TRP4_ARATH
ID TRP4_ARATH Reviewed; 640 AA.
AC Q9FFY9; O81375; Q0WUW8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Telomere repeat-binding protein 4;
DE AltName: Full=H-protein promoter binding factor-1;
DE Short=AtTBP1;
DE AltName: Full=Telomeric DNA-binding protein 1;
GN Name=TRP4; Synonyms=HPPBF-1, TBP1; OrderedLocusNames=At5g13820;
GN ORFNames=MAC12.23;
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 [MRNA], FUNCTION, DNA-BINDING, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=11513850; DOI=10.1016/s0014-5793(01)02685-0;
RA Hwang M.G., Chung I.K., Kang B.G., Cho M.H.;
RT "Sequence-specific binding property of Arabidopsis thaliana telomeric DNA
RT binding protein 1 (AtTBP1).";
RL FEBS Lett. 503:35-40(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Abbaraju H.K.R., Behal R.H., Oliver D.J.;
RT "Identification of an unusual Myb-type transcription factor that is
RT involved in the light-dependent expression of the H-protein of glycine
RT decarboxylase.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH STO.
RX PubMed=12909688; DOI=10.1093/jxb/erg241;
RA Nagaoka S., Takano T.;
RT "Salt tolerance-related protein STO binds to a Myb transcription factor
RT homologue and confers salt tolerance in Arabidopsis.";
RL J. Exp. Bot. 54:2231-2237(2003).
RN [8]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=15364931; DOI=10.1074/jbc.m407938200;
RA Karamysheva Z.N., Surovtseva Y.V., Vespa L., Shakirov E.V., Shippen D.E.;
RT "A C-terminal Myb extension domain defines a novel family of double-strand
RT telomeric DNA-binding proteins in Arabidopsis.";
RL J. Biol. Chem. 279:47799-47807(2004).
RN [9]
RP DNA-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=15688221; DOI=10.1007/s00438-004-1096-3;
RA Hwang M.G., Kim K., Lee W.K., Cho M.H.;
RT "AtTBP2 and AtTRP2 in Arabidopsis encode proteins that bind plant telomeric
RT DNA and induce DNA bending in vitro.";
RL Mol. Genet. Genomics 273:66-75(2005).
RN [10]
RP FUNCTION, MUTAGENESIS OF ARG-607, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17272298; DOI=10.1093/nar/gkm043;
RA Hwang M.G., Cho M.H.;
RT "Arabidopsis thaliana telomeric DNA-binding protein 1 is required for
RT telomere length homeostasis and its Myb-extension domain stabilizes plant
RT telomeric DNA binding.";
RL Nucleic Acids Res. 35:1333-1342(2007).
RN [11]
RP INTERACTION WITH SNL1.
RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
RA Conlan R.S.;
RT "PAH-domain-specific interactions of the Arabidopsis transcription
RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS
RT EARLY2 Myb-DNA binding factors.";
RL J. Mol. Biol. 395:937-949(2010).
CC -!- FUNCTION: Binds specifically to the plant telomeric double-stranded DNA
CC sequences 5'-TTTAGGG-3'. At least 2 repeats of telomeric sequences are
CC required for binding. Induces DNA bending.
CC {ECO:0000269|PubMed:11513850, ECO:0000269|PubMed:17272298}.
CC -!- SUBUNIT: Homomultimer. Interacts with SNL1 (via PAH2). Interacts with
CC STO. {ECO:0000269|PubMed:11513850, ECO:0000269|PubMed:12909688,
CC ECO:0000269|PubMed:19962994}.
CC -!- INTERACTION:
CC Q9FFY9; Q9SRH9: SNL1; NbExp=2; IntAct=EBI-2616485, EBI-2616294;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:12909688, ECO:0000269|PubMed:17272298}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highest expression in
CC flowers and roots. {ECO:0000269|PubMed:11513850,
CC ECO:0000269|PubMed:15364931, ECO:0000269|PubMed:15688221}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:12909688}.
CC -!- DOMAIN: The Myb-extension domain (593-622) is critical for telomere
CC binding.
CC -!- DISRUPTION PHENOTYPE: Viable, but deregulation of telomere length
CC control. {ECO:0000269|PubMed:17272298}.
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DR EMBL; AY029195; AAK31590.1; -; mRNA.
DR EMBL; AF072536; AAC24592.1; -; mRNA.
DR EMBL; AB005230; BAB11110.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91945.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68452.1; -; Genomic_DNA.
DR EMBL; AK227016; BAE99080.1; -; mRNA.
DR EMBL; BT046176; ACI49775.1; -; mRNA.
DR PIR; T51231; T51231.
DR RefSeq; NP_001330208.1; NM_001343296.1.
DR RefSeq; NP_196886.1; NM_121385.5.
DR AlphaFoldDB; Q9FFY9; -.
DR SMR; Q9FFY9; -.
DR BioGRID; 16505; 2.
DR IntAct; Q9FFY9; 1.
DR STRING; 3702.AT5G13820.1; -.
DR iPTMnet; Q9FFY9; -.
DR PaxDb; Q9FFY9; -.
DR PRIDE; Q9FFY9; -.
DR ProteomicsDB; 232382; -.
DR EnsemblPlants; AT5G13820.1; AT5G13820.1; AT5G13820.
DR EnsemblPlants; AT5G13820.2; AT5G13820.2; AT5G13820.
DR GeneID; 831227; -.
DR Gramene; AT5G13820.1; AT5G13820.1; AT5G13820.
DR Gramene; AT5G13820.2; AT5G13820.2; AT5G13820.
DR KEGG; ath:AT5G13820; -.
DR Araport; AT5G13820; -.
DR TAIR; locus:2159048; AT5G13820.
DR eggNOG; ENOG502QPSZ; Eukaryota.
DR HOGENOM; CLU_020710_2_0_1; -.
DR InParanoid; Q9FFY9; -.
DR OMA; NIMPTDS; -.
DR OrthoDB; 302274at2759; -.
DR PhylomeDB; Q9FFY9; -.
DR PRO; PR:Q9FFY9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFY9; baseline and differential.
DR Genevisible; Q9FFY9; AT.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:TAIR.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:TAIR.
DR GO; GO:0000723; P:telomere maintenance; TAS:TAIR.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR031105; TRP_plant.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR PANTHER; PTHR21717; PTHR21717; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..640
FT /note="Telomere repeat-binding protein 4"
FT /id="PRO_0000394127"
FT DOMAIN 343..422
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 530..589
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 558..585
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 442..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 607
FT /note="R->G: 60% decrease in telomere binding."
FT /evidence="ECO:0000269|PubMed:17272298"
FT MUTAGEN 607
FT /note="R->I: 80% decrease in telomere binding."
FT /evidence="ECO:0000269|PubMed:17272298"
FT CONFLICT 372
FT /note="V -> L (in Ref. 5; BAE99080)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="G -> R (in Ref. 2; AAC24592)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="P -> H (in Ref. 2; AAC24592)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="S -> P (in Ref. 2; AAC24592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 70484 MW; 9851870E51194560 CRC64;
MVVKRKLNCG GSNGFDFPNI PKAPRSSRRK VSGKRSDDES EICAIDLLAS LAGKLLEESE
SSSTSTYASE ADNLDHLGGL IKQELEDGYT TKPCKSEFFD PGNPASKSTS ENTSVTCLPF
SSFENDCILE QTPVSDCKRA SGLKSLVGSI TEETCVVNED AGSEQGANTF SLKDPSQLHS
QSPESVLLDG DVKLAPCTDQ VPNDSFKGYR NHSKLVCRDD DENYCKYYKF SDKCKSYRPL
SRVGNRRIMQ SVRAISKLKC FEDTRTDGRL KALYRKRKLC YGYNPWKRET IHRKRRLSDK
GLVVNYDGGL SSESVSNSPE KGESENGDFS AAKIGLLSKD SRVKFSIKSL RIPELVIEVP
ETATVGLLKR TVKEAVTALL GGGIRIGVLV QGKKVRDDNN TLSQTGLSCR ENLGNLGFTL
EPGLETLPVP LCSETPVLSL PTDSTKLSER SAASPALETG IPLPPQDEDY LINLGNSVEN
NDELVPHLSD IPADEQPSSD SRALVPVLAL ESDALALVPV NEKPKRTELS QRRTRRPFSV
TEVEALVSAV EEVGTGRWRD VKLRSFENAS HRTYVDLKDK WKTLVHTASI SPQQRRGEPV
PQELLDRVLG AHRYWTQHQM KQNGKHQVAT TMVVEAGSSM
