ID   SDE2_SCHPO              Reviewed;         263 AA.
AC   O14113;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Telomere maintenance protein SDE2;
DE   AltName: Full=Silencing defective protein 2;
GN   Name=sde2; ORFNames=SPAC31G5.18c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21333630; DOI=10.1016/j.bbrc.2011.02.068;
RA   Sugioka-Sugiyama R., Sugiyama T.;
RT   "Sde2: a novel nuclear protein essential for telomeric silencing and
RT   genomic stability in Schizosaccharomyces pombe.";
RL   Biochem. Biophys. Res. Commun. 406:444-448(2011).
CC   -!- FUNCTION: Plays a role in the regulation of telomeric and centromeric
CC       silencing. Contributes to the prevention of abnormal telomere
CC       elongation. Required for chromosome segregation to daughter cells in
CC       mitosis and meiosis. May participate in the recruitment of the histone
CC       deacetylase silencing complex SHREC, which prevents transcription at
CC       telomeres. {ECO:0000269|PubMed:21333630}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the SDE2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329670; CAB11702.1; -; Genomic_DNA.
DR   PIR; T38635; T38635.
DR   RefSeq; NP_594019.1; NM_001019445.2.
DR   AlphaFoldDB; O14113; -.
DR   BioGRID; 278695; 135.
DR   STRING; 4896.SPAC31G5.18c.1; -.
DR   iPTMnet; O14113; -.
DR   MaxQB; O14113; -.
DR   PaxDb; O14113; -.
DR   PRIDE; O14113; -.
DR   EnsemblFungi; SPAC31G5.18c.1; SPAC31G5.18c.1:pep; SPAC31G5.18c.
DR   GeneID; 2542222; -.
DR   KEGG; spo:SPAC31G5.18c; -.
DR   PomBase; SPAC31G5.18c; sde2.
DR   VEuPathDB; FungiDB:SPAC31G5.18c; -.
DR   eggNOG; KOG2827; Eukaryota.
DR   HOGENOM; CLU_1058291_0_0_1; -.
DR   InParanoid; O14113; -.
DR   OMA; WIGDDIS; -.
DR   PhylomeDB; O14113; -.
DR   PRO; PR:O14113; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:PomBase.
DR   InterPro; IPR024974; Sde2_N.
DR   Pfam; PF13019; Sde2_N_Ubi; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..263
FT                   /note="Telomere maintenance protein SDE2"
FT                   /id="PRO_0000352831"
FT   REGION          95..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  29251 MW;  E1A1A329D22E6320 CRC64;
     MECKTVFLNG DFLKNSVNVN LNRLATVETL LRHVLGDSYE TVLERAYLTH QSRIVHPDIQ
     LCKLEGKSTS AHLNLTLCTR VLGGKGGFGS QLRAAGGRMS KKRNEQENQD SCRDLDGNRL
     GTIRQAKELS EYLAKKPAET RAKKEAKKQK LNKVLAADSS SSRFDDHEYL EDLEQSVSNV
     RDAFQNSLLY RRGSTSASSF SSGSNGATTD EPAEKEARNN NSSINSWSRR MQASESSNEA
     EGEDSESQTS KSLYEWDDPL YGL