Detail Information for IndEnz0015000120
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)
Enzyme Sequence MVLINDKKFACEKCIKGHRVSACTHTDRPLFEVKKKGRPSTQCRHCKEKRKSAGSSVHTKCQCGATDPKTLKDILASVNAAHAAANESGGASATANTSAEPEIETRKGQPGSKPTFPRGLKDVHEIAAAANALQGWGEDDQVVKAAERTVQALLNPCKCELGGPCTCCQIKTKPRRKHSGHEFENPASAGATPPGGGCCGSSVHSRDDVATRNSPTSINSSEAIHHPPQTAPMLHKTRLFSPYSTDLRRRDSSSSTGSKTPGWASPRAMRPPVSRIKPLTDMRRLMNAAVNQDGTLASEIPRSVVGLPTLPGIESFNTSANLENGEKSKDVDMPLAFPTSEDVVIGACMCGDDCSCPGCATHDHHNISPSNRTHDGSCGESCKGHNDCAHSIPIPSGVQSIAQLICIAASQVPPPPPNRTDSLNPHDTRILPPSVSLSEDVARTMGIVPLKPLECCGGKCGCPPGECACTKQCCGCCGECTCEKDEDTRMEEEGEYTESARDVTTSSCGGCKGKEKQSGFSDMMSPQIPQSVSPTSYHVPPLQPKPLNLPVSTIHHSTLSPSFNTPQPSPPAVSSPADSLSMAVHPSNGPNVRPVPMIQPRPILPKRASDTGLVMPQGSRPPSALGRSGSMTATKRSGTSTGVRRSNSDVRKVVGPSQPHHRPSIQSSSDRSFYIGSPSNQIAPGGVPMASAPSQMTAPLNSADSNSDLLAFIQQQWSADKTSNSNSDMNPSHPTMPVSLTAEPWAFPPQNETTDDSAPVPFDLDAFLMSIGVQPDGELRNDRPLSSQPPQSLMPNIPPTQPIAPLPPIPPSMSDVRPGYDMTFANFFLNSTPSGPSGPSAIPATNIPSRHTTPQASRPLTPPESSFTEPPRWKFPGDLGGEIPIWNGPEALEGFGVLGSPVSEKEEVTEESQNEKDIIDLSKPLDSAALTKIMKALEKQGGGQSSSQGAPSVANTDQQLQSLPALQTVPPVHPASVISPTRADPAHELDDMFSQFVTLDGTPIGSNNDGLGLNGGPGMMALPTNLSLGDELGFGGEMRWDQARMWSN
Enzyme Length 1048
Uniprot Accession Number J9VT33
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 1..40; /note=Copper-fist; /evidence=ECO:0000255|PROSITE-ProRule:PRU00055
EC Number
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
PH Dependency
Pathway
nucleotide Binding
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
Induction
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
Post Translational Modification
Signal Peptide
Structure 3D
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
Mass 110,781
Kinetics
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
Cross Reference Brenda