COX17_MOUSE
ID COX17_MOUSE Reviewed; 63 AA.
AC P56394;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cytochrome c oxidase copper chaperone;
GN Name=Cox17; Synonyms=Cox17a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T.,
RA Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M.,
RA Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., Theising B.,
RA Wylie T., Lennon G., Soares B., Wilson R., Waterston R.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, COPPER-BINDING, AND MUTAGENESIS OF CYS-23; CYS-24 AND CYS-26.
RX PubMed=12370308; DOI=10.1128/mcb.22.21.7614-7621.2002;
RA Takahashi Y., Kako K., Kashiwabara S., Takehara A., Inada Y., Arai H.,
RA Nakada K., Kodama H., Hayashi J., Baba T., Munekata E.;
RT "Mammalian copper chaperone Cox17p has an essential role in activation of
RT cytochrome C oxidase and embryonic development.";
RL Mol. Cell. Biol. 22:7614-7621(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:12370308}.
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; AA168035; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC048668; AAH48668.1; -; mRNA.
DR CCDS; CCDS28165.1; -.
DR RefSeq; NP_001017429.1; NM_001017429.2.
DR RefSeq; XP_006521813.1; XM_006521750.3.
DR AlphaFoldDB; P56394; -.
DR SMR; P56394; -.
DR BioGRID; 198839; 6.
DR STRING; 10090.ENSMUSP00000054086; -.
DR iPTMnet; P56394; -.
DR PhosphoSitePlus; P56394; -.
DR EPD; P56394; -.
DR PaxDb; P56394; -.
DR PeptideAtlas; P56394; -.
DR PRIDE; P56394; -.
DR ProteomicsDB; 283356; -.
DR DNASU; 12856; -.
DR Ensembl; ENSMUST00000050273; ENSMUSP00000054086; ENSMUSG00000046516.
DR Ensembl; ENSMUST00000119704; ENSMUSP00000112386; ENSMUSG00000095464.
DR Ensembl; ENSMUST00000120495; ENSMUSP00000113430; ENSMUSG00000046516.
DR GeneID; 12856; -.
DR KEGG; mmu:12856; -.
DR UCSC; uc007zet.1; mouse.
DR CTD; 10063; -.
DR MGI; MGI:1333806; Cox17.
DR VEuPathDB; HostDB:ENSMUSG00000046516; -.
DR VEuPathDB; HostDB:ENSMUSG00000095464; -.
DR eggNOG; KOG3496; Eukaryota.
DR GeneTree; ENSGT00390000002329; -.
DR HOGENOM; CLU_149618_1_3_1; -.
DR InParanoid; P56394; -.
DR OMA; EACTKWI; -.
DR OrthoDB; 1621529at2759; -.
DR PhylomeDB; P56394; -.
DR TreeFam; TF105074; -.
DR BioGRID-ORCS; 12856; 9 hits in 39 CRISPR screens.
DR ChiTaRS; Cox17; mouse.
DR PRO; PR:P56394; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P56394; protein.
DR Bgee; ENSMUSG00000046516; Expressed in yolk sac and 250 other tissues.
DR ExpressionAtlas; P56394; baseline and differential.
DR Genevisible; P56394; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016531; F:copper chaperone activity; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:MGI.
DR GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
DR GO; GO:0008047; F:enzyme activator activity; IMP:MGI.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; ISO:MGI.
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; Disulfide bond; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..63
FT /note="Cytochrome c oxidase copper chaperone"
FT /id="PRO_0000213539"
FT DOMAIN 23..63
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..20
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:0000269|PubMed:12370308"
FT BINDING 24
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:12370308"
FT DISULFID 26..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 36..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MUTAGEN 23
FT /note="C->G: Significant reduction of copper binding; when
FT associated with G-24 and G-26."
FT /evidence="ECO:0000269|PubMed:12370308"
FT MUTAGEN 24
FT /note="C->G: Significant reduction of copper binding; when
FT associated with G-23 and G-26."
FT /evidence="ECO:0000269|PubMed:12370308"
FT MUTAGEN 26
FT /note="C->G: Significant reduction of copper binding; when
FT associated with G-23 and G-24."
FT /evidence="ECO:0000269|PubMed:12370308"
SQ SEQUENCE 63 AA; 6784 MW; 26787FE131159562 CRC64;
MPGLAAASPA PPEAQEKKPL KPCCACPETK KARDACIIEK GEEHCGHLIE AHKECMRALG
FKI
