ID   TRP1_ARATH              Reviewed;         578 AA.
AC   Q8L7L8; A8MQF8; A8MQM5; B9DFI1; C0Z2L6; Q9LTI6; Q9XGN0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Telomere repeat-binding protein 1;
DE            Short=AtTRP1;
GN   Name=TRP1; OrderedLocusNames=At5g59430; ORFNames=F2O15.20;
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], AND DNA-BINDING.
RX   PubMed=11278537; DOI=10.1074/jbc.m009659200;
RA   Chen C.M., Wang C.T., Ho C.H.;
RT   "A plant gene encoding a Myb-like protein that binds telomeric GGTTTAG
RT   repeats in vitro.";
RL   J. Biol. Chem. 276:16511-16519(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Qu L., Gu H.;
RT   "The MYB transcription factor family in Arabidopsis: a genome-wide cloning
RT   and expression pattern analysis.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [7]
RP   INTERACTION WITH KU70.
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   GENE FAMILY, TISSUE SPECIFICITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
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   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   [11]
RP   STRUCTURE BY NMR OF 464-560, AND DNA-BINDING.
RX   PubMed=16337232; DOI=10.1016/j.jmb.2005.11.009;
RA   Sue S.C., Hsiao H.H., Chung B.C., Cheng Y.H., Hsueh K.L., Chen C.M.,
RA   Ho C.H., Huang T.H.;
RT   "Solution structure of the Arabidopsis thaliana telomeric repeat-binding
RT   protein DNA binding domain: a new fold with an additional C-terminal
RT   helix.";
RL   J. Mol. Biol. 356:72-85(2006).
CC   -!- FUNCTION: Binds specifically to the plant telomeric double-stranded DNA
CC       sequences 5'-GGTTTAG-3'. At least 4 repeats of telomeric sequences are
CC       required for binding. Induces DNA bending.
CC   -!- SUBUNIT: Homodimer and heterodimer with TRP2 and TRP3. Interacts with
CC       KU70. {ECO:0000269|PubMed:15364931, ECO:0000269|PubMed:15589838}.
CC   -!- INTERACTION:
CC       Q8L7L8; Q38846: ERS1; NbExp=2; IntAct=EBI-476071, EBI-1606754;
CC       Q8L7L8; Q9FQ08: KU70; NbExp=2; IntAct=EBI-476071, EBI-476083;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8L7L8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8L7L8-2; Sequence=VSP_039134;
CC       Name=3;
CC         IsoId=Q8L7L8-3; Sequence=VSP_039135;
CC       Name=4;
CC         IsoId=Q8L7L8-4; Sequence=VSP_039133;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highest expression in
CC       flowers and leaves. {ECO:0000269|PubMed:15364931,
CC       ECO:0000269|PubMed:15688221}.
CC   -!- DOMAIN: A N-terminal domain (80-269) is responsible for the interaction
CC       with KU70.
CC   -!- DOMAIN: The C-terminal domain (464-578) is sufficient for telomere
CC       binding.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, probably due to redundancy.
CC       {ECO:0000269|PubMed:15364931}.
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DR   EMBL; Y17722; CAB50690.1; -; Genomic_DNA.
DR   EMBL; AY519544; AAS10014.1; -; mRNA.
DR   EMBL; AB025604; BAA97479.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97184.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97185.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97186.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97187.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70341.1; -; Genomic_DNA.
DR   EMBL; AY128382; AAM91585.1; -; mRNA.
DR   EMBL; BT000117; AAN15436.1; -; mRNA.
DR   EMBL; AK316779; BAH19498.1; -; mRNA.
DR   EMBL; AK318830; BAH56945.1; -; mRNA.
DR   PIR; T51230; T51230.
DR   RefSeq; NP_001078770.1; NM_001085301.1. [Q8L7L8-3]
DR   RefSeq; NP_001078771.1; NM_001085302.1. [Q8L7L8-4]
DR   RefSeq; NP_001331960.1; NM_001345351.1. [Q8L7L8-1]
DR   RefSeq; NP_200751.1; NM_125334.4. [Q8L7L8-1]
DR   RefSeq; NP_851221.1; NM_180890.1. [Q8L7L8-1]
DR   PDB; 2AJE; NMR; -; A=464-560.
DR   PDBsum; 2AJE; -.
DR   AlphaFoldDB; Q8L7L8; -.
DR   BMRB; Q8L7L8; -.
DR   SMR; Q8L7L8; -.
DR   BioGRID; 21306; 8.
DR   IntAct; Q8L7L8; 5.
DR   STRING; 3702.Q8L7L8; -.
DR   PaxDb; 3702-AT5G59430-2; -.
DR   ProteomicsDB; 232383; -. [Q8L7L8-1]
DR   EnsemblPlants; AT5G59430.1; AT5G59430.1; AT5G59430. [Q8L7L8-1]
DR   EnsemblPlants; AT5G59430.2; AT5G59430.2; AT5G59430. [Q8L7L8-1]
DR   EnsemblPlants; AT5G59430.3; AT5G59430.3; AT5G59430. [Q8L7L8-3]
DR   EnsemblPlants; AT5G59430.4; AT5G59430.4; AT5G59430. [Q8L7L8-4]
DR   EnsemblPlants; AT5G59430.5; AT5G59430.5; AT5G59430. [Q8L7L8-1]
DR   GeneID; 836062; -.
DR   Gramene; AT5G59430.1; AT5G59430.1; AT5G59430. [Q8L7L8-1]
DR   Gramene; AT5G59430.2; AT5G59430.2; AT5G59430. [Q8L7L8-1]
DR   Gramene; AT5G59430.3; AT5G59430.3; AT5G59430. [Q8L7L8-3]
DR   Gramene; AT5G59430.4; AT5G59430.4; AT5G59430. [Q8L7L8-4]
DR   Gramene; AT5G59430.5; AT5G59430.5; AT5G59430. [Q8L7L8-1]
DR   KEGG; ath:AT5G59430; -.
DR   Araport; AT5G59430; -.
DR   TAIR; AT5G59430; TRP1.
DR   eggNOG; ENOG502QPSZ; Eukaryota.
DR   InParanoid; Q8L7L8; -.
DR   OMA; SENDKTC; -.
DR   OrthoDB; 659175at2759; -.
DR   PhylomeDB; Q8L7L8; -.
DR   EvolutionaryTrace; Q8L7L8; -.
DR   PRO; PR:Q8L7L8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L7L8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0031965; C:nuclear membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:TAIR.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR   CDD; cd11660; SANT_TRF; 1.
DR   CDD; cd17039; Ubl_ubiquitin_like; 1.
DR   Gene3D; 1.10.246.220; -; 1.
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   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR21717:SF65; TELOMERE REPEAT-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR21717; TELOMERIC REPEAT BINDING PROTEIN; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   Genevisible; Q8L7L8; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..578
FT                   /note="Telomere repeat-binding protein 1"
FT                   /id="PRO_0000394124"
FT   DOMAIN          293..372
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          463..522
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        491..518
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          440..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..469
FT                   /note="Interaction with DNA"
FT   REGION          511..515
FT                   /note="Interaction with DNA"
FT   REGION          522..529
FT                   /note="Interaction with DNA"
FT   COMPBIAS        440..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         29
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_039133"
FT   VAR_SEQ         555..578
FT                   /note="QLQQNVNKLEQETQSQTTEGLLLL -> PWRSSLLCVLLLLLMIM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_039134"
FT   VAR_SEQ         555..578
FT                   /note="QLQQNVNKLEQETQSQTTEGLLLL -> HLGGRLSFVYYYYY (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_039135"
FT   CONFLICT        4
FT                   /note="H -> R (in Ref. 1; CAB50690)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="S -> P (in Ref. 1; CAB50690)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="D -> E (in Ref. 6; BAH19498)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="V -> A (in Ref. 5; AAM91585/AAN15436)"
FT                   /evidence="ECO:0000305"
FT   HELIX           473..486
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   STRAND          488..490
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   HELIX           491..495
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   STRAND          496..501
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   HELIX           507..519
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   TURN            525..529
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   HELIX           536..551
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   TURN            552..555
FT                   /evidence="ECO:0007829|PDB:2AJE"
FT   STRAND          556..558
FT                   /evidence="ECO:0007829|PDB:2AJE"
SQ   SEQUENCE   578 AA;  65036 MW;  853B54C5FC2E5E01 CRC64;
     MVSHKCVEEF GYASYLVPSN ARAPRSARKR RSIEKRISKE DDNMCAIDLL ATVAGHLSFE
     SGSSLMSIDK LIEDHRVKEE FPEEEKPLMP VALSPYRGSL SPCGFSSVIN GKVENEVDGF
     SYSGGSDACQ VGNFSQDVKP DIDGDAVVLD ARPNVVVSLG SSSRTEVPSI GNCVSHGVRD
     DVNLFSRDDD ENFSKYIHPR VTKHSPRTVP RIGDRRIRKI LASRHWKGGS RHSDTKPWRN
     YYLHQQRSYP IKKRKNFDHI SDSVTDDYRM RTKMHRGSRK GQGASFVASD SHVKLRIKSF
     RVPELFIEIP ETATVGSLKR MVMEAVSTLL SDGHRVGLMV QGKKVRDDNK TLHQTGISQD
     NSHLDSLDFS LEPSSEMPQL LTSHPLGHAC EELLPVCQAT KIDNVLESDH HDSALFPSDS
     LGNNNVTEDS KAMISVALNE LSSQSQPPSR KSRRSEQQQQ QAAQRRIRRP FSVAEVEALV
     QAVEKLGTGR WRDVKLCAFE DADHRTYVDL KDKWKTLVHT AKISPQQRRG EPVPQELLNR
     VLNAHGYWTQ QQMQQLQQNV NKLEQETQSQ TTEGLLLL
//