ID COX19_MOUSE Reviewed; 92 AA.
AC Q8K0C8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Cytochrome c oxidase assembly protein COX19;
GN Name=Cox19;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [2]
RP DISULFIDE BONDS.
RX PubMed=23676665; DOI=10.1091/mbc.e12-12-0862;
RA Fischer M., Horn S., Belkacemi A., Kojer K., Petrungaro C., Habich M.,
RA Ali M., Kuettner V., Bien M., Kauff F., Dengjel J., Herrmann J.M.,
RA Riemer J.;
RT "Protein import and oxidative folding in the mitochondrial intermembrane
RT space of intact mammalian cells.";
RL Mol. Biol. Cell 24:2160-2170(2013).
CC -!- FUNCTION: Required for the transduction of an SCO1-dependent redox
CC signal from the mitochondrion to ATP7A to regulate cellular copper
CC homeostasis. May be required for the assembly of mitochondrial
CC cytochrome c oxidase. {ECO:0000250|UniProtKB:Q3E731,
CC ECO:0000250|UniProtKB:Q49B96}.
CC -!- SUBUNIT: Interacts with CHCHD4/MIA40 forming transient intermolecular
CC disulfide bridges. {ECO:0000250|UniProtKB:Q49B96}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q49B96}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q49B96}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q49B96}. Note=Partitions between mitochondria
CC and the cytosol in a copper-dependent manner. Enriched in the cytosol
CC when intracellular copper concentrations are elevated.
CC {ECO:0000250|UniProtKB:Q49B96}.
CC -!- SIMILARITY: Belongs to the COX19 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC031792; AAH31792.1; -; mRNA.
DR CCDS; CCDS39350.1; -.
DR RefSeq; NP_932097.1; NM_197980.1.
DR AlphaFoldDB; Q8K0C8; -.
DR SMR; Q8K0C8; -.
DR BioGRID; 212613; 1.
DR STRING; 10090.ENSMUSP00000062046; -.
DR iPTMnet; Q8K0C8; -.
DR PhosphoSitePlus; Q8K0C8; -.
DR MaxQB; Q8K0C8; -.
DR PaxDb; 10090-ENSMUSP00000062046; -.
DR PeptideAtlas; Q8K0C8; -.
DR ProteomicsDB; 285267; -.
DR Pumba; Q8K0C8; -.
DR Antibodypedia; 34791; 95 antibodies from 18 providers.
DR DNASU; 68033; -.
DR Ensembl; ENSMUST00000049630.13; ENSMUSP00000062046.7; ENSMUSG00000045438.13.
DR GeneID; 68033; -.
DR KEGG; mmu:68033; -.
DR UCSC; uc009agj.1; mouse.
DR AGR; MGI:1915283; -.
DR CTD; 90639; -.
DR MGI; MGI:1915283; Cox19.
DR VEuPathDB; HostDB:ENSMUSG00000045438; -.
DR eggNOG; KOG3477; Eukaryota.
DR GeneTree; ENSGT00390000016895; -.
DR HOGENOM; CLU_141947_5_0_1; -.
DR InParanoid; Q8K0C8; -.
DR OMA; EYLGCRM; -.
DR OrthoDB; 226248at2759; -.
DR PhylomeDB; Q8K0C8; -.
DR TreeFam; TF321525; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 68033; 20 hits in 76 CRISPR screens.
DR ChiTaRS; Cox19; mouse.
DR PRO; PR:Q8K0C8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K0C8; Protein.
DR Bgee; ENSMUSG00000045438; Expressed in interventricular septum and 261 other cell types or tissues.
DR ExpressionAtlas; Q8K0C8; baseline and differential.
DR Genevisible; Q8K0C8; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR009069; Cys_alpha_HP_mot_SF.
DR PANTHER; PTHR21107; CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX19; 1.
DR PANTHER; PTHR21107:SF2; CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX19; 1.
DR Pfam; PF06747; CHCH; 1.
DR SUPFAM; SSF47072; Cysteine alpha-hairpin motif; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Disulfide bond; Mitochondrion; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q49B96"
FT CHAIN 2..92
FT /note="Cytochrome c oxidase assembly protein COX19"
FT /id="PRO_0000273152"
FT DOMAIN 27..69
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 30..40
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 51..61
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q49B96"
FT DISULFID 30..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT DISULFID 40..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
SQ SEQUENCE 92 AA; 10821 MW; B3F616804658F594 CRC64;
MSTAMNFGTK SFQPRPPDKG SFPLDHFGEC KSFKEKFMRC LRDKNYENAL CRNESKEYLM
CRMQRQLMAP EPLEKLGFRD LMEGKPEAKD EC
//
