STN1_DANRE
ID STN1_DANRE Reviewed; 368 AA.
AC B8JKF4; Q7T311;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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;
GN ORFNames=dkey-100g3.3, zgc:64174;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=27432940; DOI=10.1084/jem.20151618;
RA Simon A.J., Lev A., Zhang Y., Weiss B., Rylova A., Eyal E., Kol N.,
RA Barel O., Cesarkas K., Soudack M., Greenberg-Kushnir N., Rhodes M.,
RA Wiest D.L., Schiby G., Barshack I., Katz S., Pras E., Poran H.,
RA Reznik-Wolf H., Ribakovsky E., Simon C., Hazou W., Sidi Y., Lahad A.,
RA Katzir H., Sagie S., Aqeilan H.A., Glousker G., Amariglio N., Tzfati Y.,
RA Selig S., Rechavi G., Somech R.;
RT "Mutations in STN1 cause Coats plus syndrome and are associated with
RT genomic and telomere defects.";
RL J. Exp. Med. 213:1429-1440(2016).
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 {ECO:0000250|UniProtKB:Q9H668}.
CC -!- SUBUNIT: Component of the CST complex. {ECO:0000250|UniProtKB:Q9H668}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H668}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q9H668}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown in embryos results in
CC decreased red blood cells and an arrest in T-cell progenitors, as well
CC as increased vascularity. The vascular defects could be rescued by
CC wild-type gene and by thalidomide treatment.
CC {ECO:0000269|PubMed:27432940}.
CC -!- SIMILARITY: Belongs to the CTC1 family. {ECO:0000305}.
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DR EMBL; CT737229; CAX12853.1; -; Genomic_DNA.
DR EMBL; BC053298; AAH53298.1; -; mRNA.
DR RefSeq; NP_956683.1; NM_200389.1.
DR AlphaFoldDB; B8JKF4; -.
DR SMR; B8JKF4; -.
DR STRING; 7955.ENSDARP00000013967; -.
DR PaxDb; B8JKF4; -.
DR Ensembl; ENSDART00000027624; ENSDARP00000013967; ENSDARG00000007734.
DR GeneID; 393360; -.
DR KEGG; dre:393360; -.
DR CTD; 79991; -.
DR ZFIN; ZDB-GENE-040426-1390; stn1.
DR eggNOG; KOG3108; Eukaryota.
DR GeneTree; ENSGT00390000000909; -.
DR HOGENOM; CLU_063889_0_0_1; -.
DR InParanoid; B8JKF4; -.
DR OMA; LCWKDEK; -.
DR OrthoDB; 1451022at2759; -.
DR PhylomeDB; B8JKF4; -.
DR TreeFam; TF328623; -.
DR Reactome; R-DRE-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-DRE-174430; Telomere C-strand synthesis initiation.
DR PRO; PR:B8JKF4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000007734; Expressed in mature ovarian follicle and 24 other tissues.
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: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 GO; GO:0001944; P:vasculature development; IMP:ZFIN.
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..368
FT /note="CST complex subunit STN1"
FT /id="PRO_0000392989"
FT DNA_BIND 58..162
FT /note="OB"
FT REGION 2..192
FT /note="Interaction with CTC1"
FT /evidence="ECO:0000250|UniProtKB:Q9H668"
FT REGION 201..295
FT /note="Winged helix-turn-helix (wHTH) 1"
FT /evidence="ECO:0000250"
FT REGION 296..368
FT /note="Winged helix-turn-helix (wHTH) 2"
FT /evidence="ECO:0000250"
FT CONFLICT 128
FT /note="R -> L (in Ref. 2; AAH53298)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> C (in Ref. 2; AAH53298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 42230 MW; E5E5106150C81A80 CRC64;
MAVSLGDDDA DELPSMLWGL DPVFSSYCRL YITDILLMKE SRQVPGIYFY KTHPIFQVDV
LGIVVYKRER EDFYCYGVDD STGVINCLCW KDEKWRDQGG STTCGDASGF PRSFNIEDEL
KGLKEAERKS TVLEIGDLLR VRGTVKTSRD NREIKATSFY KVHDPAMAVQ ISRMLELPQL
YRKCYDQPFK MPSDDLGSTE AGGSSHPQYL LSRAVLTLKE FLLEKEVTRF RPYDVEFLLH
PLIQRSSAEQ EADQPGTSFA TQVGKLLKET LSFLQDEGQI FRKKRTQDEV YNVTEQDKDL
HIAIKDVLRE DTKREKYAEK GCHVLHILSS VRQRYSQNLS REVLEVALTF LESNSDIIST
TEAHYIVL