TRP2_ARATH
ID TRP2_ARATH Reviewed; 553 AA.
AC Q9SNB9; Q2V3Q5; Q3L8D5; Q700E9; Q8RX21; Q8W4L7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Telomere repeat-binding protein 2;
DE AltName: Full=Protein TRF-LIKE 1;
GN Name=TRP2; Synonyms=TRFL1, TRP4; OrderedLocusNames=At3g46590;
GN ORFNames=F12A12.110;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Chen C.M., Wang C.T., Kao Y.-H., Chang G.-D., Ho C.-H., Lee F.-M.,
RA Hseu M.-J.;
RT "Functional redundancy of the duplex telomeric DNA-binding proteins in
RT Arabidopsis.";
RL Bot. Bull. Acad. Sin. 46:315-324(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY, DNA-BINDING, TISSUE SPECIFICITY, SUBUNIT, AND DISRUPTION
RP 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 [8]
RP FUNCTION, 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 [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 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. At least 2 repeats of telomeric sequences are required for
CC binding. Induces DNA bending. {ECO:0000269|PubMed:15688221}.
CC -!- SUBUNIT: Homodimer and heterodimer with TRP1. Interacts with SNL1.
CC {ECO:0000269|PubMed:15364931, ECO:0000269|PubMed:19962994}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SNB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SNB9-2; Sequence=VSP_039136;
CC Name=3;
CC IsoId=Q9SNB9-3; Sequence=VSP_039137;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highest expression in
CC flowers and leaves. {ECO:0000269|PubMed:15364931,
CC ECO:0000269|PubMed:15688221}.
CC -!- DOMAIN: The Myb-extension domain (509-540) is necessary and sufficient
CC for telomere binding.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, probably due to redundancy.
CC {ECO:0000269|PubMed:15364931}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL32567.1; Type=Miscellaneous discrepancy; Note=Chimera. Chimera of genomic DNA and cDNA.; Evidence={ECO:0000305};
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DR EMBL; AL133314; CAB62329.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78175.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78176.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78177.1; -; Genomic_DNA.
DR EMBL; AK229705; BAF01544.1; -; mRNA.
DR EMBL; AY062489; AAL32567.1; ALT_SEQ; mRNA.
DR EMBL; AY090966; AAM14002.1; -; mRNA.
DR EMBL; AY519541; AAS10011.1; -; mRNA.
DR EMBL; AY568647; AAS79537.1; -; mRNA.
DR EMBL; AJ630475; CAG25848.1; -; mRNA.
DR EMBL; AY395985; AAR28946.1; -; mRNA.
DR EMBL; BT033142; ACF40322.1; -; mRNA.
DR PIR; T45596; T45596.
DR RefSeq; NP_001030821.1; NM_001035744.2. [Q9SNB9-1]
DR RefSeq; NP_001030822.2; NM_001035745.2. [Q9SNB9-3]
DR RefSeq; NP_190243.2; NM_114526.3. [Q9SNB9-2]
DR AlphaFoldDB; Q9SNB9; -.
DR SMR; Q9SNB9; -.
DR BioGRID; 9132; 3.
DR IntAct; Q9SNB9; 2.
DR STRING; 3702.AT3G46590.2; -.
DR PaxDb; Q9SNB9; -.
DR EnsemblPlants; AT3G46590.1; AT3G46590.1; AT3G46590. [Q9SNB9-2]
DR EnsemblPlants; AT3G46590.2; AT3G46590.2; AT3G46590. [Q9SNB9-1]
DR EnsemblPlants; AT3G46590.3; AT3G46590.3; AT3G46590. [Q9SNB9-3]
DR GeneID; 823812; -.
DR Gramene; AT3G46590.1; AT3G46590.1; AT3G46590. [Q9SNB9-2]
DR Gramene; AT3G46590.2; AT3G46590.2; AT3G46590. [Q9SNB9-1]
DR Gramene; AT3G46590.3; AT3G46590.3; AT3G46590. [Q9SNB9-3]
DR KEGG; ath:AT3G46590; -.
DR Araport; AT3G46590; -.
DR TAIR; locus:2075145; AT3G46590.
DR eggNOG; ENOG502QPSZ; Eukaryota.
DR InParanoid; Q9SNB9; -.
DR OMA; LINDCEP; -.
DR PhylomeDB; Q9SNB9; -.
DR PRO; PR:Q9SNB9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SNB9; baseline and differential.
DR Genevisible; Q9SNB9; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008301; F:DNA binding, bending; IDA:TAIR.
DR GO; GO:0042162; F:telomeric DNA binding; IDA: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 Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..553
FT /note="Telomere repeat-binding protein 2"
FT /id="PRO_0000394125"
FT DOMAIN 285..364
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 448..507
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 476..503
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15208423"
FT /id="VSP_039136"
FT VAR_SEQ 210..215
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_039137"
SQ SEQUENCE 553 AA; 61775 MW; 92C4C2D9DB252594 CRC64;
MVSHKVLEFG DDGYKLPAQA RAPRSLRKKR IYEKKIPGDD KMCAIDLLAT VAGSLLLESK
SPVNACLVVQ NTVKNEYPAD ENPVKAVPYS ESPSLFDNGK CGFSSVITNP NHLLVGDKVG
KEVEGFSSLG VSGDVKPDVV ASIGSNSSTE VGACGNGSPN ESRDDVNLFS RNDDDENFSG
YIRTRMTRPV PRIGDRRIRK ILASRHWKGG SKNNTDAKPW YCSKRSYYLH HHQRSYPIKK
RKYFDSVYDS NSDDYRLQGK THKGSRTISS MKSRNASFVS RDHHVKLRIK SFRVPELFVE
IPETATVGSL KRMVMEAVTT ILGDGLRVGL MVQGKKVRDD GKTLLQTGIS EENNHLDSLG
FSLEPSLETT PQPLLSSYLS DHACDDVTLC HDNALDSSHE PEPSPADSFG KLGTSDHSRA
LIPVASAAML APRPPNRKFK RTEQQLAAQR RIRRPFSVTE VEALVQAVEK LGTGRWRDVK
VRAFEDADHR TYVDLKDKWK TLVHTARISP QQRRGEPVPQ ELLDRVLKAH AYWSQHLMHQ
LQTEPPSTQV EAL
