HAP1_YEAS8
ID HAP1_YEAS8 Reviewed; 1483 AA.
AC C8ZDL9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
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; ORFNames=EC1118_1L7_1046g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(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). {ECO:0000250}.
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 repeat
CC region (see FT table) mediates heme induction by masking the DNA-
CC binding domain in the absence of inducer (By similarity).
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN393080; CAY81485.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZDL9; -.
DR SMR; C8ZDL9; -.
DR EnsemblFungi; CAY81485; CAY81485; EC1118_1L7_1046g.
DR HOGENOM; CLU_004380_0_0_1; -.
DR Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L7.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 3: Inferred from homology;
KW Activator; Coiled coil; DNA-binding; Heme; Iron; Metal-binding; Nucleus;
KW Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..1483
FT /note="Heme-responsive zinc finger transcription factor
FT HAP1"
FT /id="PRO_0000392062"
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 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 1483 AA; 164224 MW; 3959612138A642BE 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 HPAQNRKHDS 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 SDEMKKDDFM 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 VNGSALSTLT SPQGSDLASN SATQYKPDLE DFLMQNSNFN GLMINPSSLV
EVVGGYNDPN NLGRNDAVDF LPVDNVEIDG LVDFYRADFP IWE
