HAP1_YEAST
ID HAP1_YEAST Reviewed; 1502 AA.
AC P0CE41; D6VYQ2; P12351; Q06574; Q6BD21;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Heme-responsive zinc finger transcription factor HAP1;
DE AltName: Full=CYP1 activatory protein;
DE AltName: Full=Heme activator protein 1;
GN Name=HAP1; Synonyms=CYP1; OrderedLocusNames=YLR256W; ORFNames=L9672.1;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 FUNCTION, AND IDENTIFICATION OF STRAIN-SPECIFIC DEFECTIVE TY1 INSERTION.
RX PubMed=10541856; DOI=10.1007/s002940050490;
RA Gaisne M., Becam A.-M., Verdiere J., Herbert C.J.;
RT "A 'natural' mutation in Saccharomyces cerevisiae strains derived from
RT S288c affects the complex regulatory gene HAP1 (CYP1).";
RL Curr. Genet. 36:195-200(1999).
RN [4]
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 [5]
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: Regulation of oxygen dependent gene expression. It modulates
CC the expression of Iso-1 (CYP1) and Iso-2 (CYP3) cytochrome c. In
CC response to heme, promotes transcription of genes encoding functions
CC required for respiration, controlling oxidative damage and repression
CC of anaerobic genes. Binds to the sequence 5'-CGGNNNTNNCGG-3' (By
CC similarity). Is non-functional in terms of iso-1 cytochrome c
CC expression in strain S288c and its derivatives. {ECO:0000250,
CC ECO:0000269|PubMed:10541856}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Interacts with SRO9 and YDJ1. In the
CC absence of heme, binds to at least four cellular proteins, including
CC YDJ1 and SRO9, forming a high-molecular-weight complex (HMC) which
CC results in repression of its activity and dictates its DNA-binding
CC specificity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- MISCELLANEOUS: Heme is an effector molecule for CYP1/HAP1. The HRM
CC repeat region mediates heme induction by masking the DNA-binding domain
CC in the absence of inducer (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The sequence for strain S288c and its derivatives
CC differs from other strain backgrounds due to the insertion of a
CC defective Ty1 element in the C-terminus. This acts as a null allele in
CC terms of iso-1 cytochrome c expression and beta-galactosidase activity.
CC Also, the expression levels of ergosterol-related genes and ergosterol
CC content are decreased in laboratory strain X2180 caused by the
CC defective Ty1 insertion. The sequence of a wild-type allele can be
CC found in other strain backgrounds (AC P0CS82).
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DR EMBL; U20865; AAB67387.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09568.1; -; Genomic_DNA.
DR PIR; S59400; RGBYH1.
DR RefSeq; NP_013357.1; NM_001182143.1.
DR AlphaFoldDB; P0CE41; -.
DR SMR; P0CE41; -.
DR BioGRID; 31522; 73.
DR ComplexPortal; CPX-1276; HMC complex.
DR ComplexPortal; CPX-1882; HAP1 transcriptional repressor complex, SSA1 variant.
DR ComplexPortal; CPX-1883; HAP1 transcriptional repressor complex, SSA2 variant.
DR IntAct; P0CE41; 4.
DR MINT; P0CE41; -.
DR STRING; 4932.YLR256W; -.
DR iPTMnet; P0CE41; -.
DR MaxQB; P0CE41; -.
DR PaxDb; P0CE41; -.
DR PRIDE; P0CE41; -.
DR EnsemblFungi; YLR256W_mRNA; YLR256W; YLR256W.
DR GeneID; 850958; -.
DR KEGG; sce:YLR256W; -.
DR SGD; S000004246; HAP1.
DR VEuPathDB; FungiDB:YLR256W; -.
DR eggNOG; ENOG502QRPQ; Eukaryota.
DR HOGENOM; CLU_004380_0_0_1; -.
DR InParanoid; P0CE41; -.
DR OMA; QDNETHQ; -.
DR BioCyc; YEAST:G3O-32359-MON; -.
DR ChiTaRS; HAP1; yeast.
DR PRO; PR:P0CE41; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P0CE41; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0017053; C:transcription repressor complex; IC:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:SGD.
DR GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:SGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070482; P:response to oxygen levels; IC:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
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; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR SUPFAM; SSF57959; SSF57959; 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; Coiled coil; DNA-binding; Heme; Iron; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..1502
FT /note="Heme-responsive zinc finger transcription factor
FT HAP1"
FT /id="PRO_0000114945"
FT REPEAT 280..285
FT /note="HRM 1"
FT REPEAT 299..304
FT /note="HRM 2"
FT REPEAT 323..328
FT /note="HRM 3"
FT REPEAT 347..352
FT /note="HRM 4"
FT REPEAT 389..394
FT /note="HRM 5"
FT REPEAT 415..420
FT /note="HRM 6"
FT REPEAT 1192..1197
FT /note="HRM 7"
FT DNA_BIND 64..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 126..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..444
FT /note="Heme-responsive; required for HMC formation"
FT /evidence="ECO:0000250"
FT REGION 432..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..134
FT /evidence="ECO:0000255"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1502 AA; 166108 MW; 8782016801E3D555 CRC64;
MSNTPYNSSV PSIASMTQSS VSRSPNMHTA TTPGANTSSN SPPLHMSSDS SKIKRKRNRI
PLSCTICRKR KVKCDKLRPH CQQCTKTGVA HLCHYMEQTW AEEAEKELLK DNELKKLRER
VKSLEKTLSK VHSSPSSNSL KSYNTPESSN LFMGSDEHTT LVNANTGSAS SASHMHQQQQ
QQQQQEQQQD FSRSANANAN SSSLSISNKY DNDELDLTKD FDLLHIKSNG TIHLGATHWL
SIMKGDPYLK LLWGHIFAMR EKLNEWYYQK NSYSKLKSSK CPINHAQAPP SAAAAATRKC
PVDHSAFSSG MVAPKEETPL PRKCPVDHTM FSSGMIPPRE DTSSQKRCPV DHTMYSAGMM
PPKDETPSPF STKAMIDHNK HTMNPPQSKC PVDHRNYMKD YPSDMANSSS NPASRCPIDH
SSMKNTAALP ASTHNTIPHH QPQSGSHARS HPAQSRKHDS YMTESEVLAT LCEMLPPKRV
IALFIEKFFK HLYPAIPILD EQNFKNHVNQ MLSLSSMNPT VNNFGMSMPS SSTLENQPIT
QINLPKLSDS CNLGILIIIL RLTWLSIPSN SCEVDLGEES GSFLVPNESS NMSASALTSM
AKEESLLLKH ETPVEALELC QKYLIKFDEL SSISNNNVNL TTVQFAIFYN FYMKSASNDL
TTLTNTNNTG MANPGHDSES HQILLSNITQ MAFSCGLHRD PDNFPQLNAT IPATSQDVSN
NGSKKANPST NPTLNNNMSA ATTNSSSRSG SADSRSGSNP VNKKENQVSI ERFKHTWRKI
WYYIVSMDVN QSLSLGSPRL LRNLRDFSDT KLPSASRIDY VRDIKELIIV KNFTLFFQID
LCIIAVLNHI LNVSLARSVR KFELDSLINL LKNLTYGTEN VNDVVSSLIN KGLLPTSEGG
SVDSNNDEIY GLPKLPDILN HGQHNQNLYA DGRNTSSSDI DKKLDLPHES TTRALFFSKH
MTIRMLLYLL NYILFTHYEP MGSEDPGTNI LAKEYAQEAL NFAMDGYRNC MIFFNNIRNT
NSLFDYMNVI LSYPCLDIGH RSLQFIVCLI LRAKCGPLTG MRESSIITNG TSSGFNSSVE
DEDVKVKQES SDELKKDDFM KDVNLDSGDS LAEILMSRML LFQKLTKQLS KKYNYAIRMN
KSTGFFVSLL DTPSKKSDSK SGGSSFMLGN WKHPKVSNMS GFLAGDKDQL QKCPVYQDAL
GFVSPTGANE GSAPMQGMSL QGSTARMGGT QLPPIRSYKP ITYTSSNLRR MNETGEAEAK
RRRFNDGYID NNSNNDIPRG ISPKPSNGLS SVQPLLSSFS MNQLNGGTIP TVPSLTNITS
QMGALPSLDR ITTNQINLPD PSRDEAFDNS IKQMTPMTSA FMNANTTIPS STLNGNMNMN
GAGTANTDTS ANGSALSTLT SPQGSDLASN SATQYKPDLE DFLMQNSNFN GLMINPSSLV
EVVGGYNDPN NLGRNDAVDF LPVDNVEIDG VGIKINYHLL TSIYVTSILS YTVLEDDAND
EK
