RSF2_YEAST
ID RSF2_YEAST Reviewed; 1380 AA.
AC P46974; D6VWU6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Respiration factor 2;
DE AltName: Full=Zinc finger protein ZMS1;
GN Name=RSF2; Synonyms=ZMS1; OrderedLocusNames=YJR127C; ORFNames=J2052;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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] OF 1-1231.
RC STRAIN=RC11-6A;
RA Thomas D., Barbey R., Surdin-Kerjan Y.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DOMAIN.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
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 FUNCTION.
RX PubMed=16208474; DOI=10.1007/s00294-005-0023-4;
RA Lu L., Roberts G.G., Oszust C., Hudson A.P.;
RT "The YJR127C/ZMS1 gene product is involved in glycerol-based respiratory
RT growth of the yeast Saccharomyces cerevisiae.";
RL Curr. Genet. 48:235-246(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP DNA-BINDING, AND PREDICTION OF FUNCTION.
RX PubMed=19111667; DOI=10.1016/j.molcel.2008.11.020;
RA Badis G., Chan E.T., van Bakel H., Pena-Castillo L., Tillo D., Tsui K.,
RA Carlson C.D., Gossett A.J., Hasinoff M.J., Warren C.L., Gebbia M.,
RA Talukder S., Yang A., Mnaimneh S., Terterov D., Coburn D., Li Yeo A.,
RA Yeo Z.X., Clarke N.D., Lieb J.D., Ansari A.Z., Nislow C., Hughes T.R.;
RT "A library of yeast transcription factor motifs reveals a widespread
RT function for Rsc3 in targeting nucleosome exclusion at promoters.";
RL Mol. Cell 32:878-887(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-544, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Transcription factor that regulates expression of both
CC nuclear and mitochondrial genes, and more specifically those required
CC for glycerol-based growth and respiration.
CC {ECO:0000269|PubMed:16208474}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the RSF2/TDA9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35240.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49627; CAA89658.1; -; Genomic_DNA.
DR EMBL; L26506; AAA35240.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006943; DAA08912.1; -; Genomic_DNA.
DR PIR; S57150; S57150.
DR RefSeq; NP_012661.3; NM_001181785.3.
DR AlphaFoldDB; P46974; -.
DR BioGRID; 33883; 58.
DR DIP; DIP-2835N; -.
DR IntAct; P46974; 3.
DR MINT; P46974; -.
DR STRING; 4932.YJR127C; -.
DR iPTMnet; P46974; -.
DR MaxQB; P46974; -.
DR PaxDb; P46974; -.
DR PRIDE; P46974; -.
DR EnsemblFungi; YJR127C_mRNA; YJR127C; YJR127C.
DR GeneID; 853592; -.
DR KEGG; sce:YJR127C; -.
DR SGD; S000003888; RSF2.
DR VEuPathDB; FungiDB:YJR127C; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000176773; -.
DR HOGENOM; CLU_003977_1_0_1; -.
DR InParanoid; P46974; -.
DR OMA; VTIHEKI; -.
DR BioCyc; YEAST:G3O-31748-MON; -.
DR PRO; PR:P46974; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46974; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF04082; Fungal_trans; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1380
FT /note="Respiration factor 2"
FT /id="PRO_0000046861"
FT ZN_FING 151..173
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 179..202
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 208..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 1117..1118
FT /note="NL -> IF (in Ref. 1; AAA35240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1131
FT /note="N -> H (in Ref. 1; AAA35240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1380 AA; 155063 MW; FBE987EA5B639000 CRC64;
MEPFAFGRGA PALCILTAAA RINLDNFVPC CWALFRLSFF FPLDPAYIRN ENKETRTSWI
SIEFFFFVKH CLSQHTFFSK TLAPKRNFRA KKLKDIGDTR IDRADKDFLL VPEPSMFVNG
NQSNFAKPAG QGILPIPKKS RIIKTDKPRP FLCPTCTRGF VRQEHLKRHQ HSHTREKPYL
CIFCGRCFAR RDLVLRHQQK LHAALVGTGD PRRMTPAPNS TSSFASKRRH SVAADDPTDL
HIIKIAGNKE TILPTPKNLA GKTSEELKEA VVALAKSNNV ELPVSAPVMN DKREKTPPSK
AGSLGFREFK FSTKGVPVHS ASSDAVIDRA NTPSSMHKTK RHASFSASSA MTYMSSSNSP
HHSITNFELV EDAPHQVGFS TPQMTAKQLM ESVSELDLPP LTLDEPPQAI KFNLNLFNND
PSGQQQQQQQ QQQNSTSSTI VNSNNGSTVA TPGVYLLSSG PSLTDLLTMN SAHAGAGGYM
SSHHSPFDLG CFSHDKPTVS EFNLPSSFPN TIPSNSTTAS NSYSNLANQT YRQMSNEQPL
MSLSPKNPPT TVSDSSSTIN FNPGTNNLLE PSMEPNDKDS NIDPAAIDDK WLSEFINNSD
PKSTFKINFN HFNDIGFIYS PPSSRSSIPN KSPPNHSATS LNHEKASLSP RLNLSLNGST
DLPSTPQNQL KEPSYSDPIS HSSHKRRRDS VMMDYDLSNF FSSRQLDISK VLNGTEQNNS
HVNDDVLTLS FPGETDSNAT QKQLPVLTPS DLLSPFSVPS VSQVLFTNEL RSMMLADNNI
DSGAFPTTSQ LNDYVTYYKE EFHPFFSFIH LPSIIPNMDS YPLLLSISMV GALYGFHSTH
AKVLANAAST QIRKSLKVSE KNPETTELWV IQTLVLLTFY CIFNKNTAVI KGMHGQLTTI
IRLLKASRLN LPLESLCQPP IESDHIMEYE NSPHMFSKIR EQYNAPNQMN KNYQYFVLAQ
SRIRTCHAVL LISNLFSSLV GADCCFHSVD LKCGVPCYKE ELYQCRNSDE WSDLLCQYKI
TLDSKFSLIE LSNGNEAYEN CLRFLSTGDS FFYGNARVSL STCLSLLISI HEKILIERNN
ARISNNNTNS NNIELDDIEW KMTSRQRIDT MLKYWENLYL KNGGILTPTE NSMSTINANP
AMRLIIPVYL FAKMRRCLDL AHVIEKIWLK DWSNMNKALE EVCYDMGSLR EATEYALNMV
DAWTSFFTYI KQGKRRIFNT PVFATTCMFT AVLVISEYMK CVEDWARGYN ANNPNSALLD
FSDRVLWLKA ERILRRLQMN LIPKECDVLK SYTDFLRWQD KDALDLSALN EEQAQRAMDP
NTDINETIQL IVAASLSSKC LYLGVQILGD APIWPIILSF AHGLQSRAIY SVTKKRNTRI
