COM1_SCHPO
ID COM1_SCHPO Reviewed; 294 AA.
AC O74986; A9LJ21;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA endonuclease ctp1;
DE EC=3.1.-.-;
DE AltName: Full=Double-strand break repair protein ctp1;
DE AltName: Full=Meiotically up-regulated gene 38 protein;
DE AltName: Full=Nbs1-interacting protein 1;
DE AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog;
DE Short=SAE2;
GN Name=ctp1; Synonyms=mug38, nip1, slr9; ORFNames=SPCC338.08;
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 [MRNA], AND FUNCTION.
RX PubMed=17936710; DOI=10.1016/j.molcel.2007.09.009;
RA Limbo O., Chahwan C., Yamada Y., de Bruin R.A.M., Wittenberg C.,
RA Russell P.;
RT "Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex
RT to control double-strand break repair by homologous recombination.";
RL Mol. Cell 28:134-146(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION AT SER-114 AND
RP SER-165 BY TEL1, AND MUTAGENESIS OF SER-35; SER-114; SER-165 AND THR-175.
RX PubMed=18378696; DOI=10.1128/mcb.01828-07;
RA Akamatsu Y., Murayama Y., Yamada T., Nakazaki T., Tsutsui Y., Ohta K.,
RA Iwasaki H.;
RT "Molecular characterization of the role of the Schizosaccharomyces pombe
RT nip1+/ctp1+ gene in DNA double-strand break repair in association with the
RT Mre11-Rad50-Nbs1 complex.";
RL Mol. Cell. Biol. 28:3639-3651(2008).
RN [3]
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 [4]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [5]
RP FUNCTION.
RX PubMed=19139281; DOI=10.1128/mcb.01182-08;
RA Hartsuiker E., Mizuno K., Molnar M., Kohli J., Ohta K., Carr A.M.;
RT "Ctp1CtIP and Rad32Mre11 nuclease activity are required for Rec12Spo11
RT removal, but Rec12Spo11 removal is dispensable for other MRN-dependent
RT meiotic functions.";
RL Mol. Cell. Biol. 29:1671-1681(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 72-84 IN COMPLEX WITH NBS1,
RP INTERACTION WITH NBS1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-77;
RP THR-78; THR-79; SER-87 AND THR-89, AND MUTAGENESIS OF 77-SER--THR-79 AND
RP 87-SER--THR-89.
RX PubMed=19804755; DOI=10.1016/j.cell.2009.07.033;
RA Williams R.S., Dodson G.E., Limbo O., Yamada Y., Williams J.S.,
RA Guenther G., Classen S., Glover J.N., Iwasaki H., Russell P., Tainer J.A.;
RT "Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand
RT break processing and repair.";
RL Cell 139:87-99(2009).
CC -!- FUNCTION: Endonuclease that cooperates with the MRN complex in
CC processing meiotic and mitotic double-strand breaks by allowing the
CC endonucleolytic removal of rec12 from the break sites and ensuring both
CC resection and intrachromosomal association of the broken ends. Required
CC for the formation of RPA-coated single strand DNA adjacent to the DSBs
CC where it functions together with the MRN complex in 5'- 3' resection.
CC Required for the repair of programmed meiotic DSBs. Involved also in an
CC rhp51 recombinase-dependent recombinational repair pathway.
CC {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:17936710,
CC ECO:0000269|PubMed:18378696, ECO:0000269|PubMed:19139281}.
CC -!- INTERACTION:
CC O74986; O74986: ctp1; NbExp=4; IntAct=EBI-2463766, EBI-2463766;
CC O74986; O43070: nbs1; NbExp=6; IntAct=EBI-2463766, EBI-2125045;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19804755}.
CC Note=Accumulates at DSBs.
CC -!- PTM: Phosphorylated by tel1 in response to DNA damage.
CC {ECO:0000269|PubMed:18378696, ECO:0000269|PubMed:19804755}.
CC -!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
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DR EMBL; AB363065; BAG16512.1; -; mRNA.
DR EMBL; EU168806; ABX10016.1; -; mRNA.
DR EMBL; CU329672; CAA19339.2; -; Genomic_DNA.
DR PIR; T41734; T41734.
DR RefSeq; NP_588159.2; NM_001023148.3.
DR PDB; 3HUF; X-ray; 2.15 A; E=72-84.
DR PDB; 4X01; X-ray; 2.20 A; A/B/C/D/E/F/G/H=5-60.
DR PDBsum; 3HUF; -.
DR PDBsum; 4X01; -.
DR AlphaFoldDB; O74986; -.
DR SMR; O74986; -.
DR BioGRID; 275290; 72.
DR DIP; DIP-54853N; -.
DR IntAct; O74986; 1.
DR STRING; 4896.SPCC338.08.1; -.
DR iPTMnet; O74986; -.
DR PaxDb; O74986; -.
DR PRIDE; O74986; -.
DR EnsemblFungi; SPCC338.08.1; SPCC338.08.1:pep; SPCC338.08.
DR GeneID; 2538706; -.
DR KEGG; spo:SPCC338.08; -.
DR PomBase; SPCC338.08; ctp1.
DR VEuPathDB; FungiDB:SPCC338.08; -.
DR eggNOG; ENOG502S92Z; Eukaryota.
DR HOGENOM; CLU_947169_0_0_1; -.
DR OMA; WESDFVD; -.
DR EvolutionaryTrace; O74986; -.
DR PRO; PR:O74986; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0000405; F:bubble DNA binding; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0045027; F:DNA end binding; EXP:PomBase.
DR GO; GO:0106260; F:DNA-DNA tethering activity; IDA:PomBase.
DR GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0140656; F:endodeoxyribonuclease activator activity; IDA:PomBase.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0070336; F:flap-structured DNA binding; IDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:PomBase.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:PomBase.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IBA:GO_Central.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:PomBase.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:1990898; P:meiotic DNA double-strand break clipping; IMP:PomBase.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IMP:PomBase.
DR GO; GO:1990899; P:meiotic DNA double-strand break resectioning; IMP:PomBase.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR IDEAL; IID50240; -.
DR InterPro; IPR013882; Ctp1_C.
DR InterPro; IPR033316; RBBP8-like.
DR PANTHER; PTHR15107; PTHR15107; 1.
DR Pfam; PF08573; SAE2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase;
KW Meiosis; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..294
FT /note="DNA endonuclease ctp1"
FT /id="PRO_0000278499"
FT REGION 54..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19804755"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19804755"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19804755"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19804755"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19804755"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18378696"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18378696"
FT MUTAGEN 35
FT /note="S->A: Wild-type phosphorylation pattern."
FT /evidence="ECO:0000269|PubMed:18378696"
FT MUTAGEN 77..79
FT /note="STT->AAA: Reduces enrichment at the DSBs and
FT increases sensitivity to DNA damage; when associated with
FT 87-A--A-89."
FT /evidence="ECO:0000269|PubMed:19804755"
FT MUTAGEN 87..89
FT /note="SDT->ADA: Reduces enrichment at the DSBs and
FT increases sensitivity to DNA damage; when associated with
FT 77-A--A-79."
FT /evidence="ECO:0000269|PubMed:19804755"
FT MUTAGEN 114
FT /note="S->A: Lower levels of phosphorylation."
FT /evidence="ECO:0000269|PubMed:18378696"
FT MUTAGEN 165
FT /note="S->A: Lower levels of phosphorylation."
FT /evidence="ECO:0000269|PubMed:18378696"
FT MUTAGEN 175
FT /note="T->A: Wild-type phosphorylation pattern."
FT /evidence="ECO:0000269|PubMed:18378696"
FT HELIX 12..55
FT /evidence="ECO:0007829|PDB:4X01"
SQ SEQUENCE 294 AA; 33101 MW; 857AD70D23B88D68 CRC64;
MNEEEHNKSV HWSIVYRQLG NLLEQYEVEI ARLKSQLVLE KKLRIQVEKE LESVKTKQIS
SSASSKVSSN TIQELDSTTD EDEIPGSDTV DEEDPSLNAP FSEKNQSVKI PPHSPTLPVQ
NASAFVKPIS VPLGNVKEEK FLDTNPIGAE SFESSDGEMH LRARSPEDMI LLRETQPLAP
LDINTLGVSD NRQKKGTEKK RPFEPEFLND DVIRGNKRKA LPAYECPDCQ KFYELHGPVK
ESSVAPTWND ENRLGGGSLP NCKHQPLVQK VGRHRKLNIP KPIPNGFWES DFVD
