PIP2_YEAST
ID PIP2_YEAST Reviewed; 996 AA.
AC P52960; D6W358;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Peroxisome proliferation transcriptional regulator;
DE AltName: Full=Oleate-activated transcription factor 2;
GN Name=PIP2; Synonyms=OAF2; OrderedLocusNames=YOR363C;
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], FUNCTION, AND DNA-BINDING.
RX PubMed=8670793; DOI=10.1002/j.1460-2075.1996.tb00655.x;
RA Rottensteiner H., Kal A.J., Filipits M., Binder M., Hamilton B.,
RA Tabak H.F., Ruis H.;
RT "Pip2p: a transcriptional regulator of peroxisome proliferation in the
RT yeast Saccharomyces cerevisiae.";
RL EMBO J. 15:2924-2934(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION, DNA-BINDING, INTERACTION WITH OAF1, AND INDUCTION.
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 [5]
RP FUNCTION, INTERACTION WITH OAF1, AND INDUCTION.
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 [6]
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 [7]
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 [8]
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).
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. Activity is inhibited by
CC OAF1 under non-inducing conditions. Activity is repressed by glucose.
CC {ECO:0000269|PubMed:10428786, ECO:0000269|PubMed:8670793,
CC ECO:0000269|PubMed:8972187, ECO:0000269|PubMed:9288897}.
CC -!- SUBUNIT: Heterodimer of PIP2 and OAF1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: Autoregulated. Induced upon growth on fatty acids.
CC {ECO:0000269|PubMed:8972187, ECO:0000269|PubMed:9288897}.
CC -!- DOMAIN: the 9aaTAD motif (residues 985 to 993) is a transactivation
CC domain present in a large number of yeast and animal transcription
CC factors. {ECO:0000269|PubMed:17467953}.
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DR EMBL; X91991; CAA63046.1; -; Genomic_DNA.
DR EMBL; Z75271; CAA99692.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11124.1; -; Genomic_DNA.
DR PIR; S70646; S70646.
DR RefSeq; NP_015008.3; NM_001183783.3.
DR AlphaFoldDB; P52960; -.
DR BioGRID; 34748; 52.
DR ComplexPortal; CPX-1038; PIP2-OAF1 transcription factor complex.
DR DIP; DIP-1013N; -.
DR IntAct; P52960; 1.
DR MINT; P52960; -.
DR STRING; 4932.YOR363C; -.
DR iPTMnet; P52960; -.
DR MaxQB; P52960; -.
DR PaxDb; P52960; -.
DR PRIDE; P52960; -.
DR EnsemblFungi; YOR363C_mRNA; YOR363C; YOR363C.
DR GeneID; 854545; -.
DR KEGG; sce:YOR363C; -.
DR SGD; S000005890; PIP2.
DR VEuPathDB; FungiDB:YOR363C; -.
DR eggNOG; ENOG502QW20; Eukaryota.
DR GeneTree; ENSGT00940000176335; -.
DR HOGENOM; CLU_008453_0_0_1; -.
DR InParanoid; P52960; -.
DR OMA; HGPFTWH; -.
DR BioCyc; YEAST:G3O-33833-MON; -.
DR PRO; PR:P52960; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P52960; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
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 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 Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..996
FT /note="Peroxisome proliferation transcriptional regulator"
FT /id="PRO_0000114964"
FT DNA_BIND 25..52
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 879..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 985..993
FT /note="9aaTAD"
SQ SEQUENCE 996 AA; 114711 MW; A4E3895746EFCF3E CRC64;
MYFTDESSPA MNRVGKKRNR LSFVCQACRK AKTKCDQEKP RCGRCTKQNL FCIYDVARQA
APRNPNKDAT IARLKKEIRY WRNKTVDLTQ EKKDFYTALK RPTEELAARR TCKSLQENSF
PISLYKTHPR LIMTKVMKRE INPLSEKYLI FQDTFLKTLI ASVLLSCSRN SMIPALNADI
SRSRTQPCVK NNVVKMREVL LKNSKYESQR KSINEFTDRL LQRKNPEEQI AVNKVISLLY
SNRESSYLED TCPTENDYSD LLKGYINEIE KTLPPKAIIE QYLSHFFEHI FHLIPFASKE
MLEESIHTTV QYNELGEVRL SMGTTLIRNK MENLCILLLI LRIAYISLTF IEDKIEDYSP
YITKEMLEQY PIQSEVIFLA QQILASENWC ACANENTISC LLYIWCAFVF SPTEGDFLLE
QPSDVIINLV ILIGTSIGLH RDPSDFPALN HPEASDKRLL NLRRIQWLSI ISMATLESSL
KGRLLVSPLS MIDLFIDVRD PNCVEIYKKR VKKDLTGSES DEQLLEIHEI FFHRAQLALF
LSDLNNITIS YSGSVPMDTL ETLRVKANEL LKNKFQLRSV DINIYDEEKT FQKLTFNSIL
NSISLSGQIL GKLMMLRASI ALMLYFETLA MERSECLSFF YKYFFQCCAD TISLIRFFFL
YFNGSYEKVL SSLVCFITTK VIQLAVPTTM FTLLVIIMRV ELAKNMLLVK CNECNARGDI
SDLPEIKEKI KSLDTIKENF ERLLLEVYLL ASQNLRFKYF YIFKMLTLFD VFIQRLRKGQ
LFSGLFVKVD KDLTTKKIAT MLELTLGINL DKSDHLIDRL KGKNLTVNFT LDQLYQIIKE
FDRIKNIGVA DPQNSLNPSK PNMKDNTPTI ELLLNSSVEN ESVPPYSSSN DPTNVGNAST
YSLAHNISNQ NNEENMPPSI GSSESNRAAP NLNFMPINNN YNNSGSNINN NDNVKLPSNF
KNYYDPPMSS LDISMDVPDI FGSLDFFDYD LLFQND
