HEN2_ARATH
ID HEN2_ARATH Reviewed; 995 AA.
AC Q9ZVW2; Q941F4;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH10 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=Protein HUA ENHANCER 2 {ECO:0000303|PubMed:11923195};
GN Name=HEN2 {ECO:0000303|PubMed:11923195};
GN OrderedLocusNames=At2g06990 {ECO:0000312|Araport:AT2G06990};
GN ORFNames=T4E14.10 {ECO:0000312|EMBL:AAC67203.2};
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], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11923195; DOI=10.1242/dev.129.7.1569;
RA Western T.L., Cheng Y., Liu J., Chen X.;
RT "HUA ENHANCER2, a putative DExH-box RNA helicase, maintains homeotic B and
RT C gene expression in Arabidopsis.";
RL Development 129:1569-1581(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 REVIEW.
RX PubMed=12119159; DOI=10.1016/s1360-1385(02)02294-x;
RA Jack T.;
RT "New members of the floral organ identity AGAMOUS pathway.";
RL Trends Plant Sci. 7:286-287(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND ASSOCIATION WITH
RP THE RNA EXOSOME COMPLEX.
RX PubMed=25144737; DOI=10.1371/journal.pgen.1004564;
RA Lange H., Zuber H., Sement F.M., Chicher J., Kuhn L., Hammann P.,
RA Brunaud V., Berard C., Bouteiller N., Balzergue S., Aubourg S.,
RA Martin-Magniette M.L., Vaucheret H., Gagliardi D.;
RT "The RNA helicases AtMTR4 and HEN2 target specific subsets of nuclear
RT transcripts for degradation by the nuclear exosome in Arabidopsis
RT thaliana.";
RL PLoS Genet. 10:E1004564-E1004564(2014).
CC -!- FUNCTION: ATP-dependent RNA helicase that associates with the RNA
CC exosome complex, with the cap binding complex (CBC) and with the NEXT-
CC like complex. Involved in the degradation of a large number of non-
CC coding nuclear exosome substrates such as snoRNA and miRNA precursors,
CC incompletely spliced mRNAs, and spurious transcripts produced from
CC pseudogenes and intergenic regions (PubMed:25144737). Involved in the
CC maintenance of homeotic B and C gene expression in the reproductive
CC whorls. Regulates floral organ spacing and identity, probably through
CC the regulation of protein synthesis or mRNA degradation
CC (PubMed:11923195). {ECO:0000269|PubMed:11923195,
CC ECO:0000269|PubMed:25144737}.
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, nucleoplasm
CC {ECO:0000269|PubMed:25144737}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, leaves, stems, and
CC roots. {ECO:0000269|PubMed:11923195}.
CC -!- DEVELOPMENTAL STAGE: Expressed in specific patterns in the
CC inflorescence meristem and developing flowers. Present throughout the
CC inflorescence meristem and in young floral meristems through stage 4.
CC Around stage 5, present within the developing organs of the inner three
CC whorls but absent from sepals. At later stage of floral development,
CC present at a low level in the gynoecium but accumulate strongly in
CC developing ovules. {ECO:0000269|PubMed:11923195}.
CC -!- DISRUPTION PHENOTYPE: When combined with mutations in HUA1 and HUA2,
CC reduced stem elongation and alterations in production of flowers along
CC the inflorescence. These flowers are characterized by the presence of
CC third whorl sepal-petal-stamens and fourth whorl sepal-carpels leading
CC to abnormal floral organ number and positioning. Over-accumulation of
CC non-coding nuclear exososome targets (PubMed:25144737).
CC {ECO:0000269|PubMed:11923195, ECO:0000269|PubMed:25144737}.
CC -!- SIMILARITY: Belongs to the DExH box helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL11446.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AY050658; AAL11446.1; ALT_INIT; mRNA.
DR EMBL; AC005171; AAC67203.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06028.1; -; Genomic_DNA.
DR EMBL; BT005794; AAO64196.1; -; mRNA.
DR PIR; B84481; B84481.
DR RefSeq; NP_565338.1; NM_126675.3.
DR AlphaFoldDB; Q9ZVW2; -.
DR SMR; Q9ZVW2; -.
DR IntAct; Q9ZVW2; 1.
DR STRING; 3702.AT2G06990.1; -.
DR iPTMnet; Q9ZVW2; -.
DR PaxDb; Q9ZVW2; -.
DR PRIDE; Q9ZVW2; -.
DR ProteomicsDB; 230377; -.
DR EnsemblPlants; AT2G06990.1; AT2G06990.1; AT2G06990.
DR GeneID; 815269; -.
DR Gramene; AT2G06990.1; AT2G06990.1; AT2G06990.
DR KEGG; ath:AT2G06990; -.
DR Araport; AT2G06990; -.
DR TAIR; locus:2063648; AT2G06990.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR InParanoid; Q9ZVW2; -.
DR OMA; CEIDTAD; -.
DR OrthoDB; 176060at2759; -.
DR PhylomeDB; Q9ZVW2; -.
DR PRO; PR:Q9ZVW2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVW2; baseline and differential.
DR Genevisible; Q9ZVW2; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
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; ISS:TAIR.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0060149; P:negative regulation of post-transcriptional gene silencing; IMP:TAIR.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0016070; P:RNA metabolic process; TAS:TAIR.
DR GO; GO:0010093; P:specification of floral organ identity; 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; IPR025696; rRNA_proc-arch_dom.
DR InterPro; IPR016438; Ski2-like.
DR InterPro; IPR012961; Ski2_C.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; rRNA_proc-arch; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Developmental protein; Flowering; Helicase;
KW Hydrolase; mRNA processing; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..995
FT /note="DExH-box ATP-dependent RNA helicase DExH10"
FT /id="PRO_0000432897"
FT DOMAIN 90..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 323..524
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 194..197
FT /note="DEIH box"
FT /evidence="ECO:0000305"
FT COMPBIAS 8..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 995 AA; 111889 MW; BC9F348BD27F4131 CRC64;
MSAQMEEPET LGKRKESESS KLRSDETPTP EPRTKRRSLK RACVHEVAVP NDYTPTKEET
IHGTLDNPVF NGDMAKTYPF KLDPFQSVSV ACLERKESIL VSAHTSAGKT AVAEYAIAMA
FRDKQRVIYT SPLKALSNQK YRELQHEFKD VGLMTGDVTL SPNASCLVMT TEILRAMLYR
GSEVLKEVAW VIFDEIHYMK DRERGVVWEE SIIFLPPAIK MVFLSATMSN ATEFAEWICY
LHKQPCHVVY TDFRPTPLQH YAFPMGGGGL YLVVDDNEQF REDSFVKMQD TFPKPKSNDG
KKSANGKSGG RGAKGGGGPG DSDVYKIVKM IMERKFEPVI IFSFSRRECE QHALSMSKLD
FNTDEEKEVV EQVFNNAMQC LNEEDRSLPA IELMLPLLQR GIAVHHSGLL PVIKELVELL
FQEGLVKALF ATETFAMGLN MPAKTVVFTA VKKWDGDSHR YIGSGEYIQM SGRAGRRGKD
ERGICIIMID EQMEMNTLRD MMLGKPAPLL STFRLSYYTI LNLLSRAEGQ FTAEHVIRHS
FHQFQHEKAL PDIGNKVSKL EEEAAILNAS GEAEVAEYHN LQFDIAKHEK KLMSEIIRPE
RVLCFLDTGR LVKIREGGTD WGWGVVVNVV KNSSVGTGSA SSHGGGYIVD TLLHCSTGFS
ENGAKPKPCP PRAGEKGEMH VVPVQLPLIS ALSRLRISVP SDLRPVEARQ SILLALQELS
SRFPLGFPKL HPVKDMNIQD TEIVDLVSQI EEVEQKLLAH PMHKSEDDQQ IKSFQRKAEV
NYEIQQLKSK MRDSQLQKFR DELKNRSRVL KKLGHIDADG VVQVKGRAAC LIDTGDELLV
TELMFNGTFN DLDHHQVAAL ASCFIPVDKS NEQVNLRNEL TKPLQQLQDS ARKIAEIQHE
CKLEIDVEEY VESTIRPFLM DVIYSWSKGA SFAEIIQMTD IFEGSIIRSA RRLDEFLNQL
RAAAEAVGES SLESKFAAAS ESLRRGIMFA NSLYL
