OAF1_YEAST
ID OAF1_YEAST Reviewed; 1047 AA.
AC P39720; D6VPG6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Oleate-activated transcription factor 1;
GN Name=OAF1; Synonyms=YAF1; OrderedLocusNames=YAL051W; ORFNames=FUN43;
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=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Hong E.L., Cherry J.M.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 70; 447 AND 588.
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 PROTEIN SEQUENCE OF 118-122; 946-953 AND 959-970, FUNCTION, AND
RP DNA-BINDING.
RX PubMed=8662598; DOI=10.1074/jbc.271.20.12068;
RA Luo Y., Karpichev I.V., Kohanski R.A., Small G.M.;
RT "Purification, identification, and properties of a Saccharomyces cerevisiae
RT oleate-activated upstream activating sequence-binding protein that is
RT involved in the activation of POX1.";
RL J. Biol. Chem. 271:12068-12075(1996).
RN [5]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH PIP2.
RX PubMed=9288897; DOI=10.1111/j.1432-1033.1997.00776.x;
RA Rottensteiner H., Kal A.J., Hamilton B., Ruis H., Tabak H.F.;
RT "A heterodimer of the Zn2Cys6 transcription factors Pip2p and Oaf1p
RT controls induction of genes encoding peroxisomal proteins in Saccharomyces
RT cerevisiae.";
RL Eur. J. Biochem. 247:776-783(1997).
RN [6]
RP FUNCTION, INTERACTION WITH PIP2, AND IDENTIFICATION OF FRAMESHIFT.
RX PubMed=8972187; DOI=10.1128/mcb.17.1.69;
RA Karpichev I.V., Luo Y., Marians R.C., Small G.M.;
RT "A complex containing two transcription factors regulates peroxisome
RT proliferation and the coordinate induction of beta-oxidation enzymes in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:69-80(1997).
RN [7]
RP FUNCTION.
RX PubMed=10428786; DOI=10.1074/jbc.274.32.22208;
RA Baumgartner U., Hamilton B., Piskacek M., Ruis H., Rottensteiner H.;
RT "Functional analysis of the Zn(2)Cys(6) transcription factors Oaf1p and
RT Pip2p. Different roles in fatty acid induction of beta-oxidation in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:22208-22216(1999).
RN [8]
RP DNA-BINDING.
RX PubMed=12709061; DOI=10.1046/j.1432-1033.2003.03575.x;
RA Rottensteiner H., Hartig A., Hamilton B., Ruis H., Erdmann R., Gurvitz A.;
RT "Saccharomyces cerevisiae Pip2p-Oaf1p regulates PEX25 transcription through
RT an adenine-less ORE.";
RL Eur. J. Biochem. 270:2013-2022(2003).
RN [9]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [10]
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 [11]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, 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: The PIP2-OAF1 heterodimer acts as a transcriptional activator
CC to induce the transcription of genes encoding proteins involved in
CC fatty acid beta-oxidation, a response called oleic acid induction, when
CC cells grow on fatty acids as sole carbon source. Recognizes and binds
CC to the oleate response element (ORE) (or peroxisome box), two inverted
CC CGG triplets spaced by 14 to 18 intervening nucleotides, in the
CC promoter region of a number of genes (such as CTA1, FOX1 to FOX3, FAA2,
CC PAS8, PAS10, etc.) for peroxisomal proteins. OAF1 acts as the sensor
CC for oleate and inhibits PIP2 activity under non-inducing conditions.
CC Activity is repressed by glucose. {ECO:0000269|PubMed:10428786,
CC ECO:0000269|PubMed:8662598, ECO:0000269|PubMed:8972187,
CC ECO:0000269|PubMed:9288897}.
CC -!- SUBUNIT: Heterodimer of PIP2 and OAF1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: the 9aaTAD motif (residues 1034 to 1042) is a transactivation
CC domain present in a large number of yeast and animal transcription
CC factors. {ECO:0000269|PubMed:17467953}.
CC -!- MISCELLANEOUS: Present with 92 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U12980; AAC04981.2; -; Genomic_DNA.
DR EMBL; BK006935; DAA06936.2; -; Genomic_DNA.
DR PIR; S51969; S51969.
DR RefSeq; NP_009349.3; NM_001178195.2.
DR AlphaFoldDB; P39720; -.
DR BioGRID; 31777; 84.
DR ComplexPortal; CPX-1038; PIP2-OAF1 transcription factor complex.
DR DIP; DIP-5928N; -.
DR IntAct; P39720; 4.
DR MINT; P39720; -.
DR STRING; 4932.YAL051W; -.
DR iPTMnet; P39720; -.
DR MaxQB; P39720; -.
DR PaxDb; P39720; -.
DR PRIDE; P39720; -.
DR EnsemblFungi; YAL051W_mRNA; YAL051W; YAL051W.
DR GeneID; 851247; -.
DR KEGG; sce:YAL051W; -.
DR SGD; S000000048; OAF1.
DR VEuPathDB; FungiDB:YAL051W; -.
DR eggNOG; ENOG502QW20; Eukaryota.
DR GeneTree; ENSGT00940000176335; -.
DR HOGENOM; CLU_008453_0_0_1; -.
DR InParanoid; P39720; -.
DR OMA; CANENII; -.
DR BioCyc; YEAST:G3O-28857-MON; -.
DR PRO; PR:P39720; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39720; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0089716; C:Pip2-Oaf1 complex; IDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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:0006631; P:fatty acid metabolic process; IDA:ComplexPortal.
DR GO; GO:0007031; P:peroxisome organization; IC:ComplexPortal.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061429; P:positive regulation of transcription from RNA polymerase II promoter by oleic acid; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Sporulation; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..1047
FT /note="Oleate-activated transcription factor 1"
FT /id="PRO_0000114990"
FT DNA_BIND 66..93
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1034..1042
FT /note="9aaTAD"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 70
FT /note="R -> W (in Ref. 1; AAC04981)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="Q -> P (in Ref. 1; AAC04981)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="K -> T (in Ref. 1; AAC04981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 118891 MW; 7D9388450486F540 CRC64;
MVENSTQKAP HAGNDDNSST KPYSEAFFLG FNNPTPGLEA EHSSTSPAPE NSETHNRKRN
RILFVCQACR KSKTKCDREK PECGRCVKHG LKCVYDVSKQ PAPRIPSKDA IISRLEKDMF
YWKDKAMKLL TEREVNESGK RSASPINTNN ASGDSPDTKK QHKMEPIYEQ SGNGDINNGT
RNDIEINLYR SHPTMIMSKV MKREVKPLSE NYIIIQDCFL KILVTSVFLD TSKNTMIPAL
TANANITRAQ PSVANNLLKL KEMLIRQCQT EDEKNRVNEF TDRILQNTNS NRNLKIGMLL
SMLYNSVGYQ YLEDHCPQGG EYSDLLRNLI NECEAILPSY EIIERYKNHF YEYVYPSLPF
IELEIFEESL SQTIFPDPNN PSKVQIRMGS THLRAKVENL SLLLVILKLS YMSIRFLDHS
TADSSFYLSK EIIDKYPIPN DFILLSQRCL ASENWCACAN ENIISCLLYI WSFFAFSPEE
GDFFLEHPTD VISSLIMMLS TSIGLHRDPS DFPQLISPST SDKRTLNHRR ILWLSIVTVC
SFEASLKGRH SVSPISLMAL FLNIKDPDSL TVYMNRVRGD LSDINNHKLL RIHKFTFKRA
QLALLLSDLD NLTMTYYGSF HLHSIEFIRE KIEIFVEENF PIVPLKSVAQ DKSDLDDMNV
ISEMNILSSE NSSSFHNRIM NKLLMLRTSM AVFLHFETLI TKDKSIFPFY KKYFMVSCMD
ALSLINYFNK FFNGEYRHAI SSLTSFNVTK FIQLALSSTI FSLLGIILRI GLAIHMLSSE
VQKLSGTTDP RIKELNTKVE KFSTLQRDLE SALEGIYCSA SEHLRFTYFP VFKMLALFDV
IVQRMRKGEL WHGIFTMIQM EQMHSRIIKT LSITLGVKLD KKDRLLEELM ACNHVANFSV
EDIDELNRNI KKEIQISSGL KPPVNTIDLT NGEPFGNAVP TFTKTWSSSL DNLEKLSSAA
AVGQSLDYNS GLRQGPLAGG GSKEQTPIAG MNNLNNSINA TPIVDNSSGS QLPNGFDRGQ
ANNTPFPGYF GGLDLFDYDF LFGNDFA
