DR EMBL; AY062591; AAL32669.1; -; mRNA.
DR EMBL; AF428313; AAL16243.1; -; mRNA.
DR EMBL; AY050375; AAK91393.1; -; mRNA.
DR EMBL; BT000795; AAN31934.1; -; mRNA.
DR EMBL; BT009670; AAP78938.1; -; mRNA.
DR PIR; T52137; T52137.
DR RefSeq; NP_001030619.1; NM_001035542.1. [Q8H136-1]
DR RefSeq; NP_566141.1; NM_111020.3. [Q8H136-2]
DR RefSeq; NP_850492.1; NM_180161.2. [Q8H136-1]
DR RefSeq; NP_974206.1; NM_202477.2. [Q8H136-1]
DR AlphaFoldDB; Q8H136; -.
DR SMR; Q8H136; -.
DR BioGRID; 6449; 4.
DR IntAct; Q8H136; 1.
DR STRING; 3702.AT3G01540.2; -.
DR iPTMnet; Q8H136; -.
DR PaxDb; Q8H136; -.
DR PRIDE; Q8H136; -.
DR ProteomicsDB; 236909; -. [Q8H136-1]
DR EnsemblPlants; AT3G01540.1; AT3G01540.1; AT3G01540. [Q8H136-2]
DR EnsemblPlants; AT3G01540.2; AT3G01540.2; AT3G01540. [Q8H136-1]
DR EnsemblPlants; AT3G01540.3; AT3G01540.3; AT3G01540. [Q8H136-1]
DR EnsemblPlants; AT3G01540.4; AT3G01540.4; AT3G01540. [Q8H136-1]
DR GeneID; 821116; -.
DR Gramene; AT3G01540.1; AT3G01540.1; AT3G01540. [Q8H136-2]
DR Gramene; AT3G01540.2; AT3G01540.2; AT3G01540. [Q8H136-1]
DR Gramene; AT3G01540.3; AT3G01540.3; AT3G01540. [Q8H136-1]
DR Gramene; AT3G01540.4; AT3G01540.4; AT3G01540. [Q8H136-1]
DR KEGG; ath:AT3G01540; -.
DR Araport; AT3G01540; -.
DR TAIR; locus:2084178; AT3G01540.
DR eggNOG; KOG0331; Eukaryota.
DR InParanoid; Q8H136; -.
DR OMA; VPFTEQN; -.
DR OrthoDB; 638613at2759; -.
DR PhylomeDB; Q8H136; -.
DR PRO; PR:Q8H136; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H136; baseline and differential.
DR Genevisible; Q8H136; AT.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:TAIR.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR CDD; cd00201; WW; 1.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 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.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Helicase; Hydrolase;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..619
FT /note="DEAD-box ATP-dependent RNA helicase 14"
FT /id="PRO_0000239156"
FT DOMAIN 17..51
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 189..363
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 392..536
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 47..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 158..186
FT /note="Q motif"
FT MOTIF 311..314
FT /note="DEAD box"
FT COMPBIAS 47..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 575
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_019098"
FT CONFLICT 587
FT /note="R -> K (in Ref. 4; AAL32669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 67728 MW; 22B36764260AFFBE CRC64;
MAATAAASVV RYAPEDHTLP KPWKGLIDDR TGYLYFWNPE TNVTQYEKPT PSLPPKFSPA
VSVSSSVQVQ QTDAYAPPKD DDKYSRGSER VSRFSEGGRS GPPYSNGAAN GVGDSAYGAA
STRVPLPSSA PASELSPEAY SRRHEITVSG GQVPPPLMSF EATGFPPELL REVLSAGFSA
PTPIQAQSWP IAMQGRDIVA IAKTGSGKTL GYLIPGFLHL QRIRNDSRMG PTILVLSPTR
ELATQIQEEA VKFGRSSRIS CTCLYGGAPK GPQLRDLERG ADIVVATPGR LNDILEMRRI
SLRQISYLVL DEADRMLDMG FEPQIRKIVK EIPTKRQTLM YTATWPKGVR KIAADLLVNP
AQVNIGNVDE LVANKSITQH IEVVAPMEKQ RRLEQILRSQ EPGSKVIIFC STKRMCDQLT
RNLTRQFGAA AIHGDKSQPE RDNVLNQFRS GRTPVLVATD VAARGLDVKD IRAVVNYDFP
NGVEDYVHRI GRTGRAGATG QAFTFFGDQD SKHASDLIKI LEGANQRVPP QIREMATRGG
GGMNKFSRWG PPSGGRGRGG DSGYGGRGSF ASRDSRSSNG WGRERERSRS PERFNRAPPP
SSTGSPPRSF HETMMMKHR
