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THOC3_ARATH
ID   THOC3_ARATH             Reviewed;         315 AA.
AC   Q9FKT5;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=THO complex subunit 3;
DE   AltName: Full=TEX1 homolog;
DE            Short=AtTEX1;
GN   Name=THO3; Synonyms=TEX1; OrderedLocusNames=At5g56130; ORFNames=MDA7.19;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(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   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND MUTAGENESIS OF
RP   SER-86.
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. 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).
CC       {ECO:0000269|PubMed:20634427, ECO:0000269|PubMed:20798330}.
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:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Developmental defects as well as reduced levels
CC       of endogenous trans-acting small interfering RNA (ta-siRNA).
CC       {ECO:0000269|PubMed:20798330}.
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DR   EMBL; AB011476; BAB09295.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96724.1; -; Genomic_DNA.
DR   EMBL; AY093120; AAM13119.1; -; mRNA.
DR   EMBL; BT000174; AAN15493.1; -; mRNA.
DR   RefSeq; NP_200424.1; NM_124995.5.
DR   AlphaFoldDB; Q9FKT5; -.
DR   SMR; Q9FKT5; -.
DR   BioGRID; 20956; 61.
DR   STRING; 3702.AT5G56130.1; -.
DR   PaxDb; Q9FKT5; -.
DR   PRIDE; Q9FKT5; -.
DR   ProteomicsDB; 246464; -.
DR   EnsemblPlants; AT5G56130.1; AT5G56130.1; AT5G56130.
DR   GeneID; 835712; -.
DR   Gramene; AT5G56130.1; AT5G56130.1; AT5G56130.
DR   KEGG; ath:AT5G56130; -.
DR   Araport; AT5G56130; -.
DR   TAIR; locus:2161840; AT5G56130.
DR   eggNOG; KOG1407; Eukaryota.
DR   HOGENOM; CLU_045202_0_0_1; -.
DR   InParanoid; Q9FKT5; -.
DR   OMA; YWLAYST; -.
DR   OrthoDB; 1014314at2759; -.
DR   PhylomeDB; Q9FKT5; -.
DR   PRO; PR:Q9FKT5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FKT5; baseline and differential.
DR   Genevisible; Q9FKT5; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS: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:0031047; P:gene silencing by RNA; IMP:TAIR.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR040132; Tex1/THOC3.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR22839; PTHR22839; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW   Transport; WD repeat.
FT   CHAIN           1..315
FT                   /note="THO complex subunit 3"
FT                   /id="PRO_0000425584"
FT   REPEAT          18..57
FT                   /note="WD 1"
FT   REPEAT          64..104
FT                   /note="WD 2"
FT   REPEAT          106..145
FT                   /note="WD 3"
FT   REPEAT          189..228
FT                   /note="WD 4"
FT   REPEAT          231..270
FT                   /note="WD 5"
FT   REPEAT          272..311
FT                   /note="WD 6"
FT   MUTAGEN         86
FT                   /note="S->F: In attex1-2; reduced levels of endogenous
FT                   trans-acting small interfering RNA (ta-siRNA)."
FT                   /evidence="ECO:0000269|PubMed:20634427"
SQ   SEQUENCE   315 AA;  35375 MW;  9935657E83ACD62B CRC64;
     MEETTIPFKS LHSREYQGHK KKVHSVAWNS NGTKLASGSV DQTARIWNIE PHGHSKAKDL
     ELKGHTDSVD QLCWDPKHSD LVATASGDKS VRLWDARSGK CTQQVELSGE NINITYKPDG
     THVAVGNRDD ELTILDVRKF KPLHRRKFNY EVNEIAWNMP GDFFFLTTGL GTVEVLSYPS
     LKPLDTLTAH TAGCYCIAID PKGRYFAVGS ADSLVSLWDI SDMLCLRTFT KLEWPVRTIS
     FNYSGEYIAS ASEDLFIDIA NVQTGRTVHQ IPCRAAMNSV EWNPKYNLLA YAGDDKNPKY
     NTDEGVFRIF GFESS
 
 
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