STN1_RAT
ID STN1_RAT Reviewed; 408 AA.
AC Q6AYD2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=CST complex subunit STN1 {ECO:0000250|UniProtKB:Q9H668};
DE AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 1;
DE AltName: Full=Suppressor of cdc thirteen homolog;
GN Name=Stn1 {ECO:0000250|UniProtKB:Q9H668}; Synonyms=Obfc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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. Required for efficicient
CC replication of the duplex region of the telomere. Promotes efficient
CC replication of lagging-strand telomeres. Promotes general replication
CC start following replication-fork stalling implicating new origin
CC firing. May be in involved in C-strand fill-in during late S/G2 phase
CC independent of its role in telomere duplex replication (By similarity).
CC {ECO:0000250|UniProtKB:Q9H668}.
CC -!- SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106,
CC CTC1/C17orf68 and STN1; in the complex interacts directly with TEN1 and
CC CTC1. Interacts with ACD/TPP1, POT1 and POLA1.
CC {ECO:0000250|UniProtKB:Q9H668}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H668}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q9H668}.
CC -!- SIMILARITY: Belongs to the STN1 family. {ECO:0000305}.
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DR EMBL; BC079096; AAH79096.1; -; mRNA.
DR RefSeq; NP_001011943.1; NM_001011943.1.
DR AlphaFoldDB; Q6AYD2; -.
DR SMR; Q6AYD2; -.
DR BioGRID; 254548; 1.
DR STRING; 10116.ENSRNOP00000027614; -.
DR PaxDb; Q6AYD2; -.
DR PRIDE; Q6AYD2; -.
DR GeneID; 294025; -.
DR KEGG; rno:294025; -.
DR UCSC; RGD:1305637; rat.
DR CTD; 79991; -.
DR RGD; 1305637; Stn1.
DR eggNOG; KOG3108; Eukaryota.
DR HOGENOM; CLU_063889_0_0_1; -.
DR InParanoid; Q6AYD2; -.
DR OrthoDB; 1451022at2759; -.
DR PhylomeDB; Q6AYD2; -.
DR TreeFam; TF328623; -.
DR Reactome; R-RNO-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-RNO-174430; Telomere C-strand synthesis initiation.
DR PRO; PR:Q6AYD2; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q6AYD2; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:1990879; C:CST complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:RGD.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0016233; P:telomere capping; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.980; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR015253; CST_STN1_C.
DR InterPro; IPR042082; CST_Stn1_wHTH1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014647; Stn1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989; PTHR13989; 1.
DR Pfam; PF09170; STN1_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF036950; UCP036950; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..408
FT /note="CST complex subunit STN1"
FT /id="PRO_0000058022"
FT DNA_BIND 64..165
FT /note="OB"
FT REGION 8..195
FT /note="Interaction with CTC1"
FT /evidence="ECO:0000250|UniProtKB:Q9H668"
FT REGION 201..304
FT /note="Winged helix-turn-helix (wHTH) 1"
FT /evidence="ECO:0000250"
FT REGION 305..408
FT /note="Winged helix-turn-helix (wHTH) 1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 46783 MW; 068A9917A691ADA9 CRC64;
MPEPCLLMQC ESSPKEEEIP SLFWGLDPVF LAFAKLYIKD ILEMKESQQV PGMYFYNGHP
IRRVDIMGAV ISVKERETFY SYGVDDATGV INCVCWKRPS NAESSSDPAI LSTSRELSMT
SQLKKLQETI EQKTKIGIGD IIRVRGYVRM FREEREICAT IYYKVDDPVW NMQIARMLEL
PELYKKVYDQ PFRNPALKEE EALNSKDTLD LAGLTALLSE KVKEFLQEKK VQSFYQKELE
MVEPLQSLAS QPVTHSTCSD QVELKNDAAS DIHSVFKNAL HLLQEKGFVF QRDGGSDKLY
YVTSKDKDLH QKIYQIIKED CQKPNLWCML PQEAWRGTEE GLAVVVTLSV CLPLPVDVEK
GCHLMHVLNC VLLNLRWDLN KAVLQQVLEL LEDQSDIVST GDHYYTAF
