COA6_MOUSE
ID COA6_MOUSE Reviewed; 79 AA.
AC Q8BGD8;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c oxidase assembly factor 6 homolog;
GN Name=Coa6;
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=C57BL/6J; TISSUE=Small intestine, and Tongue;
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=FVB/N; TISSUE=Colon, Mammary gland, and Mammary tumor;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=18614015; DOI=10.1016/j.cell.2008.06.016;
RA Pagliarini D.J., Calvo S.E., Chang B., Sheth S.A., Vafai S.B., Ong S.E.,
RA Walford G.A., Sugiana C., Boneh A., Chen W.K., Hill D.E., Vidal M.,
RA Evans J.G., Thorburn D.R., Carr S.A., Mootha V.K.;
RT "A mitochondrial protein compendium elucidates complex I disease biology.";
RL Cell 134:112-123(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC 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: Involved in the maturation of the mitochondrial respiratory
CC chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps
CC of complex IV assembly. Mitochondrial respiratory chain complex IV or
CC cytochrome c oxidase is the component of the respiratory chain that
CC catalyzes the transfer of electrons from intermembrane space cytochrome
CC c to molecular oxygen in the matrix and as a consequence contributes to
CC the proton gradient involved in mitochondrial ATP synthesis. May also
CC be required for efficient formation of respiratory supercomplexes
CC comprised of complexes III and IV. {ECO:0000250|UniProtKB:Q5JTJ3}.
CC -!- SUBUNIT: Found in a complex with TMEM177, COX20, MT-CO2/COX2, COX18,
CC SCO1 and SCO2. Interacts with COA1, MT-CO2/COX2, SCO1, SCO2 and COX20.
CC Interacts with COX20 in a MT-CO2/COX2- and COX18-dependent manner.
CC Interacts with COX16. {ECO:0000250|UniProtKB:Q5JTJ3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}.
CC Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q5JTJ3}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC {ECO:0000305}.
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DR EMBL; AK008041; BAC25196.1; -; mRNA.
DR EMBL; AK009404; BAC25257.1; -; mRNA.
DR EMBL; AC151908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11811.1; -; Genomic_DNA.
DR EMBL; BC024399; AAH24399.1; -; mRNA.
DR EMBL; BC038634; AAH38634.1; -; mRNA.
DR EMBL; BC046907; AAH46907.1; -; mRNA.
DR CCDS; CCDS52709.1; -.
DR RefSeq; NP_778152.1; NM_174987.4.
DR AlphaFoldDB; Q8BGD8; -.
DR SMR; Q8BGD8; -.
DR STRING; 10090.ENSMUSP00000058279; -.
DR iPTMnet; Q8BGD8; -.
DR PhosphoSitePlus; Q8BGD8; -.
DR EPD; Q8BGD8; -.
DR jPOST; Q8BGD8; -.
DR MaxQB; Q8BGD8; -.
DR PaxDb; Q8BGD8; -.
DR PeptideAtlas; Q8BGD8; -.
DR PRIDE; Q8BGD8; -.
DR ProteomicsDB; 277990; -.
DR Antibodypedia; 34692; 101 antibodies from 20 providers.
DR Ensembl; ENSMUST00000059093; ENSMUSP00000058279; ENSMUSG00000051671.
DR Ensembl; ENSMUST00000211868; ENSMUSP00000148765; ENSMUSG00000051671.
DR GeneID; 67892; -.
DR KEGG; mmu:67892; -.
DR UCSC; uc009nyu.2; mouse.
DR CTD; 388753; -.
DR MGI; MGI:1915142; Coa6.
DR VEuPathDB; HostDB:ENSMUSG00000051671; -.
DR eggNOG; KOG3057; Eukaryota.
DR GeneTree; ENSGT00390000004094; -.
DR HOGENOM; CLU_142408_4_0_1; -.
DR InParanoid; Q8BGD8; -.
DR OMA; RDEYWRC; -.
DR OrthoDB; 1618895at2759; -.
DR PhylomeDB; Q8BGD8; -.
DR TreeFam; TF335992; -.
DR BioGRID-ORCS; 67892; 20 hits in 71 CRISPR screens.
DR ChiTaRS; Coa6; mouse.
DR PRO; PR:Q8BGD8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGD8; protein.
DR Bgee; ENSMUSG00000051671; Expressed in atrioventricular valve and 254 other tissues.
DR Genevisible; Q8BGD8; MM.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISS:UniProtKB.
DR GO; GO:0042774; P:plasma membrane ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
DR CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR Gene3D; 1.10.10.140; -; 1.
DR InterPro; IPR042289; COA6.
DR InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR PANTHER; PTHR46690; PTHR46690; 1.
DR Pfam; PF02297; COX6B; 1.
DR SUPFAM; SSF47694; SSF47694; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Mitochondrion; Reference proteome.
FT CHAIN 1..79
FT /note="Cytochrome c oxidase assembly factor 6 homolog"
FT /id="PRO_0000420734"
FT DOMAIN 9..52
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 12..22
FT /note="Cx9C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 33..44
FT /note="Cx10C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 12..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 22..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 79 AA; 9298 MW; A35B6ED61AB0D4F5 CRC64;
MAAPSMKERQ ACWGARDLYW RCLDDNAEDA ARCQKLRSSF EASCPQQWIK YFDKRRDYLK
FKEKFEAGGF QSSQSTENS
