ID   CTC1_PONAB              Reviewed;        1217 AA.
AC   Q5RDX3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=CST complex subunit CTC1;
DE   AltName: Full=Conserved telomere maintenance component 1;
GN   Name=CTC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. However, the CST complex has
CC       been shown to be involved in several aspects of telomere replication.
CC       The CST complex inhibits telomerase and is involved in telomere length
CC       homeostasis; it is proposed to bind to newly telomerase-synthesized 3'
CC       overhangs and to terminate telomerase action implicating the
CC       association with the ACD:POT1 complex thus interfering with its
CC       telomerase stimulation activity. The CST complex is also proposed to be
CC       involved in fill-in synthesis of the telomeric C-strand probably
CC       implicating recruitment and activation of DNA polymerase alpha. The CST
CC       complex facilitates recovery from many forms of exogenous DNA damage;
CC       seems to be involved in the re-initiation of DNA replication at
CC       repaired forks and/or dormant origins. Involved in telomere
CC       maintenance. Involved in genome stability (By similarity). May be in
CC       involved in telomeric C-strand fill-in during late S/G2 phase (By
CC       similarity). {ECO:0000250|UniProtKB:Q2NKJ3,
CC       ECO:0000250|UniProtKB:Q5SUQ9}.
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:0000250|UniProtKB:Q5SUQ9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2NKJ3,
CC       ECO:0000250|UniProtKB:Q5SUQ9}. Chromosome, telomere
CC       {ECO:0000250|UniProtKB:Q2NKJ3, ECO:0000250|UniProtKB:Q5SUQ9}. Note=A
CC       transmembrane region is predicted by sequence analysis tools (ESKW,
CC       MEMSAT and Phobius); however, given the telomeric localization of the
CC       protein, the relevance of the transmembrane region is unsure in vivo.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CTC1 family. {ECO:0000305}.
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DR   EMBL; CR857769; CAH90034.1; -; mRNA.
DR   RefSeq; NP_001124551.1; NM_001131079.1.
DR   AlphaFoldDB; Q5RDX3; -.
DR   SMR; Q5RDX3; -.
DR   STRING; 9601.ENSPPYP00000008942; -.
DR   GeneID; 100127094; -.
DR   KEGG; pon:100127094; -.
DR   CTD; 80169; -.
DR   eggNOG; ENOG502RBD3; Eukaryota.
DR   InParanoid; Q5RDX3; -.
DR   OrthoDB; 163417at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR   InterPro; IPR029156; CTC1.
DR   InterPro; IPR042617; CTC1-like.
DR   PANTHER; PTHR14865; PTHR14865; 1.
DR   Pfam; PF15489; CTC1; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT   CHAIN           1..1217
FT                   /note="CST complex subunit CTC1"
FT                   /id="PRO_0000287182"
FT   REGION          327..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1217 AA;  134637 MW;  21ADB9362F7F5C02 CRC64;
     MAAGRAQVPS SEQAWLEDAQ VFIQKTLCPA VKEPNVQLTP LIIDCVKTVW LSQGRNQGST
     LPLSYSFVSV QDLKTHQRLP CCSHLSWSSS AYQAWAQEAG PNGNPLPREQ LLLLGTLTDL
     SADLEQECRN GSLYVRDNTG VLSCELIDLD LSWLGHLFLF PCWSYLPPAR WNSSGEGHLE
     LWDAPVPVFP LTVSPGPVTP IPVLYPESAS RLLRLRNKLR GVQRNLAGNL VRLSALVKSK
     QKAYFILSLG RSHPAVTHVS VIVQVPAQLV WHRVLRPGTA YVLTELRVSK IRGQRQHVWM
     TSQSSRLLLL KPECVQELEL ELEGPLLEAD PKPLPTPSNS EDKKDPEGLA RYSRLLSYSG
     AVTGVLNEPA GLYELDGQLG LCLAYQQFRG LRRVMRPGVC LQLQDVHLLQ SVGGGTRRPV
     LAPCLRGAVL LQSFSRQKPG THSSRQAYGA SLYEQLVWER QLGLPLYLWA TKALEELAGK
     LCPHVLRHHQ FLQHSSPGSP SLGLQLLVPT LDLLAPPGSP VRNAHNEILE EPHHCPLQKY
     TRLQTPSSFP TLAALKEEGQ REAWASFDPE ALLPLPEASH LPSCQLNRHL AWSWLCLLPS
     AFHPAQVLLG VLVASSHKGC LQLRDQSGSL PCLLLAKHSQ PLSDPRLIGC LVRAERFQLI
     VERDVRSSFP SWKELSMPGF IQKQQARVYV QFFLADALIL PVPRPSLHSA TPSTPQTDPT
     GPEGPHLGQS RLFLLCHKEA LMKRNFCVPP GASPEVPKPV LSFCVLGSWL GGTQRKEGTG
     WGLPEPQGND DKDQKVHLIF FGSSVRWFEF LHPGQVYRLV APGPPTPMLF EKDGSSCISR
     RPLELAGCAS CLTVQDNWTL ELESSQDIQD VLDANKALPE SSLTDLLSDN FTDSLVSFSA
     EILSRTLCEP LVASLWMKLG NTGTMRRCVK LTVALETAEC EFPPHLDVYI EDPHLPPSLG
     LLPGARVHFS QLEKRVSRSH NVYCCFRSST YVQVLSFPPE TTISIPLPHI YLAELRQGGQ
     SPFQATTSCH IVSVFSLQLF WVCAYCTSIC RQGKCTRLGP TCPTQTAVSQ AIIRLLVEDG
     TAEAVVTCRN HHVAAALGLC PREWASLLEF VRVPGRVVLQ FAGPGAQLES SARVDKPMTM
     FLWTLCTSPS VLRPIVLSFE LERKPSKIVP LEPPRLQRFQ CGELPFLTHV NPRLRLSCLS
     IRESEYSSSL GILASSC