Q94FT1 · CX172_ARATH

Function

function

Copper chaperone for cytochrome c oxidase (COX). Binds 2 copper ions and delivers them to the Cu(A) site of COX (By similarity).

Features

Showing features for binding site.

17210203040506070MSGLQAQDSACSLDKPSKDVVATETKPKKRICCACPDTKKLRDECIVEHGESACTKWIEAHILCLRSEGFKV
TypeIDPosition(s)Description
Binding site32Cu cation (UniProtKB | ChEBI)
Binding site33Cu 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 Componentcytosol
Cellular Componentmitochondrial intermembrane space
Molecular Functioncopper chaperone activity
Molecular Functioncopper ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome c oxidase copper chaperone 2

Gene names

    • Name
      COX17-2
    • ORF names
      F8L10
    • Ordered locus names
      At1g53030

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
    Q94FT1
  • Secondary accessions
    • Q2HIR2
    • Q8LFR7

Proteomes

Organism-specific databases

Genome annotation databases

PTM/Processing

Features

Showing features for chain, disulfide bond.

Type
IDPosition(s)Description
ChainPRO_00004227591-72Cytochrome c oxidase copper chaperone 2
Disulfide bond35↔64
Disulfide bond45↔54

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain32-72CHCH
Motif35-45Cx9C motif 1
Motif54-64Cx9C motif 2

Sequence similarities

Belongs to the COX17 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    72
  • Mass (Da)
    7,938
  • Last updated
    2001-12-01 v1
  • Checksum
    6DC281CFFE6A6272
MSGLQAQDSACSLDKPSKDVVATETKPKKRICCACPDTKKLRDECIVEHGESACTKWIEAHILCLRSEGFKV

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict24in Ref. 5; AAM61247
Sequence conflict69in Ref. 4; ABD38858 and 5; AAM61247

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF349685
EMBL· GenBank· DDBJ
AAK73497.1
EMBL· GenBank· DDBJ
mRNA
AC022520
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CP002684
EMBL· GenBank· DDBJ
AEE32879.1
EMBL· GenBank· DDBJ
Genomic DNA
BT024519
EMBL· GenBank· DDBJ
ABD38858.1
EMBL· GenBank· DDBJ
mRNA
AY084685
EMBL· GenBank· DDBJ
AAM61247.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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