SREA_EMENI
ID SREA_EMENI Reviewed; 549 AA.
AC G5EB20; A0A1U8QV15; C8VQ32; Q5BH04; Q9Y754;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=GATA-type transcription factor sreA {ECO:0000303|PubMed:9988696};
DE AltName: Full=Siderophore uptake regulator sreA {ECO:0000303|PubMed:9988696};
GN Name=sreA {ECO:0000303|PubMed:9988696}; ORFNames=ANIA_00176;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=9988696; DOI=10.1074/jbc.274.8.4613;
RA Haas H., Zadra I., Stoffler G., Angermayr K.;
RT "The Aspergillus nidulans GATA factor SREA is involved in regulation of
RT siderophore biosynthesis and control of iron uptake.";
RL J. Biol. Chem. 274:4613-4619(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11555288; DOI=10.1046/j.1365-2958.2001.02586.x;
RA Oberegger H., Schoeser M., Zadra I., Abt B., Haas H.;
RT "SREA is involved in regulation of siderophore biosynthesis, utilization
RT and uptake in Aspergillus nidulans.";
RL Mol. Microbiol. 41:1077-1089(2001).
RN [5]
RP FUNCTION.
RX PubMed=12196195; DOI=10.1042/bst0300781;
RA Oberegger H., Zadra I., Schoeser M., Abt B., Parson W., Haas H.;
RT "Identification of members of the Aspergillus nidulans SREA regulon: genes
RT involved in siderophore biosynthesis and utilization.";
RL Biochem. Soc. Trans. 30:781-783(2002).
RN [6]
RP FUNCTION.
RX PubMed=12487628; DOI=10.1042/bj20021685;
RA Haas H., Schoeser M., Lesuisse E., Ernst J.F., Parson W., Abt B.,
RA Winkelmann G., Oberegger H.;
RT "Characterization of the Aspergillus nidulans transporters for the
RT siderophores enterobactin and triacetylfusarinine C.";
RL Biochem. J. 371:505-513(2003).
CC -!- FUNCTION: GATA-type transcription repressor that regulates
CC iron- acquisition genes through specific binding GATA sequence elements
CC of target promoters (PubMed:9988696, PubMed:11555288). Iron acquisition
CC regulation is critical for survival under both iron-limiting conditions
CC (to acquire essential iron) and iron-replete conditions (to limit iron
CC toxicity) (PubMed:11555288). SreA targets include genes encoding a
CC number of key iron-regulated factors such as those involved in
CC siderophore biosynthesis (PubMed:11555288, PubMed:12196195,
CC PubMed:12487628). {ECO:0000269|PubMed:11555288,
CC ECO:0000269|PubMed:12196195, ECO:0000269|PubMed:12487628,
CC ECO:0000269|PubMed:9988696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Expression is induced in mycelia grown in high iron medium
CC or transferred from low iron medium into high iron medium, and
CC repressed in mycelia grown in low iron medium or transferred from high
CC iron medium into low iron medium (PubMed:9988696).
CC {ECO:0000269|PubMed:9988696}.
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: Leads to increased iron uptake (PubMed:9988696).
CC leads to partial derepression of triacetylfusarinine C (TAFC) and
CC fusigen production as well as to cellular accumulation of ferricrocin
CC (FC) (PubMed:11555288). Leads also to increased oxidative stress
CC (PubMed:11555288). {ECO:0000269|PubMed:11555288,
CC ECO:0000269|PubMed:9988696}.
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DR EMBL; AF095898; AAD25328.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF90036.1; -; Genomic_DNA.
DR EMBL; AACD01000005; EAA66049.1; -; Genomic_DNA.
DR RefSeq; XP_657780.1; XM_652688.1.
DR AlphaFoldDB; G5EB20; -.
DR SMR; G5EB20; -.
DR STRING; 162425.CADANIAP00002559; -.
DR EnsemblFungi; CBF90036; CBF90036; ANIA_00176.
DR EnsemblFungi; EAA66049; EAA66049; AN0176.2.
DR GeneID; 2875952; -.
DR KEGG; ani:AN0176.2; -.
DR VEuPathDB; FungiDB:AN0176; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_021761_1_0_1; -.
DR InParanoid; G5EB20; -.
DR OMA; CYRPTTM; -.
DR OrthoDB; 1466754at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AspGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:AspGD.
DR GO; GO:0034757; P:negative regulation of iron ion transport; IMP:AspGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 2.
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 2: Evidence at transcript level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..549
FT /note="GATA-type transcription factor sreA"
FT /id="PRO_0000444401"
FT ZN_FING 106..130
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 251..275
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 40..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..198
FT /note="Cystein-rich region (CRR)"
FT /evidence="ECO:0000250|UniProtKB:Q1K8E7"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..549
FT /evidence="ECO:0000255"
FT COMPBIAS 44..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 58842 MW; 559DCF02AEFD62E3 CRC64;
MLASIPHMET LRSLPRNPDV VARHPSAEDL DAAQQLISSA QAGREHPQDR HYTDNGSRKS
EAGAPHSHHE GEYPIVQTSE TPMNGHHVEK TSPKSQKDTS FLGHSCSNCG TKSTPLWRRS
PTGAMICNAC GLYLKARNVA RPTKRNRTQA SPEAYHPQNQ SVGSQPDPAV TGSEGCTGSC
PGGGNCNGTG GAEGCDGCPA YNNRVYKSTA RGNVAAHALN RAGNSDAVPS PEAEAPARNS
GQPEGNMLVA CQNCGTTVTP LWRRDENGHP ICNACGLYYK LHGSYRPTTM KKTIIKRRKR
VVPALRENSP TAATHSSHGS SASPEASSPA TLAYSHDERH RYYSSEPVDQ YHRISPAAQR
PFGFAPPPVD FTNFNSGAVT LPHHPPPPRL LEPGHPPLSQ FARRSISPSS SGNSKKRTLA
EAGANTDTGP VPTTLEAGSN QLPPIVSSAN PPPPARLSSI SSILNHAHAR DESRLDPSLA
ALGRQQQSQP HHPQSSPLAP TQAASQSLPG VSNMDNHVED RRAKLQREAE EMREQLRAKE
RELAELAGQ
