ID   COX19_BOVIN             Reviewed;          89 AA.
AC   A8E4L1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Cytochrome c oxidase assembly protein COX19;
GN   Name=COX19;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {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; BC134520; AAI34521.1; -; mRNA.
DR   RefSeq; NP_001103436.1; NM_001109966.1.
DR   RefSeq; XP_015315893.1; XM_015460407.1.
DR   AlphaFoldDB; A8E4L1; -.
DR   SMR; A8E4L1; -.
DR   STRING; 9913.ENSBTAP00000020289; -.
DR   PaxDb; A8E4L1; -.
DR   Ensembl; ENSBTAT00000020289; ENSBTAP00000020289; ENSBTAG00000015253.
DR   GeneID; 100126182; -.
DR   KEGG; bta:100126182; -.
DR   CTD; 90639; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015253; -.
DR   VGNC; VGNC:27632; COX19.
DR   eggNOG; KOG3477; Eukaryota.
DR   GeneTree; ENSGT00390000016895; -.
DR   HOGENOM; CLU_141947_5_0_1; -.
DR   InParanoid; A8E4L1; -.
DR   OMA; LECRMDN; -.
DR   OrthoDB; 1595090at2759; -.
DR   TreeFam; TF321525; -.
DR   Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-BTA-611105; Respiratory electron transport.
DR   Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000015253; Expressed in bone marrow and 106 other tissues.
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:cellular 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   Pfam; PF06747; CHCH; 1.
DR   SUPFAM; SSF47072; SSF47072; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Disulfide bond; Mitochondrion; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q49B96"
FT   CHAIN           2..89
FT                   /note="Cytochrome c oxidase assembly protein COX19"
FT                   /id="PRO_0000328615"
FT   DOMAIN          27..69
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          1..23
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   DISULFID        40..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   89 AA;  10319 MW;  9B98ABC204C0042F CRC64;
     MSTAMNFGSK SFQPRPPDKG SFPLDHFGEC KSFKEKFMKC LRDNNFENAL CRNESKEYLE
     CRMERQLMAQ EPLEKLGFGD LIDGKSDKN