J9VX37 · CTR1_CRYNH

Function

function

High affinity copper transporter involved in Cu+ import into the cell upon copper-limitating conditions (PubMed:21819456, PubMed:23498952, PubMed:31932719).
Functions with BIM1 and probably also FRE4 and FRE7, where FRE4 and FRE7 metalloreductases liberate the Cu2+ bound to the BIM1 copper-binding site for subsequent import of Cu+ into the cell by CTR1, via the reduction of BIM1-bound Cu2+ to Cu+ to reduce binding affinity for BIM1 but increase affinity for CTR1 (Probable). The BIM1-CTR1 pathway for copper uptake plays a key role in colonization in the brain where copper amounts are low and thus in cryptococcal meningitis (PubMed:25417972, PubMed:31932719).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular Functioncopper ion transmembrane transporter activity

Names & Taxonomy

Protein names

  • Recommended name
    CUF1-dependent copper transporter 1
  • Short names
    Copper transporter 1

Gene names

    • Name
      CTR1
    • ORF names
      CNAG_07701

Organism names

Accessions

  • Primary accession
    J9VX37

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane42-62Helical
Transmembrane251-271Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Leads to a severe growth defect in copper deficiency conditions, but does not significantly affect melanin production, nor fungal virulence (PubMed:21819456, PubMed:25417972).
However, when both CTR1 and CTR4 are disrupted, the colonization in the brain and subsequent virulence are significantly reduced (PubMed:25417972).

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004495171-288CUF1-dependent copper transporter 1
Glycosylation18N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Induction

Expression is induced by copper deficiency and regulated by the CUF1 copper-dependent transcription factor (PubMed:21819456, PubMed:29608794).
The CTR1 promoter harbors the Cu-responsive element (CuRE), which is critical for CUF1 binding and activation under copper-limiting conditions (PubMed:29608794).

Interaction

Subunit

Interacts with the copper acquisition factor BIM1.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region106-125Disordered
Compositional bias154-177Polar residues
Region154-180Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    288
  • Mass (Da)
    31,538
  • Last updated
    2013-11-13 v2
  • Checksum
    F6645FB118262C1D
MDMSGMDGMDHMSSTSSNMSMSMKMYFHGTIGGDLLWFASWMPSSAGATVGVCIGLFILAIFERYLVAFRRACDAAWRRGQVGYVRPCSNGPLVFSSGKSTSLPPPVLFNRRSSTKKEKDVYNPLTPSDYALESNQDGSVEPVTPYTPSIHALRESQEGSSAPSYAHSQQGQAQAQGSGVGCDPCAEGRVAEIERCKEKAVERGLVHSHLPKAVRRSLDPGREGRWSRPFRLAVDVPRGLLQALQTLIHYLLMLVVMTFNIWWMISVVIGCGVGEMLFGRFGSSHVGH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias154-177Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003826
EMBL· GenBank· DDBJ
AFR96280.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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