TRP1_ARATH
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 03-AUG-2022, entry version 131.
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.AT5G59430.2; -.
DR PaxDb; Q8L7L8; -.
DR PRIDE; Q8L7L8; -.
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; locus:2148383; AT5G59430.
DR eggNOG; ENOG502QPSZ; Eukaryota.
DR InParanoid; Q8L7L8; -.
DR OMA; SENDKTC; -.
DR OrthoDB; 302274at2759; -.
DR PhylomeDB; Q8L7L8; -.
DR EvolutionaryTrace; Q8L7L8; -.
DR PRO; PR:Q8L7L8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7L8; baseline and differential.
DR Genevisible; Q8L7L8; AT.
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 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; PTHR21717; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
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
