TEN1L_HUMAN
ID TEN1L_HUMAN Reviewed; 123 AA.
AC Q86WV5; I3L0C7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
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; Synonyms=C17orf106;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma, and Uterus;
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 [5]
RP FUNCTION, IDENTIFICATION IN THE CST COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH STN1.
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 FUNCTION OF THE CST COMPLEX.
RX PubMed=22863775; DOI=10.1038/emboj.2012.215;
RA Stewart J.A., Wang F., Chaiken M.F., Kasbek C., Chastain P.D. II,
RA Wright W.E., Price C.M.;
RT "Human CST promotes telomere duplex replication and general replication
RT restart after fork stalling.";
RL EMBO J. 31:3537-3549(2012).
RN [7]
RP FUNCTION OF THE CST COMPLEX.
RX PubMed=22763445; DOI=10.1038/nature11269;
RA Chen L.Y., Redon S., Lingner J.;
RT "The human CST complex is a terminator of telomerase activity.";
RL Nature 488:540-544(2012).
RN [8]
RP FUNCTION OF THE CST COMPLEX.
RX PubMed=25483097; DOI=10.4161/15384101.2014.964100;
RA Wang F., Stewart J., Price C.M.;
RT "Human CST abundance determines recovery from diverse forms of DNA damage
RT and replication stress.";
RL Cell Cycle 13:3488-3498(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-123 IN COMPLEX WITH STN1, OB
RP FOLD DNA-BINDING, AND MUTAGENESIS OF TYR-115 AND ARG-119.
RX PubMed=23826127; DOI=10.1371/journal.pone.0066756;
RA Bryan C., Rice C., Harkisheimer M., Schultz D.C., Skordalakes E.;
RT "Structure of the human telomeric Stn1-Ten1 capping complex.";
RL PLoS ONE 8:E66756-E66756(2013).
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 (PubMed:22763445). The CST complex facilitates
CC recovery from many forms of exogenous DNA damage; seems to be involved
CC in the re-initiation of DNA replication at repaired forks and/or
CC dormant origins (PubMed:25483097). {ECO:0000269|PubMed:19854130,
CC ECO:0000269|PubMed:22763445, ECO:0000269|PubMed:25483097}.
CC -!- SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106,
CC CTC1/C17orf68 and STN1; in the complex interacts directly with STN1.
CC {ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:23826127}.
CC -!- INTERACTION:
CC Q86WV5; P46379-2: BAG6; NbExp=3; IntAct=EBI-2562799, EBI-10988864;
CC Q86WV5; P55212: CASP6; NbExp=3; IntAct=EBI-2562799, EBI-718729;
CC Q86WV5; Q2NKJ3: CTC1; NbExp=3; IntAct=EBI-2562799, EBI-2562802;
CC Q86WV5; P22607: FGFR3; NbExp=3; IntAct=EBI-2562799, EBI-348399;
CC Q86WV5; Q14957: GRIN2C; NbExp=3; IntAct=EBI-2562799, EBI-8285963;
CC Q86WV5; P04792: HSPB1; NbExp=3; IntAct=EBI-2562799, EBI-352682;
CC Q86WV5; O43464: HTRA2; NbExp=3; IntAct=EBI-2562799, EBI-517086;
CC Q86WV5; P42858: HTT; NbExp=9; IntAct=EBI-2562799, EBI-466029;
CC Q86WV5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2562799, EBI-10975473;
CC Q86WV5; O14901: KLF11; NbExp=3; IntAct=EBI-2562799, EBI-948266;
CC Q86WV5; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2562799, EBI-21591415;
CC Q86WV5; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2562799, EBI-2811583;
CC Q86WV5; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2562799, EBI-5280197;
CC Q86WV5; P41219: PRPH; NbExp=3; IntAct=EBI-2562799, EBI-752074;
CC Q86WV5; P60891: PRPS1; NbExp=3; IntAct=EBI-2562799, EBI-749195;
CC Q86WV5; P62826: RAN; NbExp=3; IntAct=EBI-2562799, EBI-286642;
CC Q86WV5; Q9H668: STN1; NbExp=11; IntAct=EBI-2562799, EBI-746930;
CC Q86WV5; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2562799, EBI-741480;
CC Q86WV5; Q9Y649; NbExp=3; IntAct=EBI-2562799, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19854130}.
CC Chromosome, telomere {ECO:0000269|PubMed:19854130}.
CC -!- SIMILARITY: Belongs to the TEN1 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator. Some
CC orthologous sequences cannot be extended. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47782.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK097104; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX647274; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC040980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047782; AAH47782.1; ALT_INIT; mRNA.
DR EMBL; BM558420; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS45780.2; -.
DR RefSeq; NP_001106795.2; NM_001113324.2.
DR PDB; 4JOI; X-ray; 2.05 A; C/D=2-123.
DR PDB; 6W6W; EM; 3.00 A; D=3-123.
DR PDBsum; 4JOI; -.
DR PDBsum; 6W6W; -.
DR AlphaFoldDB; Q86WV5; -.
DR SMR; Q86WV5; -.
DR BioGRID; 756076; 6.
DR ComplexPortal; CPX-2129; CST complex.
DR CORUM; Q86WV5; -.
DR DIP; DIP-56901N; -.
DR IntAct; Q86WV5; 20.
DR STRING; 9606.ENSP00000380762; -.
DR BioMuta; TEN1; -.
DR EPD; Q86WV5; -.
DR jPOST; Q86WV5; -.
DR MassIVE; Q86WV5; -.
DR MaxQB; Q86WV5; -.
DR PaxDb; Q86WV5; -.
DR PeptideAtlas; Q86WV5; -.
DR PRIDE; Q86WV5; -.
DR ProteomicsDB; 46327; -.
DR ProteomicsDB; 70210; -.
DR Antibodypedia; 49436; 6 antibodies from 4 providers.
DR DNASU; 100134934; -.
DR Ensembl; ENST00000397640.6; ENSP00000380762.1; ENSG00000257949.7.
DR GeneID; 100134934; -.
DR KEGG; hsa:100134934; -.
DR MANE-Select; ENST00000397640.6; ENSP00000380762.1; NM_001113324.3; NP_001106795.2.
DR UCSC; uc060kgd.1; human.
DR CTD; 100134934; -.
DR DisGeNET; 100134934; -.
DR GeneCards; TEN1; -.
DR HGNC; HGNC:37242; TEN1.
DR HPA; ENSG00000257949; Low tissue specificity.
DR MIM; 613130; gene.
DR neXtProt; NX_Q86WV5; -.
DR OpenTargets; ENSG00000257949; -.
DR PharmGKB; PA165431550; -.
DR VEuPathDB; HostDB:ENSG00000257949; -.
DR eggNOG; ENOG502S4ES; Eukaryota.
DR GeneTree; ENSGT00390000017589; -.
DR HOGENOM; CLU_139244_0_0_1; -.
DR InParanoid; Q86WV5; -.
DR OMA; ILTCVEG; -.
DR OrthoDB; 1496976at2759; -.
DR PhylomeDB; Q86WV5; -.
DR TreeFam; TF333010; -.
DR PathwayCommons; Q86WV5; -.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-174430; Telomere C-strand synthesis initiation.
DR SignaLink; Q86WV5; -.
DR BioGRID-ORCS; 100134934; 357 hits in 1082 CRISPR screens.
DR ChiTaRS; TEN1; human.
DR GenomeRNAi; 100134934; -.
DR Pharos; Q86WV5; Tbio.
DR PRO; PR:Q86WV5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q86WV5; protein.
DR Bgee; ENSG00000257949; Expressed in lower esophagus mucosa and 92 other tissues.
DR ExpressionAtlas; Q86WV5; baseline and differential.
DR Genevisible; Q86WV5; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:1990879; C:CST complex; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0016233; P:telomere capping; TAS:BHF-UCL.
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 3D-structure; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..123
FT /note="CST complex subunit TEN1"
FT /id="PRO_0000334683"
FT DNA_BIND 2..123
FT /note="OB"
FT MUTAGEN 115
FT /note="Y->A: 2.5-fold reduction in binding affinity for
FT STN1."
FT /evidence="ECO:0000269|PubMed:23826127"
FT MUTAGEN 119
FT /note="R->Q: 2-fold reduction in binding affinity for
FT STN1."
FT /evidence="ECO:0000269|PubMed:23826127"
FT CONFLICT 46
FT /note="A -> S (in Ref. 4; BM558420)"
FT /evidence="ECO:0000305"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:4JOI"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:4JOI"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4JOI"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:4JOI"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:4JOI"
SQ SEQUENCE 123 AA; 13856 MW; C713E9B40C2A5E34 CRC64;
MMLPKPGTYY LPWEVSAGQV PDGSTLRTFG RLCLYDMIQS RVTLMAQHGS DQHQVLVCTK
LVEPFHAQVG SLYIVLGELQ HQQDRGSVVK ARVLTCVEGM NLPLLEQAIR EQRLYKQERG
GSQ
