P39720 (OAF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oleate-activated transcription factor 1

Gene names

Name:	OAF1
Synonyms:	YAF1
Ordered Locus Names:	YAL051W
ORF Names:	FUN43

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1047 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The PIP2-OAF1 heterodimer acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as sole carbon source. Recognizes and binds to the oleate response element (ORE) (or peroxisome box), two inverted CGG triplets spaced by 14 to 18 intervening nucleotides, in the promoter region of a number of genes (such as CTA1, FOX1 to FOX3, FAA2, PAS8, PAS10, etc.) for peroxisomal proteins. OAF1 acts as the sensor for oleate and inhibits PIP2 activity under non-inducing conditions. Activity is repressed by glucose. Ref.4 Ref.5 Ref.6 Ref.7
Subunit structure	Heterodimer of PIP2 and OAF1.
Subcellular location	Nucleus.
Domain	the 9aaTAD motif (residues 1034 to 1042) is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.12
Miscellaneous	Present with 92 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.

Ontologies

Keywords
Biological process	Sporulation Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oleic acid Inferred from physical interaction PubMed 17551510. Source: SGD positive regulation of chromatin silencing at telomere Inferred from mutant phenotype PubMed 21206489. Source: SGD positive regulation of fatty acid beta-oxidation Inferred from mutant phenotype Ref.6. Source: SGD sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from physical interaction Ref.4. Source: SGD
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay Ref.4. Source: SGD RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay Ref.7. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1047	1047	Oleate-activated transcription factor 1		PRO_0000114990
Regions
	DNA binding	66 – 93	28	Zn(2)-C6 fungal-type Ref.4 Ref.5 Ref.9
	Motif	1034 – 1042	9	9aaTAD
Amino acid modifications
	Modified residue	144	1	Phosphoserine Ref.8 Ref.13 Ref.14
	Modified residue	155	1	Phosphoserine Ref.8 Ref.13
	Modified residue	947	1	Phosphoserine Ref.14
	Modified residue	949	1	Phosphoserine Ref.14
Experimental info
	Sequence conflict	70	1	R → W in AAC04981. Ref.1
	Sequence conflict	447	1	Q → P in AAC04981. Ref.1
	Sequence conflict	588	1	K → T in AAC04981. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39720 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 7D9388450486F540	FASTA	1,047	118,891
	10 20 30 40 50 60 MVENSTQKAP HAGNDDNSST KPYSEAFFLG FNNPTPGLEA EHSSTSPAPE NSETHNRKRN 70 80 90 100 110 120 RILFVCQACR KSKTKCDREK PECGRCVKHG LKCVYDVSKQ PAPRIPSKDA IISRLEKDMF 130 140 150 160 170 180 YWKDKAMKLL TEREVNESGK RSASPINTNN ASGDSPDTKK QHKMEPIYEQ SGNGDINNGT 190 200 210 220 230 240 RNDIEINLYR SHPTMIMSKV MKREVKPLSE NYIIIQDCFL KILVTSVFLD TSKNTMIPAL 250 260 270 280 290 300 TANANITRAQ PSVANNLLKL KEMLIRQCQT EDEKNRVNEF TDRILQNTNS NRNLKIGMLL 310 320 330 340 350 360 SMLYNSVGYQ YLEDHCPQGG EYSDLLRNLI NECEAILPSY EIIERYKNHF YEYVYPSLPF 370 380 390 400 410 420 IELEIFEESL SQTIFPDPNN PSKVQIRMGS THLRAKVENL SLLLVILKLS YMSIRFLDHS 430 440 450 460 470 480 TADSSFYLSK EIIDKYPIPN DFILLSQRCL ASENWCACAN ENIISCLLYI WSFFAFSPEE 490 500 510 520 530 540 GDFFLEHPTD VISSLIMMLS TSIGLHRDPS DFPQLISPST SDKRTLNHRR ILWLSIVTVC 550 560 570 580 590 600 SFEASLKGRH SVSPISLMAL FLNIKDPDSL TVYMNRVRGD LSDINNHKLL RIHKFTFKRA 610 620 630 640 650 660 QLALLLSDLD NLTMTYYGSF HLHSIEFIRE KIEIFVEENF PIVPLKSVAQ DKSDLDDMNV 670 680 690 700 710 720 ISEMNILSSE NSSSFHNRIM NKLLMLRTSM AVFLHFETLI TKDKSIFPFY KKYFMVSCMD 730 740 750 760 770 780 ALSLINYFNK FFNGEYRHAI SSLTSFNVTK FIQLALSSTI FSLLGIILRI GLAIHMLSSE 790 800 810 820 830 840 VQKLSGTTDP RIKELNTKVE KFSTLQRDLE SALEGIYCSA SEHLRFTYFP VFKMLALFDV 850 860 870 880 890 900 IVQRMRKGEL WHGIFTMIQM EQMHSRIIKT LSITLGVKLD KKDRLLEELM ACNHVANFSV 910 920 930 940 950 960 EDIDELNRNI KKEIQISSGL KPPVNTIDLT NGEPFGNAVP TFTKTWSSSL DNLEKLSSAA 970 980 990 1000 1010 1020 AVGQSLDYNS GLRQGPLAGG GSKEQTPIAG MNNLNNSINA TPIVDNSSGS QLPNGFDRGQ 1030 1040 ANNTPFPGYF GGLDLFDYDF LFGNDFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Hong E.L., Cherry J.M. Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 70; 447 AND 588. Strain: ATCC 204508 / S288c.
[4]	"Purification, identification, and properties of a Saccharomyces cerevisiae oleate-activated upstream activating sequence-binding protein that is involved in the activation of POX1." Luo Y., Karpichev I.V., Kohanski R.A., Small G.M. J. Biol. Chem. 271:12068-12075(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 118-122; 946-953 AND 959-970, FUNCTION, DNA-BINDING.
[5]	"A heterodimer of the Zn2Cys6 transcription factors Pip2p and Oaf1p controls induction of genes encoding peroxisomal proteins in Saccharomyces cerevisiae." Rottensteiner H., Kal A.J., Hamilton B., Ruis H., Tabak H.F. Eur. J. Biochem. 247:776-783(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH PIP2.
[6]	"A complex containing two transcription factors regulates peroxisome proliferation and the coordinate induction of beta-oxidation enzymes in Saccharomyces cerevisiae." Karpichev I.V., Luo Y., Marians R.C., Small G.M. Mol. Cell. Biol. 17:69-80(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PIP2, IDENTIFICATION OF FRAMESHIFT.
[7]	"Functional analysis of the Zn(2)Cys(6) transcription factors Oaf1p and Pip2p. Different roles in fatty acid induction of beta-oxidation in Saccharomyces cerevisiae." Baumgartner U., Hamilton B., Piskacek M., Ruis H., Rottensteiner H. J. Biol. Chem. 274:22208-22216(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-155, MASS SPECTROMETRY. Strain: 2124.
[9]	"Saccharomyces cerevisiae Pip2p-Oaf1p regulates PEX25 transcription through an adenine-less ORE." Rottensteiner H., Hartig A., Hamilton B., Ruis H., Erdmann R., Gurvitz A. Eur. J. Biochem. 270:2013-2022(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[10]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF FRAMESHIFT.
[11]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-155, MASS SPECTROMETRY.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-947 AND SER-949, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U12980 Genomic DNA. Translation: AAC04981.2. BK006935 Genomic DNA. Translation: DAA06936.2.
PIR	S51969.
RefSeq	NP_009349.3. NM_001178195.2.
3D structure databases
ProteinModelPortal	P39720.
SMR	P39720. Positions 57-133.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5928N.
IntAct	P39720. 4 interactions.
MINT	MINT-2781292.
STRING	4932.YAL051W.
Proteomic databases
PaxDb	P39720.
PeptideAtlas	P39720.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAL051W; YAL051W; YAL051W.
GeneID	851247.
KEGG	sce:YAL051W.
Organism-specific databases
CYGD	YAL051w.
SGD	S000000048. OAF1.
Phylogenomic databases
eggNOG	NOG39949.
GeneTree	ENSGT00390000000033.
HOGENOM	HOG000066010.
OMA	TKCDREK.
OrthoDB	EOG480N52.
Enzyme and pathway databases
BioCyc	YEAST:G3O-28857-MONOMER.
Gene expression databases
Genevestigator	P39720.
GermOnline	YAL051W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	4.10.240.10. 1 hit.
InterPro	IPR002409. Aflatoxin_BRP. IPR001138. Zn2-C6_fun-type_DNA-bd. [Graphical view]
Pfam	PF00172. Zn_clus. 1 hit. [Graphical view]
PRINTS	PR00755. AFLATOXINBRP.
SMART	SM00066. GAL4. 1 hit. [Graphical view]
SUPFAM	SSF57701. Fungi_TrN. 1 hit.
PROSITE	PS00463. ZN2_CY6_FUNGAL_1. 1 hit. PS50048. ZN2_CY6_FUNGAL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968186.

Entry information

Entry name

OAF1_YEAST

Accession

Primary (citable) accession number: P39720
Secondary accession number(s): D6VPG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program