THOC6_ARATH
ID THOC6_ARATH Reviewed; 367 AA.
AC Q8L4M1; O64576;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=THO complex subunit 6;
DE Short=AtTHO6;
DE AltName: Full=Protein DWD HYPERSENSITIVE TO ABA 1;
DE AltName: Full=WD repeat-containing protein DWA1;
GN Name=THO6; Synonyms=DWA1, THOC6; OrderedLocusNames=At2g19430;
GN ORFNames=F27F23.25;
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=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 [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, COMPONENT OF THE CUL4-RBX1-DDB1-DWA1 COMPLEX, INTERACTION WITH
RP ABI5; DDB1A AND DWA2, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20525848; DOI=10.1105/tpc.109.073783;
RA Lee J.H., Yoon H.J., Terzaghi W., Martinez C., Dai M., Li J., Byun M.O.,
RA Deng X.W.;
RT "DWA1 and DWA2, two Arabidopsis DWD protein components of CUL4-based E3
RT ligases, act together as negative regulators in aba signal transduction.";
RL Plant Cell 22:1716-1732(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).
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. {ECO:0000250}.
CC -!- FUNCTION: Component of the CUL4-RBX1-DDB1-DWA1/DWA2 E3 ubiquitin-
CC protein ligase complex that acts as negative regulator in abscisic acid
CC (ABA) signaling. May function as the substrate recognition module
CC within this complex leading to ABI5 degradation. Functionally redundant
CC with DWA2. {ECO:0000269|PubMed:20525848}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the THO complex, which is composed of THO1, THO2,
CC THO3, THO5, THO6 and THO7. Interacts with ABI5, DDB1A and DWA2.
CC {ECO:0000269|PubMed:20525848, ECO:0000269|PubMed:20634427}.
CC -!- INTERACTION:
CC Q8L4M1; Q9M0V3: DDB1A; NbExp=2; IntAct=EBI-941035, EBI-1632780;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20525848}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to abscisic acid (ABA) and
CC salt. {ECO:0000269|PubMed:20525848}.
CC -!- SIMILARITY: Belongs to the WD repeat THOC6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10142.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM14874.1; Type=Erroneous gene model prediction; 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; AC003058; AAM14874.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005917; AAD10142.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06880.1; -; Genomic_DNA.
DR EMBL; AY099718; AAM20569.1; -; mRNA.
DR EMBL; AY128879; AAM91279.1; -; mRNA.
DR PIR; T01291; T01291.
DR RefSeq; NP_849989.1; NM_179658.4.
DR AlphaFoldDB; Q8L4M1; -.
DR SMR; Q8L4M1; -.
DR BioGRID; 1817; 22.
DR IntAct; Q8L4M1; 6.
DR STRING; 3702.AT2G19430.1; -.
DR PaxDb; Q8L4M1; -.
DR PRIDE; Q8L4M1; -.
DR ProteomicsDB; 234370; -.
DR EnsemblPlants; AT2G19430.1; AT2G19430.1; AT2G19430.
DR GeneID; 816462; -.
DR Gramene; AT2G19430.1; AT2G19430.1; AT2G19430.
DR KEGG; ath:AT2G19430; -.
DR Araport; AT2G19430; -.
DR TAIR; locus:2047635; AT2G19430.
DR eggNOG; KOG0649; Eukaryota.
DR HOGENOM; CLU_060667_0_0_1; -.
DR InParanoid; Q8L4M1; -.
DR OMA; HLRSMEC; -.
DR OrthoDB; 760323at2759; -.
DR PhylomeDB; Q8L4M1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L4M1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L4M1; baseline and differential.
DR Genevisible; Q8L4M1; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR042626; THOC6.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44411; PTHR44411; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Transport; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..367
FT /note="THO complex subunit 6"
FT /id="PRO_0000396857"
FT REPEAT 23..67
FT /note="WD 1"
FT REPEAT 88..129
FT /note="WD 2"
FT REPEAT 157..196
FT /note="WD 3"
FT REPEAT 199..240
FT /note="WD 4"
FT REPEAT 243..283
FT /note="WD 5"
FT REPEAT 285..322
FT /note="WD 6"
FT REPEAT 324..363
FT /note="WD 7"
SQ SEQUENCE 367 AA; 40073 MW; 688A76897C323589 CRC64;
MYGDATNWNE DEYRESILKE REIETRTVFR TAWAPPARIS NPDAFVVASS DGTLAFHSLN
SLVSQSASFG YSKGQDVMVA EPERVVRAHE GPAYDVKFYG EDEDALLLSC GDDGRVRGWK
WREFAESDVS LHLKENHLKP LLELINPQHK GPWGALSPMP EINAMSVDPQ SGSVFTAAGD
SCAYCWDVES GKIKMTFKGH SDYLHTVVSR SSASQILTGS EDGTARIWDC KTGKCVKVIG
SQDKKSRLRV SSMALDGSES WLVCGQGKNL ALWNLPASEC VQTIPIPAHV QDVMFDEKQI
LTVGAEPLLR RFDLNGALLS QIHCAPCSVF SISLHPAGVV AVGGYGGIVD VISQFGSHLC
TFRSSSL
