J9VE33 · CRZ1_CRYNH
- ProteinTranscriptional regulator CRZ1
- GeneCRZ1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1094 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA-binding transcriptional activator that interacts with calcineurin-dependent response element (CDRE) promoters (PubMed:28376087).
Activates expression of genes required to maintain cell wall integrity during stress (PubMed:23251520, PubMed:28376087).
Activates expression of genes required for transepithelial migration through the host blood-brain barrier (PubMed:29113016).
Required for adaptation to host temperature during infection (PubMed:28376087).
Activates expression of genes required to maintain cell wall integrity during stress (PubMed:23251520, PubMed:28376087).
Activates expression of genes required for transepithelial migration through the host blood-brain barrier (PubMed:29113016).
Required for adaptation to host temperature during infection (PubMed:28376087).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | DNA-binding transcription activator activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | calcineurin-mediated signaling | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transepithelial migration of symbiont in host | |
Biological Process | regulation of fungal-type cell wall organization |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTranscriptional regulator CRZ1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex
Accessions
- Primary accessionJ9VE33
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the nucleus during calcium signaling, cell wall and heat stress (PubMed:21487010, PubMed:23251520, PubMed:24520056, PubMed:27611567, PubMed:28376087, PubMed:28898238, PubMed:31266771).
Localizes to the nucleus following dephosphorylation by CNA1 (calcineurin) (PubMed:27611567).
Localizes to the nucleus during growth on glucosamine carbon source (PubMed:28898238).
Localizes to the cytosol during vegetative growth and osmotic stress (PubMed:23251520, PubMed:28376087, PubMed:28898238).
Localizes to the nucleus following dephosphorylation by CNA1 (calcineurin) (PubMed:27611567).
Localizes to the nucleus during growth on glucosamine carbon source (PubMed:28898238).
Localizes to the cytosol during vegetative growth and osmotic stress (PubMed:23251520, PubMed:28376087, PubMed:28898238).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Decreases virulence in a mouse intranasal inhalation model and intravenous model for infection (PubMed:21487010, PubMed:27611567, PubMed:28376087, PubMed:29233914).
Decreases virulence in a moth model (PubMed:28376087).
Decreases urease activity (PubMed:29113016).
Decreases levels of: laccase and melanin (PubMed:21487010).
Hypercapsular with mucoid colony morphology (PubMed:21487010).
Sensitive to: calcium; lithium; sodium nitrite; high temperature; sodium dodecyl sulfate (cell wall stress inducer); Calcofluor White (cell wall stress inducer); Congo Red (cell wall stress inducer); caspofungin (cell wall stress inducer) (PubMed:21487010, PubMed:27611567, PubMed:28376087, PubMed:29233914, PubMed:31266771).
Abolishes filamentation during growth on glucosamine carbon source (PubMed:28898238).
Decreases RNA level of genes involved in membrane transport, carbohydrate metabolism, signaling, DNA replication, and sterol biosynthesis during heat stress (PubMed:28376087).
Decreases CHS5 and CHS6 RNA level during heat stress (PubMed:27611567, PubMed:28376087).
Decreases RNA level of ZNF2 during growth on glucosamine carbon source (PubMed:28898238).
Increases MFalpha1 expression during mating (PubMed:27611567).
Normal hyphal morphology during mating (PubMed:23251520, PubMed:28376087).
Simultaneous disruption of HAD1, PUF4 or LHP1 results in phenotypic enhancement (PubMed:27611567, PubMed:29233914).
Decreases virulence in a moth model (PubMed:28376087).
Decreases urease activity (PubMed:29113016).
Decreases levels of: laccase and melanin (PubMed:21487010).
Hypercapsular with mucoid colony morphology (PubMed:21487010).
Sensitive to: calcium; lithium; sodium nitrite; high temperature; sodium dodecyl sulfate (cell wall stress inducer); Calcofluor White (cell wall stress inducer); Congo Red (cell wall stress inducer); caspofungin (cell wall stress inducer) (PubMed:21487010, PubMed:27611567, PubMed:28376087, PubMed:29233914, PubMed:31266771).
Abolishes filamentation during growth on glucosamine carbon source (PubMed:28898238).
Decreases RNA level of genes involved in membrane transport, carbohydrate metabolism, signaling, DNA replication, and sterol biosynthesis during heat stress (PubMed:28376087).
Decreases CHS5 and CHS6 RNA level during heat stress (PubMed:27611567, PubMed:28376087).
Decreases RNA level of ZNF2 during growth on glucosamine carbon source (PubMed:28898238).
Increases MFalpha1 expression during mating (PubMed:27611567).
Normal hyphal morphology during mating (PubMed:23251520, PubMed:28376087).
Simultaneous disruption of HAD1, PUF4 or LHP1 results in phenotypic enhancement (PubMed:27611567, PubMed:29233914).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 288 | Increases CRZ1 localization to the nucleus. | ||||
Sequence: S → A | ||||||
Mutagenesis | 451-456 | Abolishes nuclear localization during heat stress and confers sensitivity to high temperature, Congo Red and sodium dodecyl sulfate. | ||||
Sequence: Missing | ||||||
Mutagenesis | 508 | Increases CRZ1 localization to the nucleus. | ||||
Sequence: S → A |
Miscellaneous
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451159 | 1-1094 | Transcriptional regulator CRZ1 | |||
Sequence: MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPFFNKPQSPPALIIPNSPVLPNIVTQSTSNNHSKGLNQPHTRHASNGAGGLFPPSNPALEHLTGMAGISPIAPNADGPMICIQPSTPISGLKEGRGLFDAALRRAGAARGAQRQGPQGQGESQEDRRQDGFNVPSPQSHPLPRTLSSDQVNQGVEMQGMDFAAQMQSYEQQGWANDTLRIAGPSRPRAKSDSIIPSPTADSFDRQAFLAFIGAGNAQPPPPNVEMQPGYVDVSEQWRNTVSAWKAGLGEGELNSQPTLDPRLLPGRESNEAVYQQLLMQQQTGQMPRLDPDQLHQLTQLEGQRARFSLNTNIAPPKYEPGEISPTSMVFYQSMGLYPHAAPELSGTVSAPWSQTAFGQVPGPGPVGHPATAGPAQQHFLTPTLSHATVRRRSFGGGEHPAMGAGTPGYGMEFSSPFAGKSVGQIRGVNMGHRRAARSEDFGRGGTGWGVGAGGSTAEFLQSITGDDGSLLPPSNRGHAMSHSRHSSTSSIRSASPALSISSQGSSFSHHSPRMDMPDSIYPGHPIIAPATPLQVSGLYEEQQTPARVAKMKVTSVATEVASTSRRTNSGIFKCPVPGCGSTFTRHFNLKGHLRSHNDERPFKCLYEGCPKAIVGFARQHDCKRHMLLHEGLRLFECEGCGKKFARLDALTRHHKSEQGQECAITHPLPTNFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSGKRRSKKSETSEED | ||||||
Modified residue | 103 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 288 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 329 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 508 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 569 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 765 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 810 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated (PubMed:21487010, PubMed:27611567).
Dephosphorylated by calcineurin (CNA1) which promotes nuclear localization (PubMed:27611567).
Dephosphorylated by calcineurin (CNA1) which promotes nuclear localization (PubMed:27611567).
Keywords
- PTM
PTM databases
Expression
Induction
Induced during glucose starvation.
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MADPASPPSFDAIFAQQPVRRSSSTSTSS | ||||||
Compositional bias | 44-58 | Polar residues | ||||
Sequence: FNSDAPLVDEPQSLS | ||||||
Region | 44-81 | Disordered | ||||
Sequence: FNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMM | ||||||
Compositional bias | 59-74 | Basic and acidic residues | ||||
Sequence: EQARKQQRDPSKDGNN | ||||||
Region | 93-428 | Disordered | ||||
Sequence: GRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPFFNKPQSPPALIIPNSPVLPNIVTQSTSNNHSKGLNQPHTRHASNGAGGLFPPS | ||||||
Compositional bias | 145-189 | Polar residues | ||||
Sequence: QTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPG | ||||||
Compositional bias | 198-266 | Polar residues | ||||
Sequence: LPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNG | ||||||
Compositional bias | 282-375 | Polar residues | ||||
Sequence: ELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPF | ||||||
Compositional bias | 392-417 | Polar residues | ||||
Sequence: VLPNIVTQSTSNNHSKGLNQPHTRHA | ||||||
Region | 477-519 | Disordered | ||||
Sequence: RAGAARGAQRQGPQGQGESQEDRRQDGFNVPSPQSHPLPRTLS | ||||||
Compositional bias | 502-519 | Polar residues | ||||
Sequence: DGFNVPSPQSHPLPRTLS | ||||||
Region | 835-888 | Disordered | ||||
Sequence: ITGDDGSLLPPSNRGHAMSHSRHSSTSSIRSASPALSISSQGSSFSHHSPRMDM | ||||||
Compositional bias | 851-884 | Polar residues | ||||
Sequence: AMSHSRHSSTSSIRSASPALSISSQGSSFSHHSP | ||||||
Zinc finger | 944-968 | C2H2-type 1 | ||||
Sequence: FKCPVPGCGSTFTRHFNLKGHLRSH | ||||||
Zinc finger | 1007-1029 | C2H2-type 2; degenerate | ||||
Sequence: FECEGCGKKFARLDALTRHHKSE | ||||||
Region | 1037-1094 | Disordered | ||||
Sequence: THPLPTNFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSGKRRSKKSETSEED | ||||||
Compositional bias | 1043-1081 | Polar residues | ||||
Sequence: NFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,094
- Mass (Da)117,964
- Last updated2012-11-28 v1
- ChecksumA8104E5A22F9D8F4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 44-58 | Polar residues | ||||
Sequence: FNSDAPLVDEPQSLS | ||||||
Compositional bias | 59-74 | Basic and acidic residues | ||||
Sequence: EQARKQQRDPSKDGNN | ||||||
Compositional bias | 145-189 | Polar residues | ||||
Sequence: QTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPG | ||||||
Compositional bias | 198-266 | Polar residues | ||||
Sequence: LPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNG | ||||||
Compositional bias | 282-375 | Polar residues | ||||
Sequence: ELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPF | ||||||
Compositional bias | 392-417 | Polar residues | ||||
Sequence: VLPNIVTQSTSNNHSKGLNQPHTRHA | ||||||
Compositional bias | 502-519 | Polar residues | ||||
Sequence: DGFNVPSPQSHPLPRTLS | ||||||
Compositional bias | 851-884 | Polar residues | ||||
Sequence: AMSHSRHSSTSSIRSASPALSISSQGSSFSHHSP | ||||||
Compositional bias | 1043-1081 | Polar residues | ||||
Sequence: NFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSG |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003820 EMBL· GenBank· DDBJ | AFR92293.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP003820 EMBL· GenBank· DDBJ | AGV15273.1 EMBL· GenBank· DDBJ | Genomic DNA |