STN1_ARATH
ID STN1_ARATH Reviewed; 160 AA.
AC Q9LMK5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=CST complex subunit STN1 {ECO:0000303|PubMed:19064932};
DE AltName: Full=Suppressor of cdc thirteen homolog {ECO:0000303|PubMed:19064932};
DE Short=AtSTN1 {ECO:0000303|PubMed:19064932};
GN Name=STN1 {ECO:0000303|PubMed:19064932};
GN OrderedLocusNames=At1g07130 {ECO:0000312|Araport:AT1G07130};
GN ORFNames=F10K1.17 {ECO:0000312|EMBL:AAF82208.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19064932; DOI=10.1073/pnas.0807867105;
RA Song X., Leehy K., Warrington R.T., Lamb J.C., Surovtseva Y.V.,
RA Shippen D.E.;
RT "STN1 protects chromosome ends in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19815-19820(2008).
RN [7]
RP INTERACTION WITH CTC1.
RX PubMed=19854131; DOI=10.1016/j.molcel.2009.09.017;
RA Surovtseva Y.V., Churikov D., Boltz K.A., Song X., Lamb J.C.,
RA Warrington R., Leehy K., Heacock M., Price C.M., Shippen D.E.;
RT "Conserved telomere maintenance component 1 interacts with STN1 and
RT maintains chromosome ends in higher eukaryotes.";
RL Mol. Cell 36:207-218(2009).
RN [8]
RP INTERACTION WITH TEN1.
RX PubMed=23572541; DOI=10.1105/tpc.112.107425;
RA Leehy K.A., Lee J.R., Song X., Renfrew K.B., Shippen D.E.;
RT "MERISTEM DISORGANIZATION1 encodes TEN1, an essential telomere protein that
RT modulates telomerase processivity in Arabidopsis.";
RL Plant Cell 25:1343-1354(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25299252; DOI=10.1371/journal.pgen.1004682;
RA Derboven E., Ekker H., Kusenda B., Bulankova P., Riha K.;
RT "Role of STN1 and DNA polymerase alpha in telomere stability and genome-
RT wide replication in Arabidopsis.";
RL PLoS Genet. 10:E1004682-E1004682(2014).
RN [10]
RP FUNCTION, AND INTERACTION WITH TEN1 AND POT1A.
RX PubMed=25329641; DOI=10.1371/journal.pgen.1004738;
RA Renfrew K.B., Song X., Lee J.R., Arora A., Shippen D.E.;
RT "POT1a and components of CST engage telomerase and regulate its activity in
RT Arabidopsis.";
RL PLoS Genet. 10:E1004738-E1004738(2014).
CC -!- FUNCTION: Component of the CST complex, a complex that binds to single-
CC stranded DNA and is required to protect telomeres from DNA degradation.
CC The CST complex binds single-stranded DNA with high affinity in a
CC sequence-independent manner, while isolated subunits bind DNA with low
CC affinity by themselves (PubMed:19064932). Associates with enzymatically
CC active telomerase (PubMed:25329641). Plays a genomewide role in DNA
CC replication and facilitates re-replication at non-telomeric loci
CC (PubMed:25299252). {ECO:0000269|PubMed:19064932,
CC ECO:0000269|PubMed:25299252, ECO:0000269|PubMed:25329641}.
CC -!- SUBUNIT: Component of the CST complex, composed of CTC1, TEN1 and STN1.
CC Interacts with CTC1 (PubMed:19854131). Interacts with TEN1
CC (PubMed:23572541, PubMed:25329641). Interacts with POT1A
CC (PubMed:25329641). In vitro interaction with TEN1 and POT1A is mutually
CC exclusive, indicating that POT1A and TEN1 may compete for the same
CC binding site (PubMed:25329641). {ECO:0000269|PubMed:19854131,
CC ECO:0000269|PubMed:23572541, ECO:0000269|PubMed:25329641}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19064932}.
CC Chromosome, telomere {ECO:0000269|PubMed:19064932}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19064932}.
CC -!- DISRUPTION PHENOTYPE: Plants display an immediate onset of growth and
CC developmental defects and reduced fertility, probably due to impaired
CC telomeres (PubMed:19064932). In nearly all mutants, apical dominance is
CC completely abolished, leading to multiple inflorescence bolts that are
CC often fused (PubMed:19064932). In addition, floral phyllotaxy is
CC perturbed and siliques develop at irregular positions on the
CC inflorescence bolt (PubMed:19064932). Moreover, leaf size is
CC substantially reduced, likely reflecting defects in cell proliferation
CC (PubMed:19064932). These effects are accompanied by catastrophic loss
CC of telomeric and subtelomeric DNA, high levels of end-to-end chromosome
CC fusions, increased G-overhang signals, and elevated telomere
CC recombination (PubMed:19064932). Progressive loss of telomeric DNA and
CC gradual onset of telomere dysfunction (PubMed:25299252). Hindered re-
CC replication of heterochromatic regions (PubMed:25299252).
CC {ECO:0000269|PubMed:19064932, ECO:0000269|PubMed:25299252}.
CC -!- SIMILARITY: Belongs to the STN1 family. {ECO:0000305}.
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DR EMBL; AC067971; AAF82208.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28079.1; -; Genomic_DNA.
DR EMBL; AK118772; BAC43365.1; -; mRNA.
DR EMBL; BT005022; AAO50555.1; -; mRNA.
DR EMBL; AY086427; AAM63429.1; -; mRNA.
DR PIR; B86206; B86206.
DR RefSeq; NP_563781.1; NM_100586.2.
DR AlphaFoldDB; Q9LMK5; -.
DR SMR; Q9LMK5; -.
DR BioGRID; 22464; 3.
DR STRING; 3702.AT1G07130.1; -.
DR PaxDb; Q9LMK5; -.
DR PRIDE; Q9LMK5; -.
DR EnsemblPlants; AT1G07130.1; AT1G07130.1; AT1G07130.
DR GeneID; 837223; -.
DR Gramene; AT1G07130.1; AT1G07130.1; AT1G07130.
DR KEGG; ath:AT1G07130; -.
DR Araport; AT1G07130; -.
DR TAIR; locus:2007352; AT1G07130.
DR eggNOG; KOG3108; Eukaryota.
DR HOGENOM; CLU_111357_0_0_1; -.
DR InParanoid; Q9LMK5; -.
DR OMA; ILWLNHL; -.
DR OrthoDB; 1451022at2759; -.
DR PhylomeDB; Q9LMK5; -.
DR PRO; PR:Q9LMK5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR Genevisible; Q9LMK5; AT.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0016233; P:telomere capping; IMP:TAIR.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR040260; RFA2-like.
DR PANTHER; PTHR13989; PTHR13989; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..160
FT /note="CST complex subunit STN1"
FT /id="PRO_0000392992"
FT DNA_BIND 41..133
FT /note="OB"
SQ SEQUENCE 160 AA; 17598 MW; C8B66C406262B72E CRC64;
MDRSLQSTHA KLVARDIQRL TQSPTESNSF SLLGGACVSR VEIVGTIVSR DLTPKFLKFG
VDDGTGCVTC VMWLNQLTSS YFSRWDPATI LLLASAARKQ AAQIRIGAVA RVRGRVGSYR
GVMQITANVA VAERDPNAEI LHWLECLKLG QSCYRVRIQS