CTC1_ARATH
ID CTC1_ARATH Reviewed; 1272 AA.
AC D0EL35; B3H4T9; Q0WL26; Q9SZ84;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=CST complex subunit CTC1 {ECO:0000303|PubMed:19854131};
DE AltName: Full=Protein CONSERVED TELOMERE MAINTENANCE COMPONENT 1 {ECO:0000303|PubMed:19854131};
DE Short=AtCTC1 {ECO:0000303|PubMed:19854131};
GN Name=CTC1 {ECO:0000303|PubMed:19854131};
GN OrderedLocusNames=At4g09680 {ECO:0000312|Araport:AT4G09680};
GN ORFNames=F17A8.30 {ECO:0000312|EMBL:CAB39635.1};
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH STN1, AND DISRUPTION PHENOTYPE.
RX PubMed=19854131; DOI=10.1016/j.molcel.2009.09.017;
RA Surovtseva Y.V., Churikov D., Boltz K.A., Song X., Lamb J.C.,
RA Warrington R., Leehy K., Heacock M., Price C.M., Shippen D.E.;
RT "Conserved telomere maintenance component 1 interacts with STN1 and
RT maintains chromosome ends in higher eukaryotes.";
RL Mol. Cell 36:207-218(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP FUNCTION, AND INTERACTION WITH POT1A.
RX PubMed=25329641; DOI=10.1371/journal.pgen.1004738;
RA Renfrew K.B., Song X., Lee J.R., Arora A., Shippen D.E.;
RT "POT1a and components of CST engage telomerase and regulate its activity in
RT Arabidopsis.";
RL PLoS Genet. 10:E1004738-E1004738(2014).
CC -!- FUNCTION: Component of the CST complex, a complex that binds to single-
CC stranded DNA and is required to protect telomeres from DNA degradation.
CC The CST complex binds single-stranded DNA with high affinity in a
CC sequence-independent manner, while isolated subunits bind DNA with low
CC affinity by themselves (PubMed:19854131). Associates with enzymatically
CC active telomerase (PubMed:25329641). {ECO:0000269|PubMed:19854131,
CC ECO:0000269|PubMed:25329641}.
CC -!- SUBUNIT: Component of the CST complex, composed of CTC1, TEN1 and STN1.
CC Interacts with POT1A (PubMed:25329641). {ECO:0000269|PubMed:25329641}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19854131}.
CC Chromosome, telomere {ECO:0000269|PubMed:19854131}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=D0EL35-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D0EL35-2; Sequence=VSP_038872, VSP_038873;
CC Name=3;
CC IsoId=D0EL35-3; Sequence=VSP_038871, VSP_038874, VSP_038875;
CC -!- DISRUPTION PHENOTYPE: Severe telomere deprotection accompanied by a
CC rapid onset of developmental defects and sterility. The large majority
CC of plants have grossly distorted floral phyllotaxy with an irregular
CC branching pattern and fasciated (thick and broad) main and lateral
CC stems and siliques. Although most mutants produce an influorescence
CC bolt, this structure is highly variable in size, ranging from very
CC short to wild-type. Flowers and siliques are often fused, and seed
CC yield is typically reduced to 10% of wild-type. The germination
CC efficiency of the few seeds that could be recovered was extremely low.
CC Telomeric and subtelomeric tracts are dramatically eroded, and
CC chromosome ends exhibit increased G overhangs, recombination, and end-
CC to-end fusions. {ECO:0000269|PubMed:19854131}.
CC -!- SIMILARITY: Belongs to the CTC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB39635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ850537; ACX37401.1; -; mRNA.
DR EMBL; AL049482; CAB39635.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161515; CAB78091.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82781.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67742.1; -; Genomic_DNA.
DR EMBL; AK230383; BAF02181.1; -; mRNA.
DR PIR; T04015; T04015.
DR RefSeq; NP_001118960.1; NM_001125488.2. [D0EL35-2]
DR RefSeq; NP_001329551.1; NM_001340629.1. [D0EL35-1]
DR AlphaFoldDB; D0EL35; -.
DR BioGRID; 11853; 2.
DR STRING; 3702.AT4G09680.1; -.
DR PaxDb; D0EL35; -.
DR PRIDE; D0EL35; -.
DR ProteomicsDB; 222723; -. [D0EL35-1]
DR EnsemblPlants; AT4G09680.2; AT4G09680.2; AT4G09680. [D0EL35-2]
DR EnsemblPlants; AT4G09680.4; AT4G09680.4; AT4G09680. [D0EL35-1]
DR GeneID; 826554; -.
DR Gramene; AT4G09680.2; AT4G09680.2; AT4G09680. [D0EL35-2]
DR Gramene; AT4G09680.4; AT4G09680.4; AT4G09680. [D0EL35-1]
DR KEGG; ath:AT4G09680; -.
DR Araport; AT4G09680; -.
DR eggNOG; ENOG502QU1G; Eukaryota.
DR InParanoid; D0EL35; -.
DR PhylomeDB; D0EL35; -.
DR PRO; PR:D0EL35; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; D0EL35; baseline and differential.
DR GO; GO:1990879; C:CST complex; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0045740; P:positive regulation of DNA replication; IBA:GO_Central.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IBA:GO_Central.
DR InterPro; IPR042617; CTC1-like.
DR InterPro; IPR028262; CTC1_plant.
DR PANTHER; PTHR14865; PTHR14865; 1.
DR Pfam; PF15491; CTC1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..1272
FT /note="CST complex subunit CTC1"
FT /id="PRO_0000392985"
FT VAR_SEQ 1..440
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038871"
FT VAR_SEQ 456..481
FT /note="GGIFTEFCMHESCGCNSEARDCNLKL -> VKWVGSLLNSACMSHADAIVKL
FT VIAT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038872"
FT VAR_SEQ 482..1272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038873"
FT VAR_SEQ 1075..1104
FT /note="VLSVYLLVLQTRSDDPSENECRNNIDIPLA -> FIFWFSKLDLMIPQKTNV
FT GTILIYHLQDLW (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038874"
FT VAR_SEQ 1105..1272
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038875"
FT CONFLICT 435
FT /note="K -> E (in Ref. 1; ACX37401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1272 AA; 141925 MW; 5C990F53DCAC11CD CRC64;
MENTTILTVK DLVNEGIAVT GASSLFSSAA SHSSSESTST NPKSHPGAVD SDFSRKFLTP
LNYPTVIFGT VALPSETLKC PNRYCFRFTD GDLTICCDIL GFEFRAIGSK ICVLSWNFLP
MNHSGGFLEI INWKFVDSGS LLSRCSGISS FPLIPSLYSS QNGDRKSRYS VCGVLESISP
VSVVPCMDGV SSDSVNLPGF LVHVMACECK VYSRDAIDCG HAFERSVFVY FCGLEAASWH
PVVMKLVGRN VALSGLKRKL VYVRGDSLLV FVTTENSVLH PPWLSKKGTV SKTVVDRRGN
CGSYRGYVRG LYLKGKLVEM DEDVWLLLTD QILNRSHSIR TGSLIFIRNV HFVNTKFPWG
EVLILGACFK TSITVEFFSP FETSCLVDSC RQTSLSLYVE SLSFPARLWT LLVRISFEKF
NRMPSDKEIL RSCQKDELTK MYAESRIPPS MFQPRGGIFT EFCMHESCGC NSEARDCNLK
LVMPISSFVH HVKVMLNELL SQIKKDFSAS DCLSHSSSTW KRYNNTNPKT LRSEDTGVIL
LGRLKISSSG RLQLHDRTSS IDVLTPDLLS DRNASRICEV PDYYLIIEGI PESMLHMPFL
KNPFRCSSVL NPTPLAIKNT LTVPFSLSLG TASCKHLLKH HPFDWRHDFN EFKEGFFHLF
RVTHKFPILK NGHPGMPDCT SVFIEALVLP WDLICTVTEE EAAAPNFEEH DTSQEIRPHK
RCKTNNGLQS QSFLSVPHEI SCQMTIRCAS SHCLVATATL SNLTENKSGK MHSAMRVLLE
FIPECSNYYG LQIGGCYLMK HGSDDSFCVG RSGISNNDKI NFRPETRLWS LEFSFDEVLT
HDGSMDVHPL VSSQPSFAVE QQNVSSRQPC SDVSLLLPYD AKGLFSVFLN DLEGLNKPLA
AGKDNNNISC CTQSETIMHA EPSRLLPSNS LFPEGNLATF RGDVVAVDAV TSSVVDVSSS
YCINVLVNHQ MVKIFGPLRR HSYLTGFGFG TNATFYRILG TGEQNSFVLT SASFIKINSR
KALDSPPLEK PTHGAALCLP KITPQEFVPC ILAGPACNSF SGNEDNQQIK FACKVLSVYL
LVLQTRSDDP SENECRNNID IPLAGFVVDD GSSTYLCWTS GERAFTILRL HEELPEETID
VVQWTRRYSN WGTTAYHLDQ IVRVHKRIVM KCNGSQIDVL FQDITIAVTS DQLLTKSEDK
FLKWLILNAI SGPIWEVAAS SMDMKMIEHL EREQCVEMET SRYNLQSVWG NEVCQVDPLV
RAWSLLQGLL NS
