TRB3_ARATH
ID TRB3_ARATH Reviewed; 295 AA.
AC Q9M2X3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 171.
DE RecName: Full=Telomere repeat-binding factor 3;
DE Short=AtTRB3;
DE AltName: Full=MYB transcription factor;
DE AltName: Full=Telomere-binding protein 2;
DE Short=AtTBP2;
GN Name=TRB3; Synonyms=TBP2; OrderedLocusNames=At3g49850; ORFNames=T16K5.200;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RA Sprenger M., Weisshaar B.;
RT "Identification and functional characterisation of the Arabidopsis telomere
RT repeat binding factor TRB3.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Qu L.-J., Gu H.;
RT "The MYB transcription factor family in Arabidopsis: a genome-wide cloning
RT and expression pattern analysis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [6]
RP GENE FAMILY.
RX PubMed=14576282; DOI=10.1104/pp.103.026856;
RA Marian C.O., Bordoli S.J., Goltz M., Santarella R.A., Jackson L.P.,
RA Danilevskaya O., Beckstette M., Meeley R., Bass H.W.;
RT "The maize Single myb histone 1 gene, Smh1, belongs to a novel gene family
RT and encodes a protein that binds telomere DNA repeats in vitro.";
RL Plant Physiol. 133:1336-1350(2003).
RN [7]
RP INTERACTION WITH TRB1 AND TRB2.
RX PubMed=15589838; DOI=10.1016/j.febslet.2004.11.021;
RA Kuchar M., Fajkus J.;
RT "Interactions of putative telomere-binding proteins in Arabidopsis
RT thaliana: identification of functional TRF2 homolog in plants.";
RL FEBS Lett. 578:311-315(2004).
RN [8]
RP TISSUE SPECIFICITY, HOMODIMERIZATION, INTERACTION WITH TRB2, AND
RP DNA-BINDING.
RX PubMed=15060584; DOI=10.1139/g03-136;
RA Schrumpfova P., Kuchar M., Mikova G., Skrisovska L., Kubicarova T.,
RA Fajkus J.;
RT "Characterization of two Arabidopsis thaliana myb-like proteins showing
RT affinity to telomeric DNA sequence.";
RL Genome 47:316-324(2004).
RN [9]
RP GENE FAMILY.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [10]
RP INTERACTION WITH TRB1.
RX PubMed=18387366; DOI=10.1016/j.febslet.2008.03.034;
RA Schrumpfova P.P., Kuchar M., Palecek J., Fajkus J.;
RT "Mapping of interaction domains of putative telomere-binding proteins
RT AtTRB1 and AtPOT1b from Arabidopsis thaliana.";
RL FEBS Lett. 582:1400-1406(2008).
RN [11]
RP FUNCTION.
RX PubMed=19102728; DOI=10.1042/bj20082195;
RA Hofr C., Sultesova P., Zimmermann M., Mozgova I.,
RA Prochazkova Schrumpfova P., Wimmerova M., Fajkus J.;
RT "Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative
RT study of telomere-binding specificity and kinetics.";
RL Biochem. J. 419:221-228(2009).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19947985; DOI=10.1111/j.1365-313x.2009.04094.x;
RA Dvorackova M., Rossignol P., Shaw P.J., Koroleva O.A., Doonan J.H.,
RA Fajkus J.;
RT "AtTRB1, a telomeric DNA-binding protein from Arabidopsis, is concentrated
RT in the nucleolus and shows highly dynamic association with chromatin.";
RL Plant J. 61:637-649(2010).
CC -!- FUNCTION: Binds preferentially double-stranded telomeric repeats, but
CC it can also bind to the single G-rich telomeric strand.
CC {ECO:0000269|PubMed:19102728}.
CC -!- SUBUNIT: Forms a homodimer or heterodimers with TRB1 or TRB2. Interacts
CC with TRB1 and TRB2. {ECO:0000269|PubMed:15060584,
CC ECO:0000269|PubMed:15589838, ECO:0000269|PubMed:18387366}.
CC -!- INTERACTION:
CC Q9M2X3; Q8VWK4: TRB1; NbExp=3; IntAct=EBI-476134, EBI-476101;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:19947985}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:19947985}. Chromosome
CC {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:19947985}.
CC Note=Localized to the nucleolus during interphase.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15060584}.
CC -!- DOMAIN: HTH myb-type domain confers double-stranded telomeric DNA-
CC binding while the H15 domain is involved in non-specific DNA-protein
CC interaction and multimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. SMH subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00837}.
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DR EMBL; U83838; AAL73440.1; -; Genomic_DNA.
DR EMBL; U83839; AAL73439.1; -; mRNA.
DR EMBL; AY519542; AAS10012.1; -; mRNA.
DR EMBL; AL132965; CAB66923.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78598.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64902.1; -; Genomic_DNA.
DR EMBL; AY058887; AAL24273.1; -; mRNA.
DR EMBL; AY065069; AAL57702.1; -; mRNA.
DR EMBL; AY079043; AAL79593.1; -; mRNA.
DR PIR; T46051; T46051.
DR RefSeq; NP_001326904.1; NM_001339442.1.
DR RefSeq; NP_190554.1; NM_114845.5.
DR AlphaFoldDB; Q9M2X3; -.
DR SMR; Q9M2X3; -.
DR BioGRID; 9465; 8.
DR IntAct; Q9M2X3; 8.
DR MINT; Q9M2X3; -.
DR STRING; 3702.AT3G49850.1; -.
DR iPTMnet; Q9M2X3; -.
DR PaxDb; Q9M2X3; -.
DR PRIDE; Q9M2X3; -.
DR ProteomicsDB; 228336; -.
DR EnsemblPlants; AT3G49850.1; AT3G49850.1; AT3G49850.
DR EnsemblPlants; AT3G49850.2; AT3G49850.2; AT3G49850.
DR GeneID; 824147; -.
DR Gramene; AT3G49850.1; AT3G49850.1; AT3G49850.
DR Gramene; AT3G49850.2; AT3G49850.2; AT3G49850.
DR KEGG; ath:AT3G49850; -.
DR Araport; AT3G49850; -.
DR TAIR; locus:2097325; AT3G49850.
DR eggNOG; ENOG502QSU2; Eukaryota.
DR HOGENOM; CLU_047477_0_1_1; -.
DR InParanoid; Q9M2X3; -.
DR OMA; LMYIEEN; -.
DR OrthoDB; 1114012at2759; -.
DR PhylomeDB; Q9M2X3; -.
DR PRO; PR:Q9M2X3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2X3; baseline and differential.
DR Genevisible; Q9M2X3; AT.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR044597; SMH1-6.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46267; PTHR46267; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..295
FT /note="Telomere repeat-binding factor 3"
FT /id="PRO_0000417012"
FT DOMAIN 1..61
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 119..187
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DNA_BIND 28..57
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 100..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 239..277
FT /evidence="ECO:0000255"
SQ SEQUENCE 295 AA; 32247 MW; 3AA46269FAA055EF CRC64;
MGAPKLKWTP EEETALKAGV LKHGTGKWRT ILSDPVYSTI LKSRSNVDLK DKWRNISVTA
LWGSRKKAKL ALKRTPLSGS RQDDNATAIT IVSLANGDVG GQQIDAPSPP AGSCEPPRPS
TSVDKIILEA ITSLKRPFGP DGKSILMYIE ENFKMQPDMK RLVTSRLKYL TNVGTLVKKK
HKYRISQNYM AEGEGQRSPQ LLLEGNKENT PKPEENGVKN LTKSQVGGEV MIMGMTEKEA
AAAAARAVAE AEFAMAEAEE AAREADKAEA EAEAAHIFAK AAMKAVKYRM HSQTR
