ROX1_YEAST
ID ROX1_YEAST Reviewed; 368 AA.
AC P25042; D6W469;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Repressor ROX1;
DE AltName: Full=Heme-dependent repression factor;
DE AltName: Full=Hypoxic function repressor;
GN Name=ROX1; OrderedLocusNames=YPR065W; ORFNames=YP9499.20;
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 [GENOMIC DNA].
RX PubMed=8413209; DOI=10.1128/mcb.13.10.6071-6078.1993;
RA Balasubramanian B., Lowry C.V., Zitomer R.S.;
RT "The Rox1 repressor of the Saccharomyces cerevisiae hypoxic genes is a
RT specific DNA-binding protein with a high-mobility-group motif.";
RL Mol. Cell. Biol. 13:6071-6078(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=8600445; DOI=10.1093/nar/24.5.808;
RA di Flumeri C., Liston P., Acheson N.H., Keng T.;
RT "The HMG domain of the ROX1 protein mediates repression of HEM13 through
RT overlapping DNA binding and oligomerization functions.";
RL Nucleic Acids Res. 24:808-815(1996).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION BY 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 represses the expression of HEM13,
CC COX5B, ANB1, CYC7 or AAC3 (hypoxic function). Binds to the DNA sequence
CC 5'-RRRTAACAAGAG-3'.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By heme.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X60458; CAA42991.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89182.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94973.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11485.1; -; Genomic_DNA.
DR PIR; A54430; A54430.
DR RefSeq; NP_015390.1; NM_001184162.1.
DR AlphaFoldDB; P25042; -.
DR SMR; P25042; -.
DR BioGRID; 36237; 212.
DR DIP; DIP-4651N; -.
DR IntAct; P25042; 10.
DR MINT; P25042; -.
DR STRING; 4932.YPR065W; -.
DR iPTMnet; P25042; -.
DR MaxQB; P25042; -.
DR PaxDb; P25042; -.
DR PRIDE; P25042; -.
DR EnsemblFungi; YPR065W_mRNA; YPR065W; YPR065W.
DR GeneID; 856178; -.
DR KEGG; sce:YPR065W; -.
DR SGD; S000006269; ROX1.
DR VEuPathDB; FungiDB:YPR065W; -.
DR eggNOG; KOG0527; Eukaryota.
DR HOGENOM; CLU_752616_0_0_1; -.
DR InParanoid; P25042; -.
DR OMA; XNSINNS; -.
DR BioCyc; YEAST:G3O-34213-MON; -.
DR PRO; PR:P25042; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P25042; protein.
DR GO; GO:0000785; C:chromatin; IC:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:SGD.
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; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:SGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..368
FT /note="Repressor ROX1"
FT /id="PRO_0000048574"
FT DNA_BIND 10..83
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 100..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41838 MW; 3B27442D7DEE3DBD CRC64;
MNPKSSTPKI PRPKNAFILF RQHYHRILID EWTAQGVEIP HNSNISKIIG TKWKGLQPED
KAHWENLAEK EKLEHERKYP EYKYKPVRKS KKKQLLLKEI EQQQQQQQKE QQQQKQSQPQ
LQQPFNNNIV LMKRAHSLSP SSSVSSSNSY QFQLNNDLKR LPIPSVNTSN YMVSRSLSGL
PLTHDKTARD LPQLSSQLNS IPYYSAPHDP STRHHYLNVA QAQPRANSTP QLPFISSIIN
NSSQTPVTTT TTSTTTATSS PGKFSSSPNS SVLENNRLNS INNSNQYLPP PLLPSLQDFQ
LDQYQQLKQM GPTYIVKPLS HTRNNLLSTT TPTHHHIPHI PNQNIPLHQI INSSNTEVTA
KTSLVSPK
