SREA_AJECA
ID SREA_AJECA Reviewed; 630 AA.
AC B4XXY3;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=GATA-type transcription factor SRE1 {ECO:0000303|PubMed:18549241};
DE AltName: Full=Siderophore uptake regulator SRE1 {ECO:0000303|PubMed:18549241};
GN Name=SRE1 {ECO:0000303|PubMed:18549241};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DNA-BINDING, AND
RP MUTAGENESIS OF CYS-128; CYS-131; CYS-219; CYS-225; CYS-234; CYS-237;
RP CYS-291 AND CYS-294.
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=18549241; DOI=10.1021/bi800066s;
RA Chao L.Y., Marletta M.A., Rine J.;
RT "Sre1, an iron-modulated GATA DNA-binding protein of iron-uptake genes in
RT the fungal pathogen Histoplasma capsulatum.";
RL Biochemistry 47:7274-7283(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22117028; DOI=10.1128/ec.05274-11;
RA Hwang L.H., Seth E., Gilmore S.A., Sil A.;
RT "SRE1 regulates iron-dependent and -independent pathways in the fungal
RT pathogen Histoplasma capsulatum.";
RL Eukaryot. Cell 11:16-25(2012).
CC -!- FUNCTION: GATA-type transcription repressor that regulates
CC iron- acquisition genes through specific binding the GATA sequence
CC element 5'-(G/A)ATC(T/A)GATAA-3' of target promoters in an iron- and
CC zinc-dependent manner (PubMed:18549241, PubMed:22117028). Regulation
CC occurs via direct binding of iron ions (PubMed:18549241). Iron
CC acquisition regulation is critical for survival under both iron-
CC limiting conditions (to acquire essential iron) and iron-replete
CC conditions (to limit iron toxicity) (PubMed:22117028). SRE1 targets
CC include genes encoding a number of key iron-regulated factors such as
CC those involved in siderophore biosynthesis, presumed ferric reductase
CC activity, iron-responsive transcriptional regulation, oxidative stress
CC response, as well as genes encoding a number of putative
CC oxidoreductases, metabolic and mitochondrial enzymes, superoxide
CC dismutase, and genes previously identified as induced during
CC nitrosative stress (PubMed:22117028). {ECO:0000269|PubMed:18549241,
CC ECO:0000269|PubMed:22117028}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed in high-iron medium, whereas
CC expression is reduced approximately 2.5-fold when an iron chelator,
CC such as deferoxamine, is added to the growth medium (PubMed:18549241).
CC {ECO:0000269|PubMed:18549241}.
CC -!- DOMAIN: The conserved cystein-rich region (CRR) localized between the
CC zinc fingers is also involved in DNA-binding and transcription
CC repressor activity (By similarity). {ECO:0000250|UniProtKB:Q1K8E7}.
CC -!- DISRUPTION PHENOTYPE: Impairs the repression of siderophore
CC biosynthesis and utilization genes in the presence of abundant iron and
CC thus produces siderophores even under iron-replete conditions
CC (PubMed:22117028). {ECO:0000269|PubMed:22117028}.
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DR EMBL; EU220030; ABY66603.1; -; Genomic_DNA.
DR AlphaFoldDB; B4XXY3; -.
DR SMR; B4XXY3; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="GATA-type transcription factor SRE1"
FT /id="PRO_0000444403"
FT ZN_FING 128..152
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 291..315
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..237
FT /note="Cystein-rich region (CRR)"
FT /evidence="ECO:0000250|UniProtKB:Q1K8E7"
FT REGION 256..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 595..630
FT /evidence="ECO:0000255"
FT COMPBIAS 62..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 128
FT /note="C->A: In gzf1; decreases both the number of zinc and
FT iron ions bound and the ability to bind DNA; when
FT associated with A-131."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 131
FT /note="C->A: In gzf1; decreases both the number of zinc and
FT iron ions bound and the ability to bind DNA; when
FT associated with A-128."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 219
FT /note="C->A: In crr1; decreases both the number of iron
FT ions bound and the ability to bind DNA; when associated
FT with A-225."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 225
FT /note="C->A: In crr1; decreases both the number of iron
FT ions bound and the ability to bind DNA; when associated
FT with A-219."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 234
FT /note="C->A: In crr2; decreases both the number of iron
FT ions bound and the ability to bind DNA; when associated
FT with A-237."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 237
FT /note="C->A: In crr2; decreases both the number of iron
FT ions bound and the ability to bind DNA; when associated
FT with A-234."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 291
FT /note="C->A: In gzf2; decreases both the number of zinc and
FT iron ions bound and the ability to bind DNA; when
FT associated with A-294."
FT /evidence="ECO:0000269|PubMed:18549241"
FT MUTAGEN 294
FT /note="C->A: In gzf2; decreases both the number of zinc and
FT iron ions bound and the ability to bind DNA; when
FT associated with A-291."
FT /evidence="ECO:0000269|PubMed:18549241"
SQ SEQUENCE 630 AA; 67308 MW; 1F6DF731B1254B64 CRC64;
MTGLLASRLR AEGARSPTKG TDIPMRQPSA EDLDAAHQLV SSARGGRDNV MNFRSDRQEM
TGKALDNTQG DGSRNMDSQL QNGHKAPVEQ RAGESPPESG ANPIDHPTSS KKSPKAQSKE
QAFTGHSCSN CGTKRTPLWR RSPTGATICN ACGLYLKARN TDRPTHRSRS LLTPYGSSSA
QTLDKSRSST SPTNDGNDPR LTDTWSNYAV KECTPSGSCP GGGSCNGTGG AEGCDGCPAY
NNRVYKSAAR NAMALHTPRT SPQVSTQGGP GSTEGDAGSS NPETMTLHIA CQNCQTTVTP
LWRRDENGHP ICNACGLYHK LHGAYRPPTM KKSIIKRRKR VVPAMREQSP PSATQSSNGS
VSPEASPAAL AHNHDSHRQY QNVEHGNGHP PPHTRPLYSH AYHAPPPADF TGYTSNVISL
PHHPPSTSQQ LRPYDNNHNN GETTNTHRAP MPALHNPKKR TISESSIEDS QRPQASQILT
HIPQINPPTP PSSSSASFPN NNPGRFNSIS SLLNHPGEAA TVTAHDRDDS RVDPALSSAV
APRTQQPQQE HQHASAGSHS PPRFSPSLSP APPSTTAVPV GGGSGSGAAA VAGVVDHRDA
KAERRARLQR EAQDMREALK AKERELALLE
