RDO2_ARATH
ID RDO2_ARATH Reviewed; 378 AA.
AC Q9ZVH8; Q8VXZ6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcription elongation factor TFIIS {ECO:0000305};
DE AltName: Full=Protein REDUCED DORMANCY 2 {ECO:0000303|PubMed:21799800};
GN Name=TFIIS {ECO:0000303|PubMed:19150360};
GN Synonyms=RDO2 {ECO:0000303|PubMed:21799800};
GN OrderedLocusNames=At2g38560 {ECO:0000312|Araport:AT2G38560};
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19150360; DOI=10.1016/j.jmb.2008.12.066;
RA Grasser M., Kane C.M., Merkle T., Melzer M., Emmersen J., Grasser K.D.;
RT "Transcript elongation factor TFIIS is involved in arabidopsis seed
RT dormancy.";
RL J. Mol. Biol. 386:598-611(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21799800; DOI=10.1371/journal.pone.0022241;
RA Liu Y., Geyer R., van Zanten M., Carles A., Li Y., Horold A.,
RA van Nocker S., Soppe W.J.;
RT "Identification of the Arabidopsis REDUCED DORMANCY 2 gene uncovers a role
RT for the polymerase associated factor 1 complex in seed dormancy.";
RL PLoS ONE 6:E22241-E22241(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
CC -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC elongation past template-encoded arresting sites (Probable). Involved
CC in the control of seed dormancy and germination (PubMed:19150360,
CC PubMed:21799800). {ECO:0000269|PubMed:19150360,
CC ECO:0000269|PubMed:21799800, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC ECO:0000269|PubMed:19150360}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:19150360}.
CC -!- DISRUPTION PHENOTYPE: Reduced seed dormancy and increased germination
CC rate of freshly harvested seeds (PubMed:19150360, PubMed:21799800).
CC Early flowering (PubMed:19150360). {ECO:0000269|PubMed:19150360,
CC ECO:0000269|PubMed:21799800}.
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DR EMBL; AC005499; AAC67362.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09550.1; -; Genomic_DNA.
DR EMBL; AK117557; BAC42218.1; -; mRNA.
DR EMBL; AY074322; AAL67018.1; -; mRNA.
DR EMBL; AY150517; AAN13033.1; -; mRNA.
DR PIR; E84806; E84806.
DR RefSeq; NP_181390.1; NM_129413.4.
DR AlphaFoldDB; Q9ZVH8; -.
DR SMR; Q9ZVH8; -.
DR IntAct; Q9ZVH8; 1.
DR STRING; 3702.AT2G38560.1; -.
DR iPTMnet; Q9ZVH8; -.
DR PaxDb; Q9ZVH8; -.
DR PRIDE; Q9ZVH8; -.
DR ProteomicsDB; 235054; -.
DR EnsemblPlants; AT2G38560.1; AT2G38560.1; AT2G38560.
DR GeneID; 818438; -.
DR Gramene; AT2G38560.1; AT2G38560.1; AT2G38560.
DR KEGG; ath:AT2G38560; -.
DR Araport; AT2G38560; -.
DR TAIR; locus:2064195; AT2G38560.
DR eggNOG; KOG1105; Eukaryota.
DR HOGENOM; CLU_037637_0_0_1; -.
DR InParanoid; Q9ZVH8; -.
DR OMA; KMVTRKS; -.
DR OrthoDB; 1579101at2759; -.
DR PhylomeDB; Q9ZVH8; -.
DR PRO; PR:Q9ZVH8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVH8; baseline and differential.
DR Genevisible; Q9ZVH8; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IMP:TAIR.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035100; TF_IIS-typ.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR006289; TFSII.
DR InterPro; IPR001222; Znf_TFIIS.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR PIRSF; PIRSF006704; TF_IIS; 1.
DR SMART; SM00510; TFS2M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR TIGRFAMs; TIGR01385; TFSII; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Elongation factor; Metal-binding; Nucleus;
KW Protein biosynthesis; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..378
FT /note="Transcription elongation factor TFIIS"
FT /id="PRO_0000432766"
FT DOMAIN 10..89
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 210..333
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 336..376
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 219
FT /note="V -> M (in Ref. 4; AAL67018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 41979 MW; 9A176DC31FA8E885 CRC64;
MESDLIDLFE GAKKAADAAA LDGVTSSGPE VSQCIDALKQ LKKFPVTYDT LVATQVGKKL
RSLAKHPVED IKSVATDLLE IWKKVVIEET AKAKKTEGTN GCKEAKVNKM DVEKPSNPAP
VKVQKLQRGD SAKSIKVERK EPDNKVVTGV KIERKVPDIK VTNGTKIDYR GQAVKDEKVS
KDNQSSMKAP AKAANAPPKL TAMLKCNDPV RDKIRELLVE ALCRVAGEAD DYERESVNAS
DPLRVAVSVE SLMFEKLGRS TGAQKLKYRS IMFNLRDSNN PDLRRRVLTG EISPEKLITL
SAEDMASDKR KQENNQIKEK ALFDCERGLA AKASTDQFKC GRCGQRKCTY YQMQTRSADE
PMTTYVTCVN CDNHWKFC
