TRB1_ARATH
ID TRB1_ARATH Reviewed; 300 AA.
AC Q8VWK4; Q8LA70; Q8VX39; Q9LPL9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Telomere repeat-binding factor 1;
DE Short=AtTRB1;
DE AltName: Full=MYB transcription factor;
GN Name=TRB1; OrderedLocusNames=At1g49950; ORFNames=F2J10.16;
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 TRB1.";
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP HOMODIMERIZATION, AND INTERACTION WITH POT1B; TRB2 AND TRB3.
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 [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 HOMODIMERIZATION, AND INTERACTION WITH POT1B; TRB2 AND TRB3.
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 MULTIMERIZATION, DNA-BINDING, AND DOMAIN.
RX PubMed=18479720; DOI=10.1016/j.phytochem.2008.04.001;
RA Mozgova I., Schrumpfova P.P., Hofr C., Fajkus J.;
RT "Functional characterization of domains in AtTRB1, a putative telomere-
RT binding protein in Arabidopsis thaliana.";
RL Phytochemistry 69:1814-1819(2008).
RN [12]
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 [13]
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.
CC {ECO:0000269|PubMed:19102728}.
CC -!- SUBUNIT: Forms a homodimer and heterodimers with TRB2 or TRB3.
CC Interacts with POT1b, TRB2 and TRB3 through its H15 domain.
CC {ECO:0000269|PubMed:15589838, ECO:0000269|PubMed:18387366}.
CC -!- INTERACTION:
CC Q8VWK4; Q6NKX5: POT1B; NbExp=4; IntAct=EBI-476101, EBI-476223;
CC Q8VWK4; Q9FJW5: TRB2; NbExp=4; IntAct=EBI-476101, EBI-476115;
CC Q8VWK4; Q9M2X3: TRB3; NbExp=3; IntAct=EBI-476101, EBI-476134;
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 -!- 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:0000269|PubMed:18479720}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. SMH subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U83623; AAL73123.1; -; Genomic_DNA.
DR EMBL; U83624; AAL73438.1; -; mRNA.
DR EMBL; AY519539; AAS10009.1; -; mRNA.
DR EMBL; AC015445; AAF76448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32497.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32498.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32499.1; -; Genomic_DNA.
DR EMBL; AY062736; AAL32814.1; -; mRNA.
DR EMBL; BT009677; AAP80178.1; -; mRNA.
DR EMBL; AY087994; AAM65540.1; -; mRNA.
DR RefSeq; NP_564559.1; NM_103882.4.
DR RefSeq; NP_849789.1; NM_179458.3.
DR RefSeq; NP_973998.1; NM_202269.2.
DR AlphaFoldDB; Q8VWK4; -.
DR SMR; Q8VWK4; -.
DR BioGRID; 26643; 6.
DR IntAct; Q8VWK4; 4.
DR MINT; Q8VWK4; -.
DR STRING; 3702.AT1G49950.3; -.
DR iPTMnet; Q8VWK4; -.
DR PaxDb; Q8VWK4; -.
DR PRIDE; Q8VWK4; -.
DR ProteomicsDB; 228387; -.
DR EnsemblPlants; AT1G49950.1; AT1G49950.1; AT1G49950.
DR EnsemblPlants; AT1G49950.2; AT1G49950.2; AT1G49950.
DR EnsemblPlants; AT1G49950.3; AT1G49950.3; AT1G49950.
DR GeneID; 841418; -.
DR Gramene; AT1G49950.1; AT1G49950.1; AT1G49950.
DR Gramene; AT1G49950.2; AT1G49950.2; AT1G49950.
DR Gramene; AT1G49950.3; AT1G49950.3; AT1G49950.
DR KEGG; ath:AT1G49950; -.
DR Araport; AT1G49950; -.
DR TAIR; locus:2031095; AT1G49950.
DR eggNOG; ENOG502QSU2; Eukaryota.
DR HOGENOM; CLU_047477_0_1_1; -.
DR InParanoid; Q8VWK4; -.
DR OMA; CKMMIRA; -.
DR OrthoDB; 1324883at2759; -.
DR PhylomeDB; Q8VWK4; -.
DR PRO; PR:Q8VWK4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VWK4; baseline and differential.
DR Genevisible; Q8VWK4; 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:0032991; C:protein-containing complex; IPI:TAIR.
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:1990841; F:promoter-specific chromatin binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:TAIR.
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..300
FT /note="Telomere repeat-binding factor 1"
FT /id="PRO_0000417010"
FT DOMAIN 1..58
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 117..185
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 93..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..290
FT /evidence="ECO:0000255"
FT COMPBIAS 93..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 188
FT /note="P -> S (in Ref. 6; AAM65540)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> V (in Ref. 1; AAL73438 and 6; AAM65540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33017 MW; 3B4A383E129F537B CRC64;
MGAPKQKWTQ EEESALKSGV IKHGPGKWRT ILKDPEFSGV LYLRSNVDLK DKWRNMSVMA
NGWGSREKSR LAVKRTFSLP KQEENSLALT NSLQSDEENV DATSGLQVSS NPPPRRPNVR
LDSLIMEAIA TLKEPGGCNK TTIGAYIEDQ YHAPPDFKRL LSTKLKYLTS CGKLVKVKRK
YRIPNSTPLS SHRRKGLGVF GGKQRTSSLP SPKTDIDEVN FQTRSQIDTE IARMKSMNVH
EAAAVAAQAV AEAEAAMAEA EEAAKEAEAA EAEAEAAQAF AEEASKTLKG RNICKMMIRA
