STN1_MOUSE
ID STN1_MOUSE Reviewed; 378 AA.
AC Q8K2X3; Q3TPH0; Q8C6I6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=CST complex subunit STN1 {ECO:0000250|UniProtKB:Q9H668};
DE AltName: Full=Alpha-accessory factor of 44 kDa;
DE Short=AAF-44;
DE Short=AAF44;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [4]
RP PROTEIN SEQUENCE OF 2-9; 136-143; 157-164; 166-176; 197-221 AND 357-375,
RP SUBCELLULAR LOCATION, INTERACTION WITH CTC1, DNA-BINDING, AND MUTAGENESIS
RP OF TRP-96 AND PHE-151.
RX PubMed=19119139; DOI=10.1074/jbc.m807593200;
RA Casteel D.E., Zhuang S., Zeng Y., Perrino F.W., Boss G.R., Goulian M.,
RA Pilz R.B.;
RT "A DNA polymerase-{alpha}primase cofactor with homology to replication
RT protein A-32 regulates DNA replication in mammalian cells.";
RL J. Biol. Chem. 284:5807-5818(2009).
RN [5]
RP INTERACTION WITH ACD.
RX PubMed=19648609; DOI=10.1074/jbc.m109.021105;
RA Wan M., Qin J., Songyang Z., Liu D.;
RT "OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1,
RT associates with TPP1 and is implicated in telomere length regulation.";
RL J. Biol. Chem. 284:26725-26731(2009).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CST
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=19854130; DOI=10.1016/j.molcel.2009.08.009;
RA Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M., Yonehara S.,
RA Saito M., Ishikawa F.;
RT "RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and
RT protects telomeres independently of the Pot1 pathway.";
RL Mol. Cell 36:193-206(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION.
RX PubMed=22748632; DOI=10.1016/j.cell.2012.05.026;
RA Wu P., Takai H., de Lange T.;
RT "Telomeric 3' overhangs derive from resection by Exo1 and Apollo and fill-
RT in by POT1b-associated CST.";
RL Cell 150:39-52(2012).
RN [9]
RP STRUCTURE BY NMR OF 205-311.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the hypothetical domain of Riken cDNA 0610009H20.";
RL Submitted (NOV-2004) to the PDB data bank.
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 (PubMed:19854130). However,
CC the CST complex has been shown to be involved in several aspects of
CC telomere replication. The CST complex inhibits telomerase and is
CC involved in telomere length homeostasis; it is proposed to bind to
CC newly telomerase-synthesized 3' overhangs and to terminate telomerase
CC action implicating the association with the ACD:POT1 complex thus
CC interfering with its telomerase stimulation activity. The CST complex
CC is also proposed to be involved in fill-in synthesis of the telomeric
CC C-strand probably implicating recruitment and activation of DNA
CC polymerase alpha (PubMed:22748632). The CST complex facilitates
CC recovery from many forms of exogenous DNA damage; seems to be involved
CC in the re-initiation of DNA replication at repaired forks and/or
CC dormant origins. Required for efficicient replication of the duplex
CC region of the telomere. Promotes efficient replication of lagging-
CC strand telomeres. Promotes general replication start following
CC replication-fork stalling implicating new origin firing. May be in
CC involved in C-strand fill-in during late S/G2 phase independent of its
CC role in telomere duplex replication (By similarity).
CC {ECO:0000250|UniProtKB:Q9H668, ECO:0000269|PubMed:19854130,
CC ECO:0000269|PubMed:22748632}.
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 (PubMed:19119139, PubMed:19854130). Interacts with ACD/TPP1
CC (PubMed:19648609). Interacts with POT1 and POLA1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H668, ECO:0000269|PubMed:19119139,
CC ECO:0000269|PubMed:19648609, ECO:0000269|PubMed:19854130}.
CC -!- INTERACTION:
CC Q8K2X3; Q5EE38: Acd; NbExp=2; IntAct=EBI-2553883, EBI-6258642;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19119139,
CC ECO:0000269|PubMed:19854130}. Chromosome, telomere
CC {ECO:0000269|PubMed:19854130}.
CC -!- SIMILARITY: Belongs to the STN1 family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:19119139, it acts as a regulator of DNA
CC replication. According to PubMed:19854130, this effect is indirect and
CC it rather acts as a general regulator of DNA metabolism. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29548.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK075574; BAC35830.1; -; mRNA.
DR EMBL; AK146929; BAE27540.1; -; mRNA.
DR EMBL; AK164386; BAE37766.1; -; mRNA.
DR EMBL; CH466534; EDL42035.1; -; Genomic_DNA.
DR EMBL; BC029548; AAH29548.1; ALT_INIT; mRNA.
DR CCDS; CCDS29892.1; -.
DR RefSeq; NP_780569.1; NM_175360.2.
DR PDB; 1WJ5; NMR; -; A=205-311.
DR PDBsum; 1WJ5; -.
DR AlphaFoldDB; Q8K2X3; -.
DR SMR; Q8K2X3; -.
DR BioGRID; 224373; 6.
DR ComplexPortal; CPX-2130; CST complex.
DR IntAct; Q8K2X3; 7.
DR STRING; 10090.ENSMUSP00000040944; -.
DR iPTMnet; Q8K2X3; -.
DR PhosphoSitePlus; Q8K2X3; -.
DR EPD; Q8K2X3; -.
DR MaxQB; Q8K2X3; -.
DR PaxDb; Q8K2X3; -.
DR PeptideAtlas; Q8K2X3; -.
DR PRIDE; Q8K2X3; -.
DR ProteomicsDB; 258642; -.
DR Antibodypedia; 31566; 187 antibodies from 21 providers.
DR DNASU; 108689; -.
DR Ensembl; ENSMUST00000049369; ENSMUSP00000040944; ENSMUSG00000042694.
DR GeneID; 108689; -.
DR KEGG; mmu:108689; -.
DR UCSC; uc008hvb.1; mouse.
DR CTD; 79991; -.
DR MGI; MGI:1915581; Stn1.
DR VEuPathDB; HostDB:ENSMUSG00000042694; -.
DR eggNOG; KOG3108; Eukaryota.
DR GeneTree; ENSGT00390000000909; -.
DR HOGENOM; CLU_063889_0_0_1; -.
DR InParanoid; Q8K2X3; -.
DR OMA; LCWKDEK; -.
DR OrthoDB; 1451022at2759; -.
DR PhylomeDB; Q8K2X3; -.
DR TreeFam; TF328623; -.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR BioGRID-ORCS; 108689; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Stn1; mouse.
DR EvolutionaryTrace; Q8K2X3; -.
DR PRO; PR:Q8K2X3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K2X3; protein.
DR Bgee; ENSMUSG00000042694; Expressed in spermatocyte and 179 other tissues.
DR ExpressionAtlas; Q8K2X3; baseline and differential.
DR Genevisible; Q8K2X3; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:1990879; C:CST complex; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:0016233; P:telomere capping; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome; Telomere.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19119139"
FT CHAIN 2..378
FT /note="CST complex subunit STN1"
FT /id="PRO_0000058021"
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..305
FT /note="Winged helix-turn-helix (wHTH) 1"
FT /evidence="ECO:0000250"
FT REGION 306..378
FT /note="Winged helix-turn-helix (wHTH) 2"
FT /evidence="ECO:0000250"
FT MUTAGEN 96
FT /note="W->A: Impairs single-stranded DNA binding; when
FT associated with A-151."
FT /evidence="ECO:0000269|PubMed:19119139"
FT MUTAGEN 151
FT /note="F->A: Impairs single-stranded DNA binding; when
FT associated with A-96."
FT /evidence="ECO:0000269|PubMed:19119139"
FT CONFLICT 339
FT /note="N -> K (in Ref. 3; AAH29548)"
FT /evidence="ECO:0000305"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:1WJ5"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:1WJ5"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:1WJ5"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:1WJ5"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1WJ5"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1WJ5"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1WJ5"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1WJ5"
SQ SEQUENCE 378 AA; 43486 MW; 23C7FC13A10C6F1F CRC64;
MPQPCLLMEC ESSPREEEIP PLFWGLDPVF LAFAKLYIKD ILEMKESQQV PGTYFYNGHP
IRRVDIMGAV ISVKERETFY SYGVDDATGV INCVCWKKLS NAESSSDPAI LSTARELSMT
SQLKKLQETI EQKTRIGIGD IIRVRGSVRM FREEREICAN IYYKVDDPVW NMQIARMLEL
PKLYQKVYDQ PFRNPALQEE EALNNKDNLD LAGLTSLLSE KIKEFLQEKK MQSFYQQELE
TVESLQSLAS RPVTHSTGSD QVELKDSGTS GVAQRVFKNA LQLLQEKGLV FQRDSGSDKL
YYVTTKDKDL QQKIYHIIKE DCQKPNHMEK GCHLLHILNC VHLNLRWDLS KAVLQRVLEL
LEDQSDIVST ADHYYAAF
