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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
 
 
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