FDO1_YEAST
ID FDO1_YEAST Reviewed; 342 AA.
AC P40214; D6VZW6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein FDO1 {ECO:0000303|PubMed:27257873};
DE AltName: Full=FKH1-interacting protein involved in donor preference {ECO:0000303|PubMed:27257873};
GN Name=FDO1 {ECO:0000303|PubMed:27257873}; OrderedLocusNames=YMR144W;
GN ORFNames=YM9375.13;
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 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [5]
RP FUNCTION, INTERACTION WITH FKH1, AND DISRUPTION PHENOTYPE.
RX PubMed=27257873; DOI=10.1371/journal.pgen.1006094;
RA Dummer A.M., Su Z., Cherney R., Choi K., Denu J., Zhao X., Fox C.A.;
RT "Binding of the Fkh1 forkhead associated domain to a phosphopeptide within
RT the Mph1 DNA helicase regulates mating-type switching in budding yeast.";
RL PLoS Genet. 12:e1006094-e1006094(2016).
CC -!- FUNCTION: In concert with FKH1, plays a role in directionality of
CC mating type switching by controlling which donor mating-type locus is
CC inserted into MAT locus during mating type switching.
CC {ECO:0000269|PubMed:27257873}.
CC -!- SUBUNIT: Interacts with FKH1. {ECO:0000269|PubMed:27257873}.
CC -!- DISRUPTION PHENOTYPE: Leads to a defect in donor preference during
CC mating-type switching (PubMed:27257873). Does not affect FKH1's
CC overlapping role with FKH2 of regulation of the expression of the CLB2
CC cluster of genes during the G2/M phase of the mitotic cell cycle
CC (PubMed:27257873). {ECO:0000269|PubMed:27257873,
CC ECO:0000303|PubMed:27257873}.
CC -!- MISCELLANEOUS: Present with 2120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z47071; CAA87358.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10040.1; -; Genomic_DNA.
DR PIR; S50400; S50400.
DR RefSeq; NP_013864.1; NM_001182646.1.
DR AlphaFoldDB; P40214; -.
DR SMR; P40214; -.
DR BioGRID; 35320; 108.
DR DIP; DIP-4431N; -.
DR IntAct; P40214; 4.
DR MINT; P40214; -.
DR STRING; 4932.YMR144W; -.
DR iPTMnet; P40214; -.
DR MaxQB; P40214; -.
DR PaxDb; P40214; -.
DR PRIDE; P40214; -.
DR EnsemblFungi; YMR144W_mRNA; YMR144W; YMR144W.
DR GeneID; 855175; -.
DR KEGG; sce:YMR144W; -.
DR SGD; S000004752; YMR144W.
DR VEuPathDB; FungiDB:YMR144W; -.
DR eggNOG; ENOG502S148; Eukaryota.
DR HOGENOM; CLU_069850_0_0_1; -.
DR InParanoid; P40214; -.
DR OMA; RHEVEDN; -.
DR BioCyc; YEAST:G3O-32836-MON; -.
DR PRO; PR:P40214; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40214; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0007535; P:donor selection; IMP:SGD.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..342
FT /note="Protein FDO1"
FT /id="PRO_0000203305"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 38570 MW; AEA7FE5E1080C8A6 CRC64;
MEENKLSGNK PIQLATWSNQ MGSPENNGNN ANNGSDVQNV IQKALGLIRQ LNNNGLMSPM
EEEHSQPSSS QETLSVDREI NEQGRLRLLM QAKDDNTRKE VGTYSSPMDS AYARENMLNV
LQSLVTHLNQ AVSQIQQLKF KNMILTSNEN NIQSRHEVED NLQKQQFERM KCQFLLERQS
LKDQLRKREN KIVKYKQKII EKNKKLNNLA KVLNQHAISD TSQIDSFSSS VKKTPSSTTT
PQEMKSDMLN TLGILATHVL KDEIDDDSGN QTILQLAAGS ISNDCNTTEL EITCSPEMGR
TITHNRPNTK DESIQDSHGN RTLQLPKMKS FSTIDGSIKD IK
