ID   COX17_CANLF             Reviewed;          63 AA.
AC   Q6J3Q7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cytochrome c oxidase copper chaperone;
GN   Name=COX17;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Spee B., Arends B., Favier R., Penning L.C., Rothuizen J.;
RT   "Copper metabolism and oxidative stress during copper toxicosis in the
RT   dog.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Copper metallochaperone essential for the assembly of the
CC       mitochondrial respiratory chain complex IV (CIV), also known as
CC       cytochrome c oxidase. Binds two copper ions and delivers them to the
CC       metallochaperone SCO1 which transports the copper ions to the Cu(A)
CC       site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
CC       {ECO:0000250|UniProtKB:Q14061}.
CC   -!- SUBUNIT: Interacts with COA1. Interacts with the chaperone CHCHD4; this
CC       is important for correct folding and the formation of disulfide bonds
CC       that stabilize the structure. {ECO:0000250|UniProtKB:Q14061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:Q14061}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q14061}.
CC   -!- SIMILARITY: Belongs to the COX17 family. {ECO:0000305}.
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DR   EMBL; AY603041; AAT37154.1; -; mRNA.
DR   RefSeq; NP_001012754.1; NM_001012736.1.
DR   AlphaFoldDB; Q6J3Q7; -.
DR   SMR; Q6J3Q7; -.
DR   STRING; 9612.ENSCAFP00000016247; -.
DR   PaxDb; Q6J3Q7; -.
DR   Ensembl; ENSCAFT00030016020; ENSCAFP00030013976; ENSCAFG00030008686.
DR   Ensembl; ENSCAFT00040047064; ENSCAFP00040041081; ENSCAFG00040025249.
DR   Ensembl; ENSCAFT00845030650; ENSCAFP00845024049; ENSCAFG00845017310.
DR   GeneID; 503668; -.
DR   KEGG; cfa:503668; -.
DR   CTD; 10063; -.
DR   VEuPathDB; HostDB:ENSCAFG00845017310; -.
DR   eggNOG; KOG3496; Eukaryota.
DR   GeneTree; ENSGT00390000002329; -.
DR   HOGENOM; CLU_149618_1_3_1; -.
DR   InParanoid; Q6J3Q7; -.
DR   OMA; EACTKWI; -.
DR   OrthoDB; 1621529at2759; -.
DR   TreeFam; TF105074; -.
DR   Proteomes; UP000002254; Chromosome 33.
DR   Bgee; ENSCAFG00000011029; Expressed in heart right ventricle and 51 other tissues.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0016531; F:copper chaperone activity; ISS:UniProtKB.
DR   GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; IEA:Ensembl.
DR   InterPro; IPR009069; Cys_alpha_HP_mot_SF.
DR   InterPro; IPR007745; Cyt_c_oxidase_Cu-chaperone.
DR   PANTHER; PTHR16719; PTHR16719; 1.
DR   Pfam; PF05051; COX17; 1.
DR   SUPFAM; SSF47072; SSF47072; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Chaperone; Copper; Cytoplasm; Disulfide bond; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..63
FT                   /note="Cytochrome c oxidase copper chaperone"
FT                   /id="PRO_0000213537"
FT   DOMAIN          23..63
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           26..36
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           45..55
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   BINDING         23
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   BINDING         24
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   DISULFID        26..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        36..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   63 AA;  6776 MW;  26679E25BEF451F2 CRC64;
     MPGLAAASPA PSDSQEKKPL KPCCACPETK KARDACIIEK GEEHCGHLIE AHKECMRALG
     FKI