TEN1L_MOUSE
ID TEN1L_MOUSE Reviewed; 161 AA.
AC Q9D7K2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=CST complex subunit TEN1;
DE AltName: Full=Protein telomeric pathways with STN1 homolog;
DE AltName: Full=Telomere length regulation protein TEN1 homolog;
GN Name=Ten1;
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].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Tongue;
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].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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).
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q86WV5,
CC ECO:0000269|PubMed:19854130}.
CC -!- SUBUNIT: Component of the CST complex, composed of TEN1, CTC1 and STN1;
CC in the complex interacts directly with STN1.
CC {ECO:0000269|PubMed:19854130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19854130}.
CC Chromosome, telomere {ECO:0000269|PubMed:19854130}.
CC -!- SIMILARITY: Belongs to the TEN1 family. {ECO:0000305}.
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DR EMBL; AK009156; BAB26112.1; -; mRNA.
DR EMBL; AK146257; BAE27018.1; -; mRNA.
DR EMBL; AL669925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027639; AAH27639.1; -; mRNA.
DR CCDS; CCDS48982.1; -.
DR RefSeq; NP_081383.1; NM_027107.1.
DR AlphaFoldDB; Q9D7K2; -.
DR SMR; Q9D7K2; -.
DR BioGRID; 213509; 8.
DR ComplexPortal; CPX-2130; CST complex.
DR IntAct; Q9D7K2; 8.
DR STRING; 10090.ENSMUSP00000021130; -.
DR EPD; Q9D7K2; -.
DR MaxQB; Q9D7K2; -.
DR PaxDb; Q9D7K2; -.
DR PeptideAtlas; Q9D7K2; -.
DR PRIDE; Q9D7K2; -.
DR ProteomicsDB; 263102; -.
DR Ensembl; ENSMUST00000021130; ENSMUSP00000021130; ENSMUSG00000020778.
DR GeneID; 69535; -.
DR KEGG; mmu:69535; -.
DR UCSC; uc007mkn.2; mouse.
DR CTD; 100134934; -.
DR MGI; MGI:1916785; Ten1.
DR VEuPathDB; HostDB:ENSMUSG00000020778; -.
DR eggNOG; ENOG502S4ES; Eukaryota.
DR GeneTree; ENSGT00390000017589; -.
DR HOGENOM; CLU_139244_0_0_1; -.
DR InParanoid; Q9D7K2; -.
DR OMA; ILTCVEG; -.
DR OrthoDB; 1496976at2759; -.
DR PhylomeDB; Q9D7K2; -.
DR TreeFam; TF333010; -.
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; 69535; 11 hits in 74 CRISPR screens.
DR PRO; PR:Q9D7K2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D7K2; protein.
DR Bgee; ENSMUSG00000020778; Expressed in lip and 243 other tissues.
DR Genevisible; Q9D7K2; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:1990879; C:CST complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0010521; F:telomerase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029146; Ten1_animal_plant.
DR PANTHER; PTHR33905; PTHR33905; 1.
DR Pfam; PF15490; Ten1_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..161
FT /note="CST complex subunit TEN1"
FT /id="PRO_0000392993"
FT DNA_BIND 1..120
FT /note="OB"
FT REGION 119..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 161 AA; 18066 MW; 4DACAD9187388A33 CRC64;
MLPKPGVYYF PWEVSDGHVP EGSTLRTFGR LYLYDMARSL MTLAAPQKPD QCQLLVCTNL
VEPFEAHVNF LYMVLGDLER MEGGAFVVRA RLLTCVEGMD LSLLEKAILE QRRHLQKRQQ
PIGDASTLQT PTPAPQSIPS DSLSLEPENR GQQVPLPQTL D
