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Protein

Cytochrome c oxidase copper chaperone

Gene

COX17

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231CopperBy similarity
Metal bindingi24 – 241CopperBy similarity

GO - Molecular functioni

  • copper chaperone activity Source: SGD

GO - Biological processi

  • intracellular copper ion transport Source: SGD
  • mitochondrial respiratory chain complex IV assembly Source: SGD
  • protein farnesylation Source: MGI
  • protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32114-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase copper chaperone
Gene namesi
Name:COX17
Ordered Locus Names:YLL009C
ORF Names:L1343
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL009C.
SGDiS000003932. COX17.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrial intermembrane space Source: SGD
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 6968Cytochrome c oxidase copper chaperonePRO_0000213541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 57By similarity
Disulfide bondi36 ↔ 47By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ12287.

Interactioni

Protein-protein interaction databases

BioGridi31242. 19 interactions.
DIPiDIP-2915N.
IntActiQ12287. 7 interactions.
MINTiMINT-517429.

Structurei

Secondary structure

1
69
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi13 – 153Combined sources
Beta strandi23 – 253Combined sources
Helixi28 – 3912Combined sources
Helixi45 – 473Combined sources
Helixi48 – 5912Combined sources
Turni60 – 623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U96NMR-A1-69[»]
1U97NMR-A1-69[»]
1Z2GNMR-A1-69[»]
DisProtiDP00277.
ProteinModelPortaliQ12287.
SMRiQ12287. Positions 1-69.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12287.

Family & Domainsi

Sequence similaritiesi

Belongs to the COX17 family.Curated

Phylogenomic databases

HOGENOMiHOG000195037.
InParanoidiQ12287.
KOiK02260.
OMAiCCVCKPE.
OrthoDBiEOG7CVQBC.

Family and domain databases

Gene3Di1.10.810.10. 1 hit.
InterProiIPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view]
PANTHERiPTHR16719. PTHR16719. 1 hit.
PfamiPF05051. COX17. 1 hit.
[Graphical view]
ProDomiPD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47072. SSF47072. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12287-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTETDKKQEQ ENHAECEDKP KPCCVCKPEK EERDTCILFN GQDSEKCKEF
60
IEKYKECMKG YGFEVPSAN
Length:69
Mass (Da):8,056
Last modified:January 23, 2007 - v3
Checksum:i7DA9A5F97C8A3F78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L75948 Genomic DNA. Translation: AAA85477.1.
Z73114 Genomic DNA. Translation: CAA97453.1.
BK006945 Genomic DNA. Translation: DAA09309.1.
PIRiS62056.
RefSeqiNP_013092.1. NM_001181829.1.

Genome annotation databases

EnsemblFungiiYLL009C; YLL009C; YLL009C.
GeneIDi850651.
KEGGisce:YLL009C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L75948 Genomic DNA. Translation: AAA85477.1.
Z73114 Genomic DNA. Translation: CAA97453.1.
BK006945 Genomic DNA. Translation: DAA09309.1.
PIRiS62056.
RefSeqiNP_013092.1. NM_001181829.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U96NMR-A1-69[»]
1U97NMR-A1-69[»]
1Z2GNMR-A1-69[»]
DisProtiDP00277.
ProteinModelPortaliQ12287.
SMRiQ12287. Positions 1-69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31242. 19 interactions.
DIPiDIP-2915N.
IntActiQ12287. 7 interactions.
MINTiMINT-517429.

Proteomic databases

MaxQBiQ12287.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL009C; YLL009C; YLL009C.
GeneIDi850651.
KEGGisce:YLL009C.

Organism-specific databases

EuPathDBiFungiDB:YLL009C.
SGDiS000003932. COX17.

Phylogenomic databases

HOGENOMiHOG000195037.
InParanoidiQ12287.
KOiK02260.
OMAiCCVCKPE.
OrthoDBiEOG7CVQBC.

Enzyme and pathway databases

BioCyciYEAST:G3O-32114-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiQ12287.
PROiQ12287.

Family and domain databases

Gene3Di1.10.810.10. 1 hit.
InterProiIPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view]
PANTHERiPTHR16719. PTHR16719. 1 hit.
PfamiPF05051. COX17. 1 hit.
[Graphical view]
ProDomiPD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47072. SSF47072. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase."
    Glerum D.M., Shtanko A., Tzagoloff A.
    J. Biol. Chem. 271:14504-14509(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24657 / D273-10B.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle."
    Beers J., Glerum D.M., Tzagoloff A.
    J. Biol. Chem. 272:33191-33196(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-6, CHARACTERIZATION, SUBCELLULAR LOCATION.
  5. "Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae."
    Srinivasan C., Posewitz M.C., George G.N., Winge D.R.
    Biochemistry 37:7572-7577(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCOX17_YEAST
AccessioniPrimary (citable) accession number: Q12287
Secondary accession number(s): D6VXZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.