SREA_NEUCR
ID SREA_NEUCR Reviewed; 587 AA.
AC Q1K8E7;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=GATA-type transcription factor sre {ECO:0000303|PubMed:9790585};
DE AltName: Full=Siderophore uptake regulator sreA {ECO:0000303|PubMed:9790585};
GN Name=sre {ECO:0000303|PubMed:9790585}; ORFNames=NCU07728;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=9790585; DOI=10.1007/s004380050845;
RA Zhou L.W., Haas H., Marzluf G.A.;
RT "Isolation and characterization of a new gene, sre, which encodes a GATA-
RT type regulatory protein that controls iron transport in Neurospora
RT crassa.";
RL Mol. Gen. Genet. 259:532-540(1998).
RN [3]
RP FUNCTION, DNA-BINDING, DOMAIN, AND MUTAGENESIS OF 284-ASN--GLY-286 AND
RP 305-ALA-CYS-306.
RX PubMed=10194352; DOI=10.1021/bi982543f;
RA Zhou L., Marzluf G.A.;
RT "Functional analysis of the two zinc fingers of SRE, a GATA-type factor
RT that negatively regulates siderophore synthesis in Neurospora crassa.";
RL Biochemistry 38:4335-4341(1999).
RN [4]
RP FUNCTION, DNA-BINDING, DOMAIN, AND MUTAGENESIS OF CYS-204; CYS-210; CYS-219
RP AND CYS-222.
RX PubMed=12484767; DOI=10.1021/bi0204995;
RA Harrison K.A., Marzluf G.A.;
RT "Characterization of DNA binding and the cysteine rich region of SRE, a
RT GATA factor in Neurospora crassa involved in siderophore synthesis.";
RL Biochemistry 41:15288-15295(2002).
CC -!- FUNCTION: GATA-type transcription repressor that regulates
CC iron- acquisition genes through specific binding the GATA sequence
CC elements of target promoters in a zinc-dependent manner
CC (PubMed:9790585, PubMed:10194352, PubMed:12484767). 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:10194352). Represses the synthesis of siderophores in
CC high iron conditions (PubMed:9790585). {ECO:0000269|PubMed:10194352,
CC ECO:0000269|PubMed:12484767, ECO:0000269|PubMed:9790585}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: The promoter contains a number of GATA sequences; however,
CC expression occurs in a constitutive fashion and is not regulated by the
CC concentration of iron available to the cells (PubMed:9790585).
CC {ECO:0000269|PubMed:9790585}.
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 (PubMed:12484767). {ECO:0000269|PubMed:12484767}.
CC -!- DOMAIN: Both the N-terminal and C-terminal zinc fingers are involved in
CC DNA-binding, although the C-terminal finger plays a more important role
CC in the binding (PubMed:10194352). {ECO:0000269|PubMed:10194352}.
CC -!- DISRUPTION PHENOTYPE: Derepresses siderophore biosynthesis in high iron
CC concentrations (PubMed:9790585). {ECO:0000269|PubMed:9790585}.
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DR EMBL; CM002239; EAA32742.1; -; Genomic_DNA.
DR RefSeq; XP_961978.1; XM_956885.2.
DR AlphaFoldDB; Q1K8E7; -.
DR SMR; Q1K8E7; -.
DR STRING; 5141.EFNCRP00000008012; -.
DR EnsemblFungi; EAA32742; EAA32742; NCU07728.
DR GeneID; 3878126; -.
DR KEGG; ncr:NCU07728; -.
DR VEuPathDB; FungiDB:NCU07728; -.
DR HOGENOM; CLU_021761_1_0_1; -.
DR InParanoid; Q1K8E7; -.
DR OMA; CYRPTTM; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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:0008270; F:zinc ion binding; IEA:InterPro.
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; 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; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..587
FT /note="GATA-type transcription factor sre"
FT /id="PRO_0000444399"
FT ZN_FING 118..142
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 282..306
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..222
FT /note="Cystein-rich region (CRR)"
FT /evidence="ECO:0000269|PubMed:12484767"
FT REGION 335..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 553..585
FT /evidence="ECO:0000255"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 204
FT /note="C->S: Decreases DNA-binding and fails to exhibit
FT iron-mediated regulation of siderophore synthesis; when
FT associated with S-210."
FT /evidence="ECO:0000269|PubMed:12484767"
FT MUTAGEN 210
FT /note="C->S: Decreases DNA-binding and fails to exhibit
FT iron-mediated regulation of siderophore synthesis; when
FT associated with S-204."
FT /evidence="ECO:0000269|PubMed:12484767"
FT MUTAGEN 219
FT /note="C->S: Decreases DNA-binding and fails to exhibit
FT iron-mediated regulation of siderophore synthesis; when
FT associated with S-222."
FT /evidence="ECO:0000269|PubMed:12484767"
FT MUTAGEN 222
FT /note="C->S: Decreases DNA-binding and fails to exhibit
FT iron-mediated regulation of siderophore synthesis; when
FT associated with S-219."
FT /evidence="ECO:0000269|PubMed:12484767"
FT MUTAGEN 284..286
FT /note="NCG->LAF: Decreases the DNA-binding and the
FT subsequent transcription repressor activity."
FT /evidence="ECO:0000269|PubMed:10194352"
FT MUTAGEN 305..306
FT /note="AC->EL: Decreases the DNA-binding and the subsequent
FT transcription repressor activity."
FT /evidence="ECO:0000269|PubMed:10194352"
SQ SEQUENCE 587 AA; 62014 MW; B0DFC7215DB97829 CRC64;
MALPDDTRLM NNQTSIEGNS APDRMALPSR PPPPTASNEP PEHESTGPVD EAASKSESGL
SPNSKKAGHA AQSPSGRKKS PKIQNAQPAQ SPAETVGVVN VATLGLVPSV QGHAGQVCSN
CGTTHTPLWR RSPQGAIICN ACGLYLKARN AARPANIRRP PSVMASNVRQ AAAKLSPKKA
TAPLLPSNPG ATYVAADQTP SGSCPGGGRC NGTGGAEGCG GCPAYNNRVS KSASLNVLKC
QGAAAASSKK PQAAEGSGEE PTEMDITALH VQSQNTTVVI ACQNCGTTIT PLWRRDEAGH
TICNACGLYY KLHGVHRPVT MKKAIIKRRK RVIPAAGGDA EIEPSEAPDS PPATSEPPME
KGTVNEDGSV NLGIRRRSVR PLTLVPEDEL RRNRQASPLS SAALGQYHSS HTNQPHHGAH
ASLTYENRLA PIHSLALPVD RQASISPASF LSPSRKRSIS AVENEPSSHN DNESHKRLSS
IKSILNPMPS SEIHREVSPA DQLRMQPASR SPAMSSLTPA HSPGSFSNST VIGTPTSAPI
LRSASRDTHN DSERMKAERR AALEREAEMM RELLAAKERE LAELGYD
