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CST complex subunit CTC1 (Alpha-accessory factor of 132 kDa) (AAF-132) (AAF132) (Conserved telomere maintenance component 1)

 CTC1_MOUSE              Reviewed;        1212 AA.
Q5SUQ9; B2RW14; Q3UKQ1; Q6P9S2; Q8BRK2; Q91WN0; Q9CW32;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 2.
12-SEP-2018, entry version 97.
RecName: Full=CST complex subunit CTC1;
AltName: Full=Alpha-accessory factor of 132 kDa;
Short=AAF-132;
Short=AAF132;
AltName: Full=Conserved telomere maintenance component 1;
Name=Ctc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, Lung, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 244-1211 (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 98-108; 110-127; 561-568; 814-832; 962-968;
1090-1106; 1111-1137 AND 1159-1165, SUBCELLULAR LOCATION, DNA-BINDING,
AND INTERACTION WITH STN1.
PubMed=19119139; DOI=10.1074/jbc.M807593200;
Casteel D.E., Zhuang S., Zeng Y., Perrino F.W., Boss G.R., Goulian M.,
Pilz R.B.;
"A DNA polymerase-{alpha}primase cofactor with homology to replication
protein A-32 regulates DNA replication in mammalian cells.";
J. Biol. Chem. 284:5807-5818(2009).
[5]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
CST COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=19854130; DOI=10.1016/j.molcel.2009.08.009;
Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M.,
Yonehara S., Saito M., Ishikawa F.;
"RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
DNA and protects telomeres independently of the Pot1 pathway.";
Mol. Cell 36:193-206(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION.
PubMed=22748632; DOI=10.1016/j.cell.2012.05.026;
Wu P., Takai H., de Lange T.;
"Telomeric 3' overhangs derive from resection by Exo1 and Apollo and
fill-in by POT1b-associated CST.";
Cell 150:39-52(2012).
-!- FUNCTION: Component of the CST complex proposed to act as a
specialized replication factor promoting DNA replication under
conditions of replication stress or natural replication barriers
such as the telomere duplex. The CST complex binds single-stranded
DNA with high affinity in a sequence-independent manner, while
isolated subunits bind DNA with low affinity by themselves.
Initially the CST complex has been proposed to protect telomeres
from DNA degradation (PubMed:19854130). However, the CST complex
has been shown to be involved in several aspects of telomere
replication. The CST complex inhibits telomerase and is involved
in telomere length homeostasis; it is proposed to bind to newly
telomerase-synthesized 3' overhangs and to terminate telomerase
action implicating the association with the ACD:POT1 complex thus
interfering with its telomerase stimulation activity. The CST
complex is also proposed to be involved in fill-in synthesis of
the telomeric C-strand probably implicating recruitment and
activation of DNA polymerase alpha. The CST complex facilitates
recovery from many forms of exogenous DNA damage; seems to be
involved in the re-initiation of DNA replication at repaired forks
and/or dormant origins. Involved in telomere maintenance. Involved
in genome stability (By similarity). May be in involved in
telomeric C-strand fill-in during late S/G2 phase
(PubMed:22748632). {ECO:0000250|UniProtKB:Q2NKJ3,
ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22748632}.
-!- SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106,
CTC1/C17orf68 and STN1; in the complex interacts directly with
STN1. Interacts with ACD and POT1 (By similarity).
{ECO:0000250|UniProtKB:Q2NKJ3, ECO:0000269|PubMed:19119139,
ECO:0000269|PubMed:19854130}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19119139,
ECO:0000269|PubMed:19854130}. Chromosome, telomere
{ECO:0000269|PubMed:19854130}. Note=A transmembrane region is
predicted by sequence analysis tools (ESKW, MEMSAT and Phobius);
however, given the telomeric localization of the protein, the
relevance of the transmembrane region is unsure in vivo.
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5SUQ9-1; Sequence=Displayed;
Name=2;
IsoId=Q5SUQ9-2; Sequence=VSP_025355;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q5SUQ9-3; Sequence=VSP_025354;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the CTC1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH14687.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH60629.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC30081.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE26750.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE38452.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK005190; BAB23872.1; -; mRNA.
EMBL; AK038651; BAC30081.1; ALT_INIT; mRNA.
EMBL; AK044055; BAC31756.1; -; mRNA.
EMBL; AK145919; BAE26750.1; ALT_INIT; mRNA.
EMBL; AK165906; BAE38452.1; ALT_INIT; mRNA.
EMBL; AL645902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014687; AAH14687.1; ALT_INIT; mRNA.
EMBL; BC060629; AAH60629.3; ALT_INIT; mRNA.
EMBL; BC147495; AAI47496.1; -; mRNA.
EMBL; BC147497; AAI47498.1; -; mRNA.
CCDS; CCDS36189.2; -. [Q5SUQ9-1]
CCDS; CCDS48824.1; -. [Q5SUQ9-2]
RefSeq; NP_001013274.2; NM_001013256.2. [Q5SUQ9-1]
RefSeq; NP_001137262.1; NM_001143790.1. [Q5SUQ9-2]
RefSeq; NP_001268394.1; NM_001281465.1. [Q5SUQ9-3]
UniGene; Mm.285785; -.
SMR; Q5SUQ9; -.
ComplexPortal; CPX-2130; CST complex.
IntAct; Q5SUQ9; 3.
STRING; 10090.ENSMUSP00000112063; -.
iPTMnet; Q5SUQ9; -.
PhosphoSitePlus; Q5SUQ9; -.
EPD; Q5SUQ9; -.
PaxDb; Q5SUQ9; -.
PeptideAtlas; Q5SUQ9; -.
PRIDE; Q5SUQ9; -.
Ensembl; ENSMUST00000021278; ENSMUSP00000021278; ENSMUSG00000020898. [Q5SUQ9-2]
Ensembl; ENSMUST00000116359; ENSMUSP00000112063; ENSMUSG00000020898. [Q5SUQ9-1]
GeneID; 68964; -.
KEGG; mmu:68964; -.
UCSC; uc007jox.2; mouse. [Q5SUQ9-1]
UCSC; uc007joz.2; mouse. [Q5SUQ9-2]
CTD; 80169; -.
MGI; MGI:1916214; Ctc1.
eggNOG; ENOG410IGVR; Eukaryota.
eggNOG; ENOG410Y8V3; LUCA.
GeneTree; ENSGT00390000011553; -.
HOVERGEN; HBG097256; -.
InParanoid; Q5SUQ9; -.
OMA; FELERKP; -.
OrthoDB; EOG091G0VEW; -.
PhylomeDB; Q5SUQ9; -.
TreeFam; TF335866; -.
ChiTaRS; Ctc1; mouse.
PRO; PR:Q5SUQ9; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020898; Expressed in 278 organ(s), highest expression level in embryonic stem cell.
CleanEx; MM_1500010J02RIK; -.
ExpressionAtlas; Q5SUQ9; baseline and differential.
Genevisible; Q5SUQ9; MM.
GO; GO:1990879; C:CST complex; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
GO; GO:0007568; P:aging; IMP:MGI.
GO; GO:0048539; P:bone marrow development; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0051276; P:chromosome organization; IMP:MGI.
GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
GO; GO:0090399; P:replicative senescence; IMP:MGI.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
InterPro; IPR029156; CTC1.
Pfam; PF15489; CTC1; 1.
1: Evidence at protein level;
Alternative splicing; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Nucleus; Reference proteome;
Telomere.
CHAIN 1 1212 CST complex subunit CTC1.
/FTId=PRO_0000287183.
VAR_SEQ 1 246 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025354.
VAR_SEQ 821 821 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_025355.
CONFLICT 446 446 Missing (in Ref. 1; BAC30081).
{ECO:0000305}.
CONFLICT 969 969 K -> E (in Ref. 1; BAE26750).
{ECO:0000305}.
CONFLICT 1144 1144 P -> H (in Ref. 1; BAE26750).
{ECO:0000305}.
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


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