ID   RAD9_SCHPO              Reviewed;         426 AA.
AC   P26306; Q10455;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=DNA repair protein rad9;
GN   Name=rad9; ORFNames=SPAC664.07c;
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 [GENOMIC DNA], AND MUTANT RAD9-192.
RX   PubMed=1852603; DOI=10.1093/nar/19.13.3525;
RA   Murray J.M., Carr A.M., Lehmann A.R., Watts F.Z.;
RT   "Cloning and characterisation of the rad9 DNA repair gene from
RT   Schizosaccharomyces pombe.";
RL   Nucleic Acids Res. 19:3525-3531(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1588907; DOI=10.1007/bf00266239;
RA   Lieberman H., Hopkins K.M., Laverty M., Chu H.M.;
RT   "Molecular cloning and analysis of Schizosaccharomyces pombe rad9, a gene
RT   involved in DNA repair and mutagenesis.";
RL   Mol. Gen. Genet. 232:367-376(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8536960; DOI=10.1093/genetics/141.1.107;
RA   Lieberman H.B.;
RT   "Extragenic suppressors of Schizosaccharomyces pombe rad9 mutations
RT   uncouple radioresistance and hydroxyurea sensitivity from cell cycle
RT   checkpoint control.";
RL   Genetics 141:107-117(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Malidevorans;
RX   PubMed=7821792; DOI=10.1016/0378-1119(94)90438-3;
RA   Lieberman H.B., Hopkins K.M.;
RT   "Schizosaccharomyces malidevorans and Sz. octosporus homologues of Sz.
RT   pombe rad9, a gene that mediates radioresistance and cell-cycle
RT   progression.";
RL   Gene 150:281-286(1994).
RN   [5]
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).
CC   -!- FUNCTION: Acts in DNA repair and mutagenesis. Involved in promoting
CC       resistance to ionizing radiation and UV light, as well as regulating
CC       cell cycle progression after irradiation. Repressor of entry into
CC       mitosis that is activated by chromosome breaks.
CC   -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000305}.
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DR   EMBL; X58231; CAA41189.1; -; Genomic_DNA.
DR   EMBL; X64648; CAA45919.1; -; Genomic_DNA.
DR   EMBL; X65864; CAA46693.1; -; Genomic_DNA.
DR   EMBL; X77276; CAA54491.1; -; mRNA.
DR   EMBL; CU329670; CAB65808.1; -; Genomic_DNA.
DR   PIR; S26143; S26143.
DR   PIR; T52475; T52475.
DR   RefSeq; NP_593455.1; NM_001018888.2.
DR   AlphaFoldDB; P26306; -.
DR   SMR; P26306; -.
DR   BioGRID; 279961; 78.
DR   IntAct; P26306; 1.
DR   STRING; 4896.SPAC664.07c.1; -.
DR   iPTMnet; P26306; -.
DR   PaxDb; P26306; -.
DR   EnsemblFungi; SPAC664.07c.1; SPAC664.07c.1:pep; SPAC664.07c.
DR   GeneID; 2543544; -.
DR   KEGG; spo:SPAC664.07c; -.
DR   PomBase; SPAC664.07c; rad9.
DR   VEuPathDB; FungiDB:SPAC664.07c; -.
DR   eggNOG; KOG2810; Eukaryota.
DR   HOGENOM; CLU_030657_1_0_1; -.
DR   InParanoid; P26306; -.
DR   OMA; IAYAESM; -.
DR   PhylomeDB; P26306; -.
DR   Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR   PRO; PR:P26306; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030896; C:checkpoint clamp complex; IDA:PomBase.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:PomBase.
DR   GO; GO:0035591; F:signaling adaptor activity; IGI:PomBase.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; EXP:PomBase.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR   GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR   InterPro; IPR026584; Rad9.
DR   InterPro; IPR007268; Rad9/Ddc1.
DR   PANTHER; PTHR15237; PTHR15237; 1.
DR   Pfam; PF04139; Rad9; 1.
DR   PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
PE   1: Evidence at protein level;
KW   DNA damage; Reference proteome.
FT   CHAIN           1..426
FT                   /note="DNA repair protein rad9"
FT                   /id="PRO_0000097157"
FT   REGION          1..147
FT                   /note="Required for DNA repair function"
FT   REGION          402..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         196
FT                   /note="L->P: In rad9-192; sensitive to ionizing radiation."
SQ   SEQUENCE   426 AA;  47494 MW;  A5C1173D43688E98 CRC64;
     MEFTVSNVNL RDLARIFTNL SRIDDAVNWE INKNQIEITC LNSSRSGFSM VTLKKAFFDK
     YIFQPDSVLL TGLMTPTIRI RTQVKPILSV FRNKIFDFIP TVVTTNSKNG YGSESASRKD
     VIVENVQISI STGSECRIIF KFLCKHGVIK TYKISYEQTQ TLHAVFDKSL SHNNFQINSK
     ILKDLTEHFG QRTEELTIQP LQERVLLTSF TEEVVHNRDI LKQPTQTTVS IDGKEFERVA
     LNEGVSVTLS LREFRAAVIL AEALGSSICA YYGVPGKPIL LTFAKGKNSE IEAQFILATV
     VGSDEQEVSS MMGNRWQHSS TPASLFNSVE RNNSLTAVAH NPPGSIGWQT DQSDSSRMFN
     SALDRSDETN GIKEPSTTND AGQSLFLDGI PNESELAAFN NDVNDDAEFG PTQAEQSYHG
     IFSQED