O82089 · CCH_ARATH

Function

function

Involved in copper homeostasis. Can complement the yeast mutants atx1 and sod1.

Cofactor

Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 1 copper ion per subunit.

Features

Showing features for binding site.

1121102030405060708090100110120
TypeIDPosition(s)Description
Binding site13Cu cation (UniProtKB | ChEBI)
Binding site16Cu cation (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast
Cellular Componentcytosol
Molecular Functioncopper chaperone activity
Molecular Functionmetal ion binding
Molecular Functionprotein domain specific binding
Biological Processcopper ion transport
Biological Processintracellular copper ion homeostasis
Biological Processresponse to cadmium ion

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Copper transport protein CCH
  • Alternative names
    • Copper chaperone CCH

Gene names

    • Name
      CCH
    • ORF names
      F18O21.200
    • Ordered locus names
      At3g56240

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    O82089

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal growth conditions.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00004227612-121Copper transport protein CCH

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in phloem (at protein level).

Induction

Induced by copper deficiency, ozone and senescence. Down-regulated by excess of copper.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain2-65HMA
Region70-121Disordered
Compositional bias73-113Basic and acidic residues

Sequence similarities

Belongs to the ATX1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    121
  • Mass (Da)
    12,971
  • Last updated
    1998-11-01 v1
  • Checksum
    271D38907ED4012C
MAQTVVLKVGMSCQGCVGAVNRVLGKMEGVESFDIDIKEQKVTVKGNVEPEAVFQTVSKTGKKTSYWPVEAEAEPKAEADPKVETVTETKTEAETKTEAKVDAKADVEPKAAEAETKPSQV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1I9LNC0A0A1I9LNC0_ARATHCCH111

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias73-113Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U88711
EMBL· GenBank· DDBJ
AAC33510.1
EMBL· GenBank· DDBJ
mRNA
AL163763
EMBL· GenBank· DDBJ
CAB87423.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE79500.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
ANM64077.1
EMBL· GenBank· DDBJ
Genomic DNA
AF361860
EMBL· GenBank· DDBJ
AAK32872.1
EMBL· GenBank· DDBJ
mRNA
AY066056
EMBL· GenBank· DDBJ
AAL47423.1
EMBL· GenBank· DDBJ
mRNA
AY085657
EMBL· GenBank· DDBJ
AAM62878.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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