THOC1_ARATH
ID THOC1_ARATH Reviewed; 599 AA.
AC Q93VM9; Q8H134; Q9FIC0;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=THO complex subunit 1;
DE Short=AtTHO1;
DE AltName: Full=HPR1 homolog;
DE Short=AtHPR1;
GN Name=THO1; Synonyms=EMU, HPR1; OrderedLocusNames=At5g09860;
GN ORFNames=MYH9.7;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20798330; DOI=10.1105/tpc.110.076638;
RA Jauvion V., Elmayan T., Vaucheret H.;
RT "The conserved RNA trafficking proteins HPR1 and TEX1 are involved in the
RT production of endogenous and exogenous small interfering RNA in
RT Arabidopsis.";
RL Plant Cell 22:2697-2709(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=20634427; DOI=10.1073/pnas.0911341107;
RA Yelina N.E., Smith L.M., Jones A.M., Patel K., Kelly K.A., Baulcombe D.C.;
RT "Putative Arabidopsis THO/TREX mRNA export complex is involved in transgene
RT and endogenous siRNA biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13948-13953(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20668032; DOI=10.1261/rna.2265710;
RA Furumizu C., Tsukaya H., Komeda Y.;
RT "Characterization of EMU, the Arabidopsis homolog of the yeast THO complex
RT member HPR1.";
RL RNA 16:1809-1817(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22035198; DOI=10.1111/j.1365-313x.2011.04835.x;
RA Pan H., Liu S., Tang D.;
RT "HPR1, a component of the THO/TREX complex, plays an important role in
RT disease resistance and senescence in Arabidopsis.";
RL Plant J. 69:831-843(2012).
CC -!- FUNCTION: Acts as component of the THO subcomplex of the TREX complex
CC which is thought to couple mRNA transcription, processing and nuclear
CC export. Contributes to the integrity of the endogenous trans-acting
CC small interfering RNA (ta-siRNA) pathway. May process or transport a
CC long RNA molecule so that it can be a template for secondary siRNA
CC production. May participate in the trafficking of siRNA precursors to
CC the ARGONAUTE catalytic center. Required for the generation of
CC functional messenger ribonucleoproteins (mRNPs). Plays an important
CC roles in plant innate immunity. {ECO:0000269|PubMed:20668032,
CC ECO:0000269|PubMed:20798330, ECO:0000269|PubMed:22035198}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of THO1, THO2,
CC THO3, THO5, THO6 and THO7. {ECO:0000269|PubMed:20634427}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22035198}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q93VM9-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Developmental defects as well as reduced levels
CC of endogenous trans-acting small interfering RNA (ta-siRNA).
CC {ECO:0000269|PubMed:20668032, ECO:0000269|PubMed:20798330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016893; BAB09407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91456.1; -; Genomic_DNA.
DR EMBL; AF424566; AAL11560.1; -; mRNA.
DR EMBL; AF428323; AAL16253.1; -; mRNA.
DR EMBL; BT000829; AAN33204.1; -; mRNA.
DR RefSeq; NP_568219.1; NM_121023.4. [Q93VM9-1]
DR AlphaFoldDB; Q93VM9; -.
DR BioGRID; 16124; 100.
DR STRING; 3702.AT5G09860.1; -.
DR iPTMnet; Q93VM9; -.
DR PaxDb; Q93VM9; -.
DR PRIDE; Q93VM9; -.
DR ProteomicsDB; 234351; -. [Q93VM9-1]
DR EnsemblPlants; AT5G09860.1; AT5G09860.1; AT5G09860. [Q93VM9-1]
DR GeneID; 830846; -.
DR Gramene; AT5G09860.1; AT5G09860.1; AT5G09860. [Q93VM9-1]
DR KEGG; ath:AT5G09860; -.
DR Araport; AT5G09860; -.
DR TAIR; locus:2178183; AT5G09860.
DR eggNOG; KOG2491; Eukaryota.
DR HOGENOM; CLU_027906_1_1_1; -.
DR InParanoid; Q93VM9; -.
DR OMA; TQGHIPR; -.
DR OrthoDB; 403879at2759; -.
DR PhylomeDB; Q93VM9; -.
DR PRO; PR:Q93VM9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93VM9; baseline and differential.
DR Genevisible; Q93VM9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IGI:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR InterPro; IPR021861; THO_THOC1.
DR PANTHER; PTHR13265; PTHR13265; 1.
DR Pfam; PF11957; efThoc1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; mRNA transport;
KW Nucleus; Plant defense; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transport.
FT CHAIN 1..599
FT /note="THO complex subunit 1"
FT /id="PRO_0000425582"
FT REGION 376..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 372
FT /note="C -> Y (in Ref. 3; AAN33204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 68334 MW; 9B5FA02175D4F68D CRC64;
MDAFRDAILQ RAPIETFALK TVQHFIQPQK QTKLAQDENQ MLENMLRTLL QELVAAAAQS
GEQIMQYGQL IDDDDDDDDI HGQIPHLLDV VLYLCEKEHV EGGMIFQLLE DLTEMSTMKN
CKDVFGYIES KQDILGKQEL FARGKLVMLR TCNQLLRRLS KANDVVFCGR ILMFLAHFFP
LSERSAVNIK GVFNTSNETK YEKDPPKGIS VDFNFYKTFW SLQEYFCNPA SLTSASTKWQ
KFSSSLAVVL NTFDAQPLSE EEGEANSLEE EAATFNIKYL TSSKLMGLEL KDSSFRRHIL
LQCLIMFDYL RAPGKNDKDL PSETMKEELK SCEDRVKKLL EITPPKGKEF LRAVEHILER
EKNWVWWKRD GCPPFEKQPI DKKSPNAGQK KRRQRWRLGN KELSQLWRWA DQNPNALTDS
QRVRTPDIAD YWKPLAEDMD PSAGIEDEYH HKNNRVYCWK GLRFTARQDL EGFSRFTEMG
IEGVVPVELL PPEVRSKYQA KPNEKAKRAK KEETKGGSHE TEGNQIGVSN SEAEAEGGRG
DAETMESDAI ADTPTPEEQQ RLGGSDTENG QEAGQIEDGE TEEAGLMDTD LDHPPMPVS
