ID   GRISA_PODAS             Reviewed;         597 AA.
AC   Q92258;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Protein GRISEA;
DE   AltName: Full=MAC1 homolog;
GN   Name=grisea {ECO:0000312|EMBL:CAA61598.1};
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1] {ECO:0000312|EMBL:CAA61598.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s {ECO:0000312|EMBL:CAA61598.1};
RX   PubMed=8804410; DOI=10.1007/bf02173211;
RA   Osiewacz H.D., Nuber U.;
RT   "GRISEA, a putative copper-activated transcription factor from Podospora
RT   anserina involved in differentiation and senescence.";
RL   Mol. Gen. Genet. 252:115-124(1996).
RN   [2] {ECO:0000305}
RP   MUTANT GRISEA.
RX   PubMed=9380708; DOI=10.1073/pnas.94.20.10768;
RA   Borghouts C., Kimpel E., Osiewacz H.D.;
RT   "Mitochondrial DNA rearrangements of Podospora anserina are under the
RT   control of the nuclear gene grisea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:10768-10773(1997).
RN   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=9894921; DOI=10.1007/s004380050922;
RA   Borghouts C., Osiewacz H.D.;
RT   "GRISEA, a copper-modulated transcription factor from Podospora anserina
RT   involved in senescence and morphogenesis, is an ortholog of MAC1 in
RT   Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 260:492-502(1998).
RN   [4] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11134328; DOI=10.1128/mcb.21.2.390-399.2001;
RA   Borghouts C., Werner A., Elthon T., Osiewacz H.D.;
RT   "Copper-modulated gene expression and senescence in the filamentous fungus
RT   Podospora anserina.";
RL   Mol. Cell. Biol. 21:390-399(2001).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=12200031; DOI=10.1016/s1357-2725(02)00078-x;
RA   Borghouts C., Scheckhuber C.Q., Stephan O., Osiewacz H.D.;
RT   "Copper homeostasis and aging in the fungal model system Podospora
RT   anserina: differential expression of PaCtr3 encoding a copper
RT   transporter.";
RL   Int. J. Biochem. Cell Biol. 34:1355-1371(2002).
CC   -!- FUNCTION: Copper-sensing transcription factor that regulates copper
CC       uptake by transactivation of Ctr3, a high affinity copper permease.
CC       Binds to the palindromic UAS sequence 5'-TGTTGCTCANNNNAGAGCAACT-3'.
CC       Also transactivates Sod2, a mitochondrial manganese superoxide
CC       dismutase through the palindromic UAS sequence 5'-GTTTGCTCA-3' with 352
CC       bp separating the two inverted repeats. Loss of function indirectly
CC       leads to rearrangement of mitochondrial DNA associated with senescence
CC       in wild-type strains. {ECO:0000269|PubMed:11134328,
CC       ECO:0000269|PubMed:12200031, ECO:0000269|PubMed:9894921}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; X89429; CAA61598.1; -; Genomic_DNA.
DR   PIR; S72468; S72468.
DR   AlphaFoldDB; Q92258; -.
DR   VEuPathDB; FungiDB:PODANS_4_8950; -.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 3.90.430.10; -; 1.
DR   InterPro; IPR001083; Cu_fist_DNA-bd_dom.
DR   InterPro; IPR036395; Cu_fist_DNA-bd_dom_sf.
DR   Pfam; PF00649; Copper-fist; 1.
DR   PRINTS; PR00617; COPPERFIST.
DR   SMART; SM01090; Copper-fist; 1.
DR   SMART; SM00412; Cu_FIST; 1.
DR   SUPFAM; SSF57879; SSF57879; 1.
DR   PROSITE; PS01119; COPPER_FIST_1; 1.
DR   PROSITE; PS50073; COPPER_FIST_2; 1.
PE   3: Inferred from homology;
KW   Activator; Copper; DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..597
FT                   /note="Protein GRISEA"
FT                   /id="PRO_0000194929"
FT   DNA_BIND        1..41
FT                   /note="Copper-fist"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT   REGION          70..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..260
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..316
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..520
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P41772,
FT                   ECO:0000255|PROSITE-ProRule:PRU00055"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P41772,
FT                   ECO:0000255|PROSITE-ProRule:PRU00055"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P41772,
FT                   ECO:0000255|PROSITE-ProRule:PRU00055"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P41772,
FT                   ECO:0000255|PROSITE-ProRule:PRU00055"
SQ   SEQUENCE   597 AA;  62302 MW;  39DC3895C96DA30B CRC64;
     MPIINGQKMA CGPCIRGHRS TKCNHYNERV MVPVRKPGRP LSTCPCPPGK PCVCGGVRVA
     IPKKQKCHCP AGTVDSATSS EFDPSPVDTP ISPASRTSSN RVTKSGSGSK SASRRQSLAL
     ANLERMDPNS INLIPSPNGN GMIGITAMVS PRDATFGHPM GMVPMGPRES FVPAPPPDFG
     GPMGYNMPPS MPPHMPPPHY PPHIQIPQHI KTENGGFVPM LNGTFVSPVP IPAFVDGPHP
     QGMQAFNGPP PPPPSNPVLE PSAMSKPKGG SGGGGCCGGG KKAPQIQAPP PVPAPLPTPP
     QQQMPNIMPP PQPQNAPSGG GGSCCSSKSS QPPPMPQMSP NAMQAPPQPG FGQGFMPQYQ
     TPIDIKMENM HHHQPFQFPG QTVFTYPAEY GSWQMPINPA IWQQVVSRPP TQQQHETPIS
     ATAPNGNNGT VGGNSHECGC GEGCQCVGCL AHPFNSQMLQ YVQNAYSPNS SHGNSGSADS
     SANASPSANP LNLASPVEIP SGPELPPSHQ TQPQPPPRPN ANESDGSSNA PTPPNEGSPA
     LSNEEELTAL DYYFVHLPIS ALCGGALDMC PCDESCECVG CLVHNTAGFP QGDGGFS