IED ID |
IndEnz0015000120 |
Enzyme Type ID |
laccase000120 |
Protein Name |
Copper-dependent transcription factor 1
|
Gene Name |
CUF1 CNAG_07724 |
Organism |
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Fungi
Dikarya
Basidiomycota
Agaricomycotina
Tremellomycetes
Tremellales (jelly fungi)
Cryptococcaceae
Cryptococcus
Cryptococcus neoformans species complex
Cryptococcus neoformans (Filobasidiella neoformans)
Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
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Enzyme Sequence |
MVLINDKKFACEKCIKGHRVSACTHTDRPLFEVKKKGRPSTQCRHCKEKRKSAGSSVHTKCQCGATDPKTLKDILASVNAAHAAANESGGASATANTSAEPEIETRKGQPGSKPTFPRGLKDVHEIAAAANALQGWGEDDQVVKAAERTVQALLNPCKCELGGPCTCCQIKTKPRRKHSGHEFENPASAGATPPGGGCCGSSVHSRDDVATRNSPTSINSSEAIHHPPQTAPMLHKTRLFSPYSTDLRRRDSSSSTGSKTPGWASPRAMRPPVSRIKPLTDMRRLMNAAVNQDGTLASEIPRSVVGLPTLPGIESFNTSANLENGEKSKDVDMPLAFPTSEDVVIGACMCGDDCSCPGCATHDHHNISPSNRTHDGSCGESCKGHNDCAHSIPIPSGVQSIAQLICIAASQVPPPPPNRTDSLNPHDTRILPPSVSLSEDVARTMGIVPLKPLECCGGKCGCPPGECACTKQCCGCCGECTCEKDEDTRMEEEGEYTESARDVTTSSCGGCKGKEKQSGFSDMMSPQIPQSVSPTSYHVPPLQPKPLNLPVSTIHHSTLSPSFNTPQPSPPAVSSPADSLSMAVHPSNGPNVRPVPMIQPRPILPKRASDTGLVMPQGSRPPSALGRSGSMTATKRSGTSTGVRRSNSDVRKVVGPSQPHHRPSIQSSSDRSFYIGSPSNQIAPGGVPMASAPSQMTAPLNSADSNSDLLAFIQQQWSADKTSNSNSDMNPSHPTMPVSLTAEPWAFPPQNETTDDSAPVPFDLDAFLMSIGVQPDGELRNDRPLSSQPPQSLMPNIPPTQPIAPLPPIPPSMSDVRPGYDMTFANFFLNSTPSGPSGPSAIPATNIPSRHTTPQASRPLTPPESSFTEPPRWKFPGDLGGEIPIWNGPEALEGFGVLGSPVSEKEEVTEESQNEKDIIDLSKPLDSAALTKIMKALEKQGGGQSSSQGAPSVANTDQQLQSLPALQTVPPVHPASVISPTRADPAHELDDMFSQFVTLDGTPIGSNNDGLGLNGGPGMMALPTNLSLGDELGFGGEMRWDQARMWSN |
Enzyme Length |
1048 |
Uniprot Accession Number |
J9VT33 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
DNA_BIND 1..40; /note=Copper-fist; /evidence=ECO:0000255|PROSITE-ProRule:PRU00055 |
EC Number |
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Enzyme Function |
FUNCTION: Transcription factor that regulates copper acquisition and homeostasis, and which plays a central role in fungal pathogenesis during neurologic infection (PubMed:21489137, PubMed:23511945, PubMed:29608794). The transcriptional regulation exerted by CUF1 is intrinsically complex since it acts as a dual sensor of copper levels, responsible for expression of a set of copper-specific copper transporters, CTR1 and CTR4, at low copper concentrations, and 2 metallothioneins, CMT1 and CMT2, at high copper concentrations (PubMed:17290306, PubMed:21489137, PubMed:21819456, PubMed:29608794). Positively regulates the expression of the copper acquisition factor BIM1 under copper-limiting conditions (PubMed:31932719). Also positively regulates the expression of super oxide dismutase SOD2 isoform 2 during oxidative stress and copper-limiting conditions (PubMed:33567338). Negatively regulates the expression of super oxide dismutase SOD1 during copper-limiting conditions (PubMed:33567338). Regulates also ATM1, an ABC transporter with functions in the iron-sulfur clusters (ISC) export machinery, during copper stress (PubMed:29089435). Another target of CUF1 is the gene encoding the laccase LAC1 (PubMed:19459959). Binds promoters of target genes at Cu-responsive elements (CuREs) that contain a variable A/T rich 5' region followed by the core consensus sequence 5'-G(G/C)CTC(A/G)-3' (PubMed:29608794, PubMed:31932719, PubMed:33567338). Negatively regulates capsule biosynthesis, probably via modulating iron acquisition through the high-affinity iron uptake pathway (PubMed:20112673). {ECO:0000269|PubMed:17290306, ECO:0000269|PubMed:19459959, ECO:0000269|PubMed:20112673, ECO:0000269|PubMed:21489137, ECO:0000269|PubMed:21819456, ECO:0000269|PubMed:23511945, ECO:0000269|PubMed:29089435, ECO:0000269|PubMed:29608794, ECO:0000269|PubMed:31932719, ECO:0000269|PubMed:33567338}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
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Features |
Chain (1); Compositional bias (7); DNA binding (1); Metal binding (4); Motif (2); Region (4) |
Keywords |
Copper;Cytoplasm;Metal-binding;Nucleus;Transcription;Transcription regulation;Zinc |
Interact With |
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Induction |
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Subcellular Location |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21489137, ECO:0000269|PubMed:33567338}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21489137}. Note=Upon copper depletion, localizes exclusively to the nucleus as an activator for CTR4 transcription, while it is located to the cell periphery in the presence of exogenous copper. {ECO:0000269|PubMed:21489137}. |
Modified Residue |
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Post Translational Modification |
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Signal Peptide |
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Structure 3D |
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Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
MOTIF 348..362; /note="CRM-I"; /evidence="ECO:0000305|PubMed:17290306, ECO:0000305|PubMed:21489137, ECO:0000305|PubMed:29608794"; MOTIF 455..482; /note="CRM-II"; /evidence="ECO:0000305|PubMed:21489137, ECO:0000305|PubMed:29608794" |
Gene Encoded By |
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Mass |
110,781 |
Kinetics |
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Metal Binding |
METAL 11; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00055; METAL 14; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00055; METAL 23; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00055; METAL 25; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00055 |
Rhea ID |
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Cross Reference Brenda |
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