CUF1_SCHPO
ID CUF1_SCHPO Reviewed; 411 AA.
AC Q09728;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Metal-binding regulatory protein cuf1;
GN Name=cuf1; ORFNames=SPAC31A2.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=FY254;
RX PubMed=10593913; DOI=10.1074/jbc.274.51.36252;
RA Labbe S., Pena M.M.O., Fernandes A.R., Thiele D.J.;
RT "A copper-sensing transcription factor regulates iron uptake genes in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 274:36252-36260(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-13; ARG-16; ARG-19;
RP LYS-24; ARG-28; LYS-45; ARG-47; ARG-50; ARG-53; CYS-328; CYS-330; CYS-334;
RP CYS-336 AND CYS-339.
RX PubMed=16467469; DOI=10.1128/ec.5.2.277-292.2006;
RA Beaudoin J., Labbe S.;
RT "Copper induces cytoplasmic retention of fission yeast transcription factor
RT cuf1.";
RL Eukaryot. Cell 5:277-292(2006).
CC -!- FUNCTION: Copper-sensing transcription factor that regulates iron
CC uptake genes. Under copper starvation conditions activates the
CC transcription of the copper transport genes, ctr4, ctr5 and ctr6.
CC {ECO:0000269|PubMed:10593913, ECO:0000269|PubMed:16467469}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16467469}. Nucleus
CC {ECO:0000269|PubMed:16467469}. Note=Cytoplasmic in presence of excess
CC copper ions. The Cys-His motif (328-342) interacts with the N-terminal
CC nuclear localization signal region leading to sequestration in the
CC cytoplasm. Nuclear under copper starvation conditions.
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DR EMBL; AF175404; AAD51063.1; -; Genomic_DNA.
DR EMBL; AJ243832; CAB52304.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA90469.1; -; Genomic_DNA.
DR PIR; T38609; S58105.
DR RefSeq; NP_592923.1; NM_001018324.2.
DR AlphaFoldDB; Q09728; -.
DR SMR; Q09728; -.
DR BioGRID; 279627; 10.
DR STRING; 4896.SPAC31A2.11c.1; -.
DR MaxQB; Q09728; -.
DR PaxDb; Q09728; -.
DR EnsemblFungi; SPAC31A2.11c.1; SPAC31A2.11c.1:pep; SPAC31A2.11c.
DR GeneID; 2543198; -.
DR KEGG; spo:SPAC31A2.11c; -.
DR PomBase; SPAC31A2.11c; cuf1.
DR VEuPathDB; FungiDB:SPAC31A2.11c; -.
DR eggNOG; ENOG502S7CA; Eukaryota.
DR HOGENOM; CLU_669319_0_0_1; -.
DR InParanoid; Q09728; -.
DR OMA; MACMKCI; -.
DR PRO; PR:Q09728; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005507; F:copper ion binding; IMP:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:PomBase.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:PomBase.
DR GO; GO:0035874; P:cellular response to copper ion starvation; IC:GOC-OWL.
DR GO; GO:0055070; P:copper ion homeostasis; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:PomBase.
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 1: Evidence at protein level;
KW Copper; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..411
FT /note="Metal-binding regulatory protein cuf1"
FT /id="PRO_0000194930"
FT DNA_BIND 1..40
FT /note="Copper-fist"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT REGION 63..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..92
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:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT MUTAGEN 13
FT /note="K->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 16
FT /note="R->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 19
FT /note="R->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 24
FT /note="K->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 28
FT /note="R->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 45
FT /note="K->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 47
FT /note="R->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 50
FT /note="R->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 53
FT /note="R->A: No nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 328
FT /note="C->A: Constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 330
FT /note="C->A: Constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 334
FT /note="C->A: Constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 336
FT /note="C->A: Constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
FT MUTAGEN 339
FT /note="C->A: Constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:16467469"
SQ SEQUENCE 411 AA; 45473 MW; DB18E877B65D5699 CRC64;
MVVINNVKMA CMKCIRGHRS STCKHNDREL FPIRPKGRPI SQCEKCRIAR ITRHLHVKCT
CNSRKKGSKC STSSTTDLDS SSASNSSCSI PSSISEKLLP RDNVKTHCPK RSASCCGKKP
DVMPLKINLE SQTDFMGMPL QSQRPHSESY RMLPEPEKFK SEYGYPSQFL PIEKLTSNVA
YPPNYNNYLK SPYQQPTNFP PEIQYNYSHS PQHSIQEAEE AAVYGPPVYR SGYQILYNNN
TDSIAAAAAT HDLYPQPDVP LTFAMLADGN YVPLPSSTNT YGPSNSYGYE ININESTNHV
DSSYLPHPIQ LSNYFTLPSS CAQADAACQC GDNCECLGCL THPNNATTLA ALNHISALEK
ETISHTDLHH TFKHEVNSSN NYELTNDELA ASSPLYTSSS VPPSHITTGS T
