HAP1_YEASK
ID HAP1_YEASK Reviewed; 1480 AA.
AC G2WJ80; G2WJ81; P0CE42; P12351; Q06574; Q6BD21;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 45.
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=SYK7_048311/048321;
OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=721032;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-815 AND 892-1480.
RC STRAIN=Kyokai no. 7 / NBRC 101557;
RX PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT 7.";
RL DNA Res. 18:423-434(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 505-1480.
RC STRAIN=Kyokai no. 7 / NBRC 101557;
RX PubMed=16233684; DOI=10.1016/s1389-1723(04)00260-9;
RA Tamura K., Gu Y., Wang Q., Yamada T., Ito K., Shimoi H.;
RT "A hap1 mutation in a laboratory strain of Saccharomyces cerevisiae results
RT in decreased expression of ergosterol-related genes and cellular ergosterol
RT content compared to sake yeast.";
RL J. Biosci. Bioeng. 98:159-166(2004).
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'. Is non-
CC functional in terms of iso-1 cytochrome c expression in strain S288c
CC and its derivatives (By 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 HRM
CC repeat region mediates heme induction by masking the DNA-binding domain
CC in the absence of inducer (By similarity). {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; DG000048; GAA25123.1; -; Genomic_DNA.
DR EMBL; DG000048; GAA25124.1; -; Genomic_DNA.
DR EMBL; AB161977; BAD35005.1; -; Genomic_DNA.
DR AlphaFoldDB; G2WJ80; -.
DR SMR; G2WJ80; -.
DR EnsemblFungi; GAA25123; GAA25123; SYK7_048311.
DR EnsemblFungi; GAA25124; GAA25124; SYK7_048321.
DR HOGENOM; CLU_346690_0_0_1; -.
DR Proteomes; UP000001608; Chromosome XII.
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..1480
FT /note="Heme-responsive zinc finger transcription factor
FT HAP1"
FT /id="PRO_0000415343"
FT REPEAT 280..285
FT /note="HRM 1"
FT REPEAT 296..301
FT /note="HRM 2"
FT REPEAT 320..325
FT /note="HRM 3"
FT REPEAT 344..349
FT /note="HRM 4"
FT REPEAT 386..391
FT /note="HRM 5"
FT REPEAT 412..417
FT /note="HRM 6"
FT REPEAT 1189..1194
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..441
FT /note="Heme-responsive; required for HMC formation"
FT /evidence="ECO:0000250"
FT REGION 429..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1408
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 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..763
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"
FT CONFLICT 621
FT /note="L -> S (in Ref. 2; BAD35005)"
FT /evidence="ECO:0000305"
FT CONFLICT 953
FT /note="F -> S (in Ref. 2; BAD35005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1099
FT /note="D -> G (in Ref. 2; BAD35005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1480 AA; 164008 MW; D16AC4A4BB443E9B CRC64;
MSNTPYNSSV PSIASMTQSS VSRSPNMHTA TTPGANTSSN SPPLHMSSDS SKIKRKRNRI
PLSCTICRKR KVKCDKLRPH CQQCTKTGVA HLCHYMEQTW AEEAEKELLK DNELKKLRER
VKSLEKTLSK VHSSPSSNSL KSYNTPESSN LFMGNDEHTT LVNANTGSAS SASHMHQQQQ
QQQQQEQQQD FSRSANANAN SSSLSISNKY DNDELDLTKD FDLLHIKSNG TIHLGATHWL
SIMKGDPYLK LLWGHIFAMR EKLNEWYYQK NSYSKLKSSK CPINHAQAPP SAATRKCPVD
HSAFSSGMVA PKEETPLPRK CPVDHTMFSS GMIPPREDTS SQKRCPVDHT MYSAGMMPPK
DETPSPFSTK AMIDHNKHTM NPPQSKCPVD HRNYMKEYPS DMANSSSNPA SRCPIDHSSM
KNTAALPAST HNTIPHHQPQ SGSHARSHPA QSRKHDSYMT ESEVLATLCE MLPPKRVIAL
FIEKFFKHLY PAIPILDEQN FKNHMNQMLS LSSMNPTVNN FGMSMPSSST LENQPITQIN
LPKLSDSCNL GILIIILRLT WLSIPSNSCE VDLGEESGSF LVPNESSNMS ASALTSMAKE
ESLLLKHETP VEALELCQKY LIKFDELSNI SNNNVNLTTV QFAIFYNFYM KSASNDLTTL
TNTNNTGMAN PGHDSESHQI LLSNITQMAF SCGLHRDPDN FPQLNATIPA TSQDVSNNGS
KKANPSTNPT LNNNMSAATT NSSSRSGSAD SRSGSNPVNK KENQVSIERF KHTWRKIWYY
IVSMDVNQSL SLGSPRLLRN LRDFSDTKLP SASRIDYVRD IKELIIVKNF TLFFQIDLCI
IAVLNHILNV SLARSVRKFE LDSLINLLKN LTYGTENVND VVGSLINKGL LPTSEGGSVD
SNNDEIYGLP KLPDILNHGQ HNQNLYADGR NTSSSDIDKK LDLPHESTTR ALFFSKHMTI
RMLLYLLNYI LFTHYEPMGS EDPGTNILAK EYAQEALNFA MDGYRNCMIF FNNIRNTNSL
FDYMNVILSY PCLDIGHRSL QFIVCLILRA KCGPLTGMRE SSIITNGTSS GFNSSVEDED
VKVKQESSDE LKKDDFMKDV NLDSGDSLAE ILMSRMLLFQ KLTKQLSKKY NYAIRMNKST
GFFVSLLDTP SKKSDSKSGG SSFMLGNWKH PKVSNMSGFL AGDKDQLQKC PVYQDALGFV
SPTGANEGSA PMQGMSLQGS TARMGGTQLP PIRSYKPITY TSSNLRRMNE TGEAEAKRRR
FNDGYIDNNS NNDIPRGISP KPSNGLSSVQ PLLSSFSMNQ LNGGTIPTVP SLTNITSQMG
ALPSLDRITT NQINLPDPSR DEAFDNSIKQ MTPMTSAFMN ANTTIPSSTL NGNMNMNGAG
TANTDTSANG SALSTLTSPQ GSDLASNSAT QYKPDLEDFL MQNSNFNGLM INPSSLVEVV
GGYNDPNNLG RNDAVDFLPV DNVEIDGLVD FYRADFPIWE
