COX18_MOUSE
ID COX18_MOUSE Reviewed; 331 AA.
AC Q8VC74; A6H626; G3X965; Q3U1D5;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 5.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome c oxidase assembly protein COX18, mitochondrial;
DE Flags: Precursor;
GN Name=Cox18; Synonyms=Oxa1l2;
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=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Liver, and Mammary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Mitochondrial membrane insertase required for the
CC translocation of the C-terminus of cytochrome c oxidase subunit II (MT-
CC CO2/COX2) across the mitochondrial inner membrane. Plays a role in MT-
CC CO2/COX2 maturation following the COX20-mediated stabilization of newly
CC synthesized MT-CO2/COX2 protein and before the action of the
CC metallochaperones SCO1/2. Essential for the assembly and stability of
CC the mitochondrial respiratory chain complex IV (also known as
CC cytochrome c oxidase). {ECO:0000250|UniProtKB:Q8N8Q8}.
CC -!- SUBUNIT: Found in a complex with TMEM177, COA6, MT-CO2/COX2, COX20,
CC SCO1 and SCO2. Interacts transiently with MT-CO2/COX2 during its
CC maturation. Interacts with COX20 in a MT-CO2/COX2-dependent manner.
CC {ECO:0000250|UniProtKB:Q8N8Q8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8N8Q8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21612.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK156053; BAE33563.1; -; mRNA.
DR EMBL; AC162171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466617; EDL05329.1; -; Genomic_DNA.
DR EMBL; BC021612; AAH21612.1; ALT_SEQ; mRNA.
DR EMBL; BC138972; AAI38973.1; -; mRNA.
DR EMBL; BC145728; AAI45729.1; -; mRNA.
DR CCDS; CCDS19411.1; -.
DR RefSeq; NP_001028482.2; NM_001033310.3.
DR AlphaFoldDB; Q8VC74; -.
DR STRING; 10090.ENSMUSP00000113353; -.
DR iPTMnet; Q8VC74; -.
DR PhosphoSitePlus; Q8VC74; -.
DR SwissPalm; Q8VC74; -.
DR MaxQB; Q8VC74; -.
DR PaxDb; Q8VC74; -.
DR PRIDE; Q8VC74; -.
DR ProteomicsDB; 285255; -.
DR Antibodypedia; 44370; 87 antibodies from 20 providers.
DR DNASU; 231430; -.
DR Ensembl; ENSMUST00000048363; ENSMUSP00000044144; ENSMUSG00000035505.
DR GeneID; 231430; -.
DR KEGG; mmu:231430; -.
DR UCSC; uc008yar.2; mouse.
DR CTD; 285521; -.
DR MGI; MGI:2448532; Cox18.
DR VEuPathDB; HostDB:ENSMUSG00000035505; -.
DR eggNOG; KOG1239; Eukaryota.
DR GeneTree; ENSGT00530000063506; -.
DR HOGENOM; CLU_029282_2_0_1; -.
DR InParanoid; Q8VC74; -.
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; 231430; 13 hits in 72 CRISPR screens.
DR PRO; PR:Q8VC74; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VC74; protein.
DR Bgee; ENSMUSG00000035505; Expressed in metanephric loop of Henle and 243 other tissues.
DR ExpressionAtlas; Q8VC74; baseline and differential.
DR Genevisible; Q8VC74; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032977; F:membrane insertase activity; ISS:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR GO; GO:0051205; P:protein insertion into membrane; IBA:GO_Central.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; ISS:UniProtKB.
DR GO; GO:0051204; P:protein insertion into mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR PANTHER; PTHR12428; PTHR12428; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..63
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 64..331
FT /note="Cytochrome c oxidase assembly protein COX18,
FT mitochondrial"
FT /id="PRO_0000043327"
FT TOPO_DOM 64..164
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..220
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..259
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..331
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="G -> R (in Ref. 1; BAE33563 and 4; AAI38973/
FT AAI45729)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="I -> V (in Ref. 1; BAE33563 and 4; AAH21612/
FT AAI38973/AAI45729)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="Y -> H (in Ref. 1; BAE33563 and 4; AAH21612/
FT AAI38973/AAI45729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36303 MW; AA19F757FA5ECF77 CRC64;
MLCRSCAGWL RSLPTLRLPA PGSPPAWSSA RLPALPVWAA ASVSAASPGG WYEALAASAP
VRTAEEVLLG AQEATGLPWW SNIILSTVAL RGAVTLPLAA YQHYILAKVE NLQPEIKDIA
KRLNQEVAVC ARQFGWSKRV ARLTYLKNMR RLISELYVRD NCHPFKATVL VWVQLPMWVF
ISVALRNLST GATHSDGISV QEQLAAGGTL WFPDLTAVDS TWILPVSVGV VNLLIVEIFA
LQKIGTSRFQ MYVTNFVRAV SVLMIPVAAT VPSALVLYWL CSSLMGLAQN LLLRSPGFRQ
LCRIPPSKSD SETPYRDLSA AFCAKFLSRK R
