CSM3_YEAST
ID CSM3_YEAST Reviewed; 317 AA.
AC Q04659; D6VZM3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chromosome segregation in meiosis protein 3;
GN Name=CSM3; OrderedLocusNames=YMR048W; ORFNames=YM9796.01;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=11470404; DOI=10.1016/s0960-9822(01)00274-3;
RA Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E.,
RA Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E.,
RA Klein F., Knop M., Nasmyth K.;
RT "A screen for genes required for meiosis and spore formation based on
RT whole-genome expression.";
RL Curr. Biol. 11:1001-1009(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH TOF1.
RX PubMed=14742714; DOI=10.1091/mbc.e03-08-0619;
RA Mayer M.L., Pot I., Chang M., Xu H., Aneliunas V., Kwok T., Newitt R.,
RA Aebersold R., Boone C., Brown G.W., Hieter P.;
RT "Identification of protein complexes required for efficient sister
RT chromatid cohesion.";
RL Mol. Biol. Cell 15:1736-1745(2004).
RN [8]
RP FUNCTION.
RX PubMed=15282308; DOI=10.1128/mcb.24.16.7082-7090.2004;
RA Xu H., Boone C., Klein H.L.;
RT "Mrc1 is required for sister chromatid cohesion to aid in recombination
RT repair of spontaneous damage.";
RL Mol. Cell. Biol. 24:7082-7090(2004).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE FPC COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15755447; DOI=10.1016/j.jmb.2005.01.041;
RA Nedelcheva M.N., Roguev A., Dolapchiev L.B., Shevchenko A., Taskov H.B.,
RA Shevchenko A., Stewart A.F., Stoynov S.S.;
RT "Uncoupling of unwinding from DNA synthesis implies regulation of MCM
RT helicase by Tof1/Mrc1/Csm3 checkpoint complex.";
RL J. Mol. Biol. 347:509-521(2005).
RN [10]
RP FUNCTION.
RX PubMed=16024805; DOI=10.1128/mcb.25.15.6707-6721.2005;
RA Archambault V., Ikui A.E., Drapkin B.J., Cross F.R.;
RT "Disruption of mechanisms that prevent rereplication triggers a DNA damage
RT response.";
RL Mol. Cell. Biol. 25:6707-6721(2005).
RN [11]
RP FUNCTION OF THE FPC COMPLEX.
RX PubMed=16219777; DOI=10.1534/genetics.105.046128;
RA Redon C., Pilch D.R., Bonner W.M.;
RT "Genetic analysis of Saccharomyces cerevisiae H2A serine 129 mutant
RT suggests a functional relationship between H2A and the sister-chromatid
RT cohesion partners Csm3-Tof1 for the repair of topoisomerase I-induced DNA
RT damage.";
RL Genetics 172:67-76(2006).
RN [12]
RP FUNCTION OF THE FPC COMPLEX.
RX PubMed=16418273; DOI=10.1073/pnas.0506540103;
RA Mohanty B.K., Bairwa N.K., Bastia D.;
RT "The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control
RT replication termination of Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:897-902(2006).
CC -!- FUNCTION: Forms a fork protection complex (FPC) with TOF1 which is
CC required for chromosome segregation during meiosis and DNA damage
CC repair. FPC coordinates leading and lagging strand synthesis and moves
CC with the replication fork. FPC stabilizes replication forks in a
CC configuration that is recognized by replication checkpoint sensors and
CC protects stalled replication forks against the fork-releasing activity
CC of RRM3 helicase. {ECO:0000269|PubMed:11470404,
CC ECO:0000269|PubMed:14742714, ECO:0000269|PubMed:15282308,
CC ECO:0000269|PubMed:15755447, ECO:0000269|PubMed:16024805,
CC ECO:0000269|PubMed:16219777, ECO:0000269|PubMed:16418273}.
CC -!- SUBUNIT: Component of the fork protection complex (FPC) consisting of
CC TOF1 and CSM3. {ECO:0000269|PubMed:15755447}.
CC -!- INTERACTION:
CC Q04659; P53840: TOF1; NbExp=7; IntAct=EBI-28093, EBI-28257;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR EMBL; Z49703; CAA89758.1; -; Genomic_DNA.
DR EMBL; AY558400; AAS56726.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09947.1; -; Genomic_DNA.
DR PIR; S54548; S54548.
DR RefSeq; NP_013763.1; NM_001182545.1.
DR PDB; 6SKL; EM; 3.70 A; Y=1-317.
DR PDB; 7PMK; EM; 3.20 A; Y=1-317.
DR PDB; 7PMN; EM; 3.20 A; Y=1-317.
DR PDBsum; 6SKL; -.
DR PDBsum; 7PMK; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; Q04659; -.
DR SMR; Q04659; -.
DR BioGRID; 35222; 325.
DR ComplexPortal; CPX-1673; Replication fork protection complex.
DR DIP; DIP-1944N; -.
DR IntAct; Q04659; 10.
DR MINT; Q04659; -.
DR STRING; 4932.YMR048W; -.
DR iPTMnet; Q04659; -.
DR MaxQB; Q04659; -.
DR PaxDb; Q04659; -.
DR PRIDE; Q04659; -.
DR EnsemblFungi; YMR048W_mRNA; YMR048W; YMR048W.
DR GeneID; 855067; -.
DR KEGG; sce:YMR048W; -.
DR SGD; S000004651; CSM3.
DR VEuPathDB; FungiDB:YMR048W; -.
DR eggNOG; KOG3004; Eukaryota.
DR HOGENOM; CLU_068300_0_0_1; -.
DR InParanoid; Q04659; -.
DR OMA; EWEMNDI; -.
DR BioCyc; YEAST:G3O-32753-MON; -.
DR PRO; PR:Q04659; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04659; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0043111; P:replication fork arrest; IMP:SGD.
DR GO; GO:0048478; P:replication fork protection; IDA:ComplexPortal.
DR InterPro; IPR012923; Csm3.
DR InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR PANTHER; PTHR13220; PTHR13220; 1.
DR Pfam; PF07962; Swi3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; DNA damage; DNA repair;
KW DNA replication inhibitor; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..317
FT /note="Chromosome segregation in meiosis protein 3"
FT /id="PRO_0000203277"
FT REGION 16..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 317 AA; 36355 MW; 0B92F561F91197AE CRC64;
MDQDFDSLLL GFNDSDSVQK DPTVPNGLDG SVVDPTIADP TAITARKRRP QVKLTAEKLL
SDKGLPYVLK NAHKRIRISS KKNSYDNLSN IIQFYQLWAH ELFPKAKFKD FMKICQTVGK
TDPVLREYRV SLFRDEMGMS FDVGTRETGQ DLERQSPMVE EHVTSAEERP IVADSFAQDK
RNVNNVDYDN DEDDDIYHLS YRNRRGRVLD ERGNNETVLN NVVPPKEDLD ALLKTFRVQG
PVGLEENEKK LLLGWLDAHR KMEKGSMTEE DVQLIQSLEE WEMNDIEGQH THYDLLPGGD
EFGVDQDELD AMKEMGF
