COX19_HUMAN
ID COX19_HUMAN Reviewed; 90 AA.
AC Q49B96; A4FTX0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome c oxidase assembly protein COX19;
DE Short=hCOX19;
GN Name=COX19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16212937; DOI=10.1016/j.bbrc.2005.09.127;
RA Sacconi S., Trevisson E., Pistollato F., Baldoin M.C., Rezzonico R.,
RA Bourget I., Desnuelle C., Tenconi R., Basso G., DiMauro S., Salviati L.;
RT "hCOX18 and hCOX19: two human genes involved in cytochrome c oxidase
RT assembly.";
RL Biochem. Biophys. Res. Commun. 337:832-839(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23345593; DOI=10.1091/mbc.e12-09-0705;
RA Leary S.C., Cobine P.A., Nishimura T., Verdijk R.M., de Krijger R.,
RA de Coo R., Tarnopolsky M.A., Winge D.R., Shoubridge E.A.;
RT "COX19 mediates the transduction of a mitochondrial redox signal from SCO1
RT that regulates ATP7A-mediated cellular copper efflux.";
RL Mol. Biol. Cell 24:683-691(2013).
RN [6]
RP SUBCELLULAR LOCATION, DISULFIDE BONDS, AND INTERACTION WITH CHCHD4.
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Required for the transduction of an SCO1-dependent redox
CC signal from the mitochondrion to ATP7A to regulate cellular copper
CC homeostasis (PubMed:23345593). May be required for the assembly of
CC mitochondrial cytochrome c oxidase (By similarity).
CC {ECO:0000250|UniProtKB:Q3E731, ECO:0000269|PubMed:23345593}.
CC -!- SUBUNIT: Interacts with CHCHD4/MIA40 forming transient intermolecular
CC disulfide bridges. {ECO:0000269|PubMed:23676665}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16212937,
CC ECO:0000269|PubMed:23345593, ECO:0000269|PubMed:23676665}.
CC Mitochondrion intermembrane space {ECO:0000269|PubMed:23345593,
CC ECO:0000269|PubMed:23676665}. Mitochondrion
CC {ECO:0000269|PubMed:23345593, ECO:0000269|PubMed:23676665}.
CC Note=Partitions between mitochondria and the cytosol in a copper-
CC dependent manner. Enriched in the cytosol when intracellular copper
CC concentrations are elevated. {ECO:0000269|PubMed:23345593}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC skeletal muscle. {ECO:0000269|PubMed:16212937}.
CC -!- SIMILARITY: Belongs to the COX19 family. {ECO:0000305}.
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DR EMBL; AY957566; AAY35062.1; -; mRNA.
DR EMBL; BC070383; AAH70383.1; -; mRNA.
DR EMBL; BC103632; AAI03633.1; -; mRNA.
DR EMBL; BC110420; AAI10421.1; -; mRNA.
DR CCDS; CCDS34582.1; -.
DR RefSeq; NP_001026788.1; NM_001031617.2.
DR AlphaFoldDB; Q49B96; -.
DR SMR; Q49B96; -.
DR BioGRID; 124748; 7.
DR IntAct; Q49B96; 5.
DR MINT; Q49B96; -.
DR STRING; 9606.ENSP00000342015; -.
DR iPTMnet; Q49B96; -.
DR MetOSite; Q49B96; -.
DR PhosphoSitePlus; Q49B96; -.
DR BioMuta; COX19; -.
DR DMDM; 121943561; -.
DR EPD; Q49B96; -.
DR jPOST; Q49B96; -.
DR MassIVE; Q49B96; -.
DR MaxQB; Q49B96; -.
DR PaxDb; Q49B96; -.
DR PeptideAtlas; Q49B96; -.
DR PRIDE; Q49B96; -.
DR ProteomicsDB; 62072; -.
DR Antibodypedia; 34791; 86 antibodies from 18 providers.
DR DNASU; 90639; -.
DR Ensembl; ENST00000344111.4; ENSP00000342015.3; ENSG00000240230.6.
DR GeneID; 90639; -.
DR KEGG; hsa:90639; -.
DR MANE-Select; ENST00000344111.4; ENSP00000342015.3; NM_001031617.3; NP_001026788.1.
DR UCSC; uc003sjp.2; human.
DR CTD; 90639; -.
DR DisGeNET; 90639; -.
DR GeneCards; COX19; -.
DR HGNC; HGNC:28074; COX19.
DR HPA; ENSG00000240230; Low tissue specificity.
DR MIM; 610429; gene.
DR neXtProt; NX_Q49B96; -.
DR OpenTargets; ENSG00000240230; -.
DR PharmGKB; PA145008561; -.
DR VEuPathDB; HostDB:ENSG00000240230; -.
DR eggNOG; KOG3477; Eukaryota.
DR GeneTree; ENSGT00390000016895; -.
DR HOGENOM; CLU_141947_5_0_1; -.
DR InParanoid; Q49B96; -.
DR OMA; LECRMDN; -.
DR OrthoDB; 1595090at2759; -.
DR PhylomeDB; Q49B96; -.
DR TreeFam; TF321525; -.
DR PathwayCommons; Q49B96; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; Q49B96; -.
DR BioGRID-ORCS; 90639; 250 hits in 1075 CRISPR screens.
DR ChiTaRS; COX19; human.
DR GenomeRNAi; 90639; -.
DR Pharos; Q49B96; Tbio.
DR PRO; PR:Q49B96; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q49B96; protein.
DR Bgee; ENSG00000240230; Expressed in tendon of biceps brachii and 175 other tissues.
DR ExpressionAtlas; Q49B96; baseline and differential.
DR Genevisible; Q49B96; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP: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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Disulfide bond; Mitochondrion; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..90
FT /note="Cytochrome c oxidase assembly protein COX19"
FT /id="PRO_0000273151"
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:0007744|PubMed:19413330"
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 90 AA; 10394 MW; 238A37E8A70EFA09 CRC64;
MSTAMNFGTK SFQPRPPDKG SFPLDHLGEC KSFKEKFMKC LHNNNFENAL CRKESKEYLE
CRMERKLMLQ EPLEKLGFGD LTSGKSEAKK
