CTC1_MOUSE
ID CTC1_MOUSE Reviewed; 1212 AA.
AC Q5SUQ9; B2RW14; Q3UKQ1; Q6P9S2; Q8BRK2; Q91WN0; Q9CW32;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=CST complex subunit CTC1;
DE AltName: Full=Alpha-accessory factor of 132 kDa;
DE Short=AAF-132;
DE Short=AAF132;
DE AltName: Full=Conserved telomere maintenance component 1;
GN Name=Ctc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, Lung, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 244-1211 (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 98-108; 110-127; 561-568; 814-832; 962-968; 1090-1106;
RP 1111-1137 AND 1159-1165, SUBCELLULAR LOCATION, DNA-BINDING, AND INTERACTION
RP WITH STN1.
RX PubMed=19119139; DOI=10.1074/jbc.m807593200;
RA Casteel D.E., Zhuang S., Zeng Y., Perrino F.W., Boss G.R., Goulian M.,
RA Pilz R.B.;
RT "A DNA polymerase-{alpha}primase cofactor with homology to replication
RT protein A-32 regulates DNA replication in mammalian cells.";
RL J. Biol. Chem. 284:5807-5818(2009).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CST
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=19854130; DOI=10.1016/j.molcel.2009.08.009;
RA Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M., Yonehara S.,
RA Saito M., Ishikawa F.;
RT "RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and
RT protects telomeres independently of the Pot1 pathway.";
RL Mol. Cell 36:193-206(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=22748632; DOI=10.1016/j.cell.2012.05.026;
RA Wu P., Takai H., de Lange T.;
RT "Telomeric 3' overhangs derive from resection by Exo1 and Apollo and fill-
RT in by POT1b-associated CST.";
RL Cell 150:39-52(2012).
CC -!- FUNCTION: Component of the CST complex proposed to act as a specialized
CC replication factor promoting DNA replication under conditions of
CC replication stress or natural replication barriers such as the telomere
CC duplex. The CST complex binds single-stranded DNA with high affinity in
CC a sequence-independent manner, while isolated subunits bind DNA with
CC low affinity by themselves. Initially the CST complex has been proposed
CC to protect telomeres from DNA degradation (PubMed:19854130). However,
CC the CST complex has been shown to be involved in several aspects of
CC telomere replication. The CST complex inhibits telomerase and is
CC involved in telomere length homeostasis; it is proposed to bind to
CC newly telomerase-synthesized 3' overhangs and to terminate telomerase
CC action implicating the association with the ACD:POT1 complex thus
CC interfering with its telomerase stimulation activity. The CST complex
CC is also proposed to be involved in fill-in synthesis of the telomeric
CC C-strand probably implicating recruitment and activation of DNA
CC polymerase alpha. The CST complex facilitates recovery from many forms
CC of exogenous DNA damage; seems to be involved in the re-initiation of
CC DNA replication at repaired forks and/or dormant origins. Involved in
CC telomere maintenance. Involved in genome stability (By similarity). May
CC be in involved in telomeric C-strand fill-in during late S/G2 phase
CC (PubMed:22748632). {ECO:0000250|UniProtKB:Q2NKJ3,
CC ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22748632}.
CC -!- SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106,
CC CTC1/C17orf68 and STN1; in the complex interacts directly with STN1.
CC Interacts with ACD and POT1 (By similarity).
CC {ECO:0000250|UniProtKB:Q2NKJ3, ECO:0000269|PubMed:19119139,
CC ECO:0000269|PubMed:19854130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19119139,
CC ECO:0000269|PubMed:19854130}. Chromosome, telomere
CC {ECO:0000269|PubMed:19854130}. Note=A transmembrane region is predicted
CC by sequence analysis tools (ESKW, MEMSAT and Phobius); however, given
CC the telomeric localization of the protein, the relevance of the
CC transmembrane region is unsure in vivo. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SUQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SUQ9-2; Sequence=VSP_025355;
CC Name=3;
CC IsoId=Q5SUQ9-3; Sequence=VSP_025354;
CC -!- SIMILARITY: Belongs to the CTC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14687.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH60629.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC30081.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE26750.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE38452.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005190; BAB23872.1; -; mRNA.
DR EMBL; AK038651; BAC30081.1; ALT_INIT; mRNA.
DR EMBL; AK044055; BAC31756.1; -; mRNA.
DR EMBL; AK145919; BAE26750.1; ALT_INIT; mRNA.
DR EMBL; AK165906; BAE38452.1; ALT_INIT; mRNA.
DR EMBL; AL645902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014687; AAH14687.1; ALT_INIT; mRNA.
DR EMBL; BC060629; AAH60629.3; ALT_INIT; mRNA.
DR EMBL; BC147495; AAI47496.1; -; mRNA.
DR EMBL; BC147497; AAI47498.1; -; mRNA.
DR CCDS; CCDS36189.2; -. [Q5SUQ9-1]
DR CCDS; CCDS48824.1; -. [Q5SUQ9-2]
DR RefSeq; NP_001013274.2; NM_001013256.2. [Q5SUQ9-1]
DR RefSeq; NP_001137262.1; NM_001143790.1. [Q5SUQ9-2]
DR RefSeq; NP_001268394.1; NM_001281465.1. [Q5SUQ9-3]
DR AlphaFoldDB; Q5SUQ9; -.
DR SMR; Q5SUQ9; -.
DR BioGRID; 213143; 3.
DR ComplexPortal; CPX-2130; CST complex.
DR IntAct; Q5SUQ9; 3.
DR STRING; 10090.ENSMUSP00000112063; -.
DR iPTMnet; Q5SUQ9; -.
DR PhosphoSitePlus; Q5SUQ9; -.
DR EPD; Q5SUQ9; -.
DR jPOST; Q5SUQ9; -.
DR MaxQB; Q5SUQ9; -.
DR PaxDb; Q5SUQ9; -.
DR PeptideAtlas; Q5SUQ9; -.
DR PRIDE; Q5SUQ9; -.
DR ProteomicsDB; 285388; -. [Q5SUQ9-1]
DR ProteomicsDB; 285389; -. [Q5SUQ9-2]
DR ProteomicsDB; 285390; -. [Q5SUQ9-3]
DR Antibodypedia; 47974; 58 antibodies from 11 providers.
DR DNASU; 68964; -.
DR Ensembl; ENSMUST00000021278; ENSMUSP00000021278; ENSMUSG00000020898. [Q5SUQ9-2]
DR Ensembl; ENSMUST00000116359; ENSMUSP00000112063; ENSMUSG00000020898. [Q5SUQ9-1]
DR GeneID; 68964; -.
DR KEGG; mmu:68964; -.
DR UCSC; uc007jox.2; mouse. [Q5SUQ9-1]
DR UCSC; uc007joz.2; mouse. [Q5SUQ9-2]
DR CTD; 80169; -.
DR MGI; MGI:1916214; Ctc1.
DR VEuPathDB; HostDB:ENSMUSG00000020898; -.
DR eggNOG; ENOG502RBD3; Eukaryota.
DR GeneTree; ENSGT00390000011553; -.
DR HOGENOM; CLU_008170_0_0_1; -.
DR InParanoid; Q5SUQ9; -.
DR OMA; SMAGFIQ; -.
DR OrthoDB; 163417at2759; -.
DR PhylomeDB; Q5SUQ9; -.
DR TreeFam; TF335866; -.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR BioGRID-ORCS; 68964; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Ctc1; mouse.
DR PRO; PR:Q5SUQ9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SUQ9; protein.
DR Bgee; ENSMUSG00000020898; Expressed in ventricular zone and 263 other tissues.
DR ExpressionAtlas; Q5SUQ9; baseline and differential.
DR Genevisible; Q5SUQ9; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:1990879; C:CST complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:0048539; P:bone marrow development; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0090399; P:replicative senescence; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR InterPro; IPR029156; CTC1.
DR InterPro; IPR042617; CTC1-like.
DR PANTHER; PTHR14865; PTHR14865; 1.
DR Pfam; PF15489; CTC1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Direct protein sequencing; DNA-binding;
KW Nucleus; Reference proteome; Telomere.
FT CHAIN 1..1212
FT /note="CST complex subunit CTC1"
FT /id="PRO_0000287183"
FT VAR_SEQ 1..246
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025354"
FT VAR_SEQ 821
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025355"
FT CONFLICT 446
FT /note="Missing (in Ref. 1; BAC30081)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="K -> E (in Ref. 1; BAE26750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1144
FT /note="P -> H (in Ref. 1; BAE26750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1212 AA; 134028 MW; 4254E5B091CA5E1D CRC64;
MAACRAQPPT SEQAWLEAAQ TFIQETLCPA GKEVDKELTR SVIACVKETW LSQGENQDLT
LPFSYSFVSV QSLKTHQRLP CCSHLSWSQS AYQAWTRGGR PGDGVLPREQ LILLGTLVDL
LGDSEQECRS GSLYVRDNTG TLDCELIDLD LSWLGHLFLF PSWSYLPSAK RNSLGEGHLE
LWGTPVPVFP LTVSPGPLIP IPVLYPEKAS HLLRYRKKSS IKEINLAGKL VHLSALIITQ
NKRYFIMTLG ELAQAGSQVS IIVQIPAQMV WHRVLRPGRA YVLTKLQVTK TRIHLSCIWT
TIPSSTLKPL RPGYVQELEL DLEFSKADLK PPPQPTSSKD SRGQEGLVRA SKVLHYLGTV
TAVLHESAGL YILDGQLILC LAYQKIHGLR RVIRPGVCLE LRDVHLLQAV GGATTKPVLA
LCLHGTVRLQ GFSCLKPLTL PSSKVYGASL YEQLVWKCQL GLPLYLWAAK TLEDLIYKLC
PHVLRCHQFL KQPSPGKPSL GLQLLAPSWD VLIPPGSPMR HAYSEILEEP HNCPLQKYTP
LQTPYSFPTM LALAEEGQHR AWATFDPKAM LPLPEASHLT SCQLNRHLAW SWVCLPSCVF
QPAQVLLGVL VASSRKGCLE LRDLRGSLPC IPLTESSQPL IDPNLVGCLV RVEKFQLVVE
REVRSSFPSW EEMGMARFIQ KKQARVYVQF YLADALILPV PRPTFGSEPS QTASSCPEGP
HLGQSRLFLL SHKEALMKRN FCLLPGDSSQ PAKPTLSFHV SGTWLCGTQR KEGSGWSPPE
SLAVESKDQK VFLIFLGSSV RWFPFLYPNQ VYRLVASGPS QTPVFETEGS AGTSRRPLEL
ADCGSCLTVQ EEWTLELGSS QDIPNVLEVP RTLPESSLAQ LLGDNSPDSL VSFSAEILSR
ILCEPPLALR RMKPGNAGAI KTGVKLTVAL EMDDCEYPPH LDIYIEDPQL PPQIGLLPGA
RVHFSQLEKR ISRSNIVYCC FRSSTSVQVL SFPPETKASA PLPHIYLAEL LQGDRPPFQA
TTSCHIVYVL SLQILWVCAH CTSICPQGKC SRRDPSCPSQ RAVSQANIRL LVEDGTAEAT
VICRNHLVAR ALGLSPSEWS SILEHARGPG RVALQFTGLG GQTESASKTH EPLTLLLRTL
CTSPFVLRPV KLSFALERRP TDISPREPSR LQQFQCGELP LLTRVNPRLR LVCLSLQEPE
LPNPPQASAA SS
