ID   COX17_PIG               Reviewed;          62 AA.
AC   P81045;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cytochrome c oxidase copper chaperone;
DE   AltName: Full=Dopuin;
GN   Name=COX17;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Small intestine;
RX   PubMed=9370362; DOI=10.1111/j.1432-1033.1997.t01-2-00518.x;
RA   Chen Z.-W., Bergman T., Ostenson C.-G., Efendic S., Mutt V., Joernvall H.;
RT   "Characterization of dopuin, a polypeptide with special residue
RT   distributions.";
RL   Eur. J. Biochem. 249:518-522(1997).
RN   [2]
RP   FUNCTION.
RX   PubMed=17182746; DOI=10.1073/pnas.0606189103;
RA   Banci L., Bertini I., Ciofi-Baffoni S., Leontari I., Martinelli M.,
RA   Palumaa P., Sillard R., Wang S.;
RT   "Human Sco1 functional studies and pathological implications of the P174L
RT   mutant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15-20(2007).
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:0000269|PubMed:17182746}.
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   AlphaFoldDB; P81045; -.
DR   SMR; P81045; -.
DR   STRING; 9823.ENSSSCP00000012672; -.
DR   PaxDb; P81045; -.
DR   PeptideAtlas; P81045; -.
DR   eggNOG; KOG3496; Eukaryota.
DR   HOGENOM; CLU_149618_1_3_1; -.
DR   InParanoid; P81045; -.
DR   OMA; EACTKWI; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P81045; SS.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0016531; F:copper chaperone activity; IDA:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Chaperone; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome.
FT   CHAIN           1..62
FT                   /note="Cytochrome c oxidase copper chaperone"
FT                   /id="PRO_0000213540"
FT   DOMAIN          22..62
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           25..35
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           44..54
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   BINDING         22
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   BINDING         23
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14061"
FT   DISULFID        25..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        35..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   62 AA;  6695 MW;  8C01130B2EF5D83E CRC64;
     PGLAAAIPAP PESQEKKPLK PCCACPETKK ARDACIIEKG EEHCGHLIEA HKECMRALGF
     KI