ID   STN1_BOVIN              Reviewed;         370 AA.
AC   Q08DB2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) 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. 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; BC123847; AAI23848.1; -; mRNA.
DR   RefSeq; NP_001070317.1; NM_001076849.1.
DR   AlphaFoldDB; Q08DB2; -.
DR   SMR; Q08DB2; -.
DR   STRING; 9913.ENSBTAP00000019995; -.
DR   PaxDb; Q08DB2; -.
DR   PRIDE; Q08DB2; -.
DR   Ensembl; ENSBTAT00000019995; ENSBTAP00000019995; ENSBTAG00000015019.
DR   Ensembl; ENSBTAT00000070266; ENSBTAP00000059546; ENSBTAG00000015019.
DR   GeneID; 514213; -.
DR   KEGG; bta:514213; -.
DR   CTD; 79991; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015019; -.
DR   VGNC; VGNC:35408; STN1.
DR   eggNOG; KOG3108; Eukaryota.
DR   GeneTree; ENSGT00390000000909; -.
DR   HOGENOM; CLU_063889_0_0_1; -.
DR   InParanoid; Q08DB2; -.
DR   OMA; LCWKDEK; -.
DR   OrthoDB; 1451022at2759; -.
DR   TreeFam; TF328623; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000015019; Expressed in cortex of kidney and 106 other tissues.
DR   ExpressionAtlas; Q08DB2; baseline and differential.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR   GO; GO:1990879; C:CST complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; 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; IPR040260; RFA2-like.
DR   InterPro; IPR014647; Stn1.
DR   InterPro; IPR018856; Stn1_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13989; PTHR13989; 1.
DR   Pfam; PF10451; Stn1; 1.
DR   Pfam; PF09170; STN1_2; 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..370
FT                   /note="CST complex subunit STN1"
FT                   /id="PRO_0000392987"
FT   DNA_BIND        57..157
FT                   /note="OB"
FT   REGION          1..187
FT                   /note="Interaction with CTC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H668"
FT   REGION          193..297
FT                   /note="Winged helix-turn-helix (wHTH) 1"
FT                   /evidence="ECO:0000250"
FT   REGION          298..370
FT                   /note="Winged helix-turn-helix (wHTH) 2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  41936 MW;  F530DF73E7E85BA6 CRC64;
     MESNSSQCED ETPSLLWGLD PVFLAFAKLY IRDILDLKES GQVQGVFFYN GHPIKQVDIL
     GTVIGVREKD AFYSYGVDDS TGVINCICWK RLNNTKSSSA TATPSARELS LTSQLKKLQE
     TIAQRAKLEI GDIIRVRGHI RMFRGEREIH ATTYYKVDDP VCNVQIARML ELPAIYRKVY
     DQPFHSPALK EDEALSNPGT LDLDSLTCLL SEKAKEFLVE NRVQSFYQQE LETVESLLSL
     ANQPVIHSAC SGQMGFKNDT TSRAIHSIFR NAVKLLQEEG LVFQKDGGFD NLFYVTREDK
     ELHRKIHRII QEECQKPNHV EKGCHFLHIL ACARLSLSPG LSEPVLQQVL QLLEDQSDIV
     STTEKYYTAF