COX6C_MOUSE
ID COX6C_MOUSE Reviewed; 76 AA.
AC Q9CPQ1; Q52KC6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cytochrome c oxidase subunit 6C;
DE AltName: Full=Cytochrome c oxidase polypeptide VIc;
GN Name=Cox6c;
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 PRELIMINARY NUCLEOTIDE SEQUENCE.
RX PubMed=1645653; DOI=10.1111/j.1432-1033.1991.tb15989.x;
RA Schneyder B., Mell O., Anthony G., Kadenbach B.;
RT "Cross reactivity of monoclonal antibodies and cDNA hybridization suggest
RT evolutionary relationships between cytochrome c oxidase subunits VIa and
RT VIc and between VIIa and VIIb.";
RL Eur. J. Biochem. 198:85-92(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP PROTEIN SEQUENCE OF 21-38 AND 48-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P04038}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04038}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)).
CC {ECO:0000250|UniProtKB:P04038}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04038}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P04038}.
CC -!- PTM: Acetylation of Lys-61 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6c family.
CC {ECO:0000305}.
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DR EMBL; AK012602; BAB28348.1; -; mRNA.
DR EMBL; AK013459; BAB28866.1; -; mRNA.
DR EMBL; BC024666; AAH24666.1; -; mRNA.
DR EMBL; BC094413; AAH94413.1; -; mRNA.
DR CCDS; CCDS27424.1; -.
DR PIR; S16083; S16083.
DR RefSeq; NP_444301.1; NM_053071.2.
DR PDB; 7O37; EM; 3.20 A; i=2-76.
DR PDB; 7O3C; EM; 3.30 A; i=2-76.
DR PDB; 7O3E; EM; 3.60 A; i=2-76.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR AlphaFoldDB; Q9CPQ1; -.
DR SMR; Q9CPQ1; -.
DR BioGRID; 198845; 40.
DR CORUM; Q9CPQ1; -.
DR IntAct; Q9CPQ1; 4.
DR STRING; 10090.ENSMUSP00000014457; -.
DR iPTMnet; Q9CPQ1; -.
DR PhosphoSitePlus; Q9CPQ1; -.
DR EPD; Q9CPQ1; -.
DR jPOST; Q9CPQ1; -.
DR MaxQB; Q9CPQ1; -.
DR PaxDb; Q9CPQ1; -.
DR PeptideAtlas; Q9CPQ1; -.
DR PRIDE; Q9CPQ1; -.
DR ProteomicsDB; 283429; -.
DR TopDownProteomics; Q9CPQ1; -.
DR Antibodypedia; 4263; 246 antibodies from 30 providers.
DR DNASU; 12864; -.
DR Ensembl; ENSMUST00000014457; ENSMUSP00000014457; ENSMUSG00000014313.
DR Ensembl; ENSMUST00000153512; ENSMUSP00000123609; ENSMUSG00000014313.
DR Ensembl; ENSMUST00000156915; ENSMUSP00000122391; ENSMUSG00000014313.
DR GeneID; 12864; -.
DR KEGG; mmu:12864; -.
DR UCSC; uc007vmi.1; mouse.
DR CTD; 1345; -.
DR MGI; MGI:104614; Cox6c.
DR VEuPathDB; HostDB:ENSMUSG00000014313; -.
DR eggNOG; ENOG502SEI2; Eukaryota.
DR GeneTree; ENSGT00940000162275; -.
DR HOGENOM; CLU_196254_0_0_1; -.
DR InParanoid; Q9CPQ1; -.
DR OMA; YKNYDPM; -.
DR OrthoDB; 1618740at2759; -.
DR PhylomeDB; Q9CPQ1; -.
DR TreeFam; TF353619; -.
DR UniPathway; UPA00705; -.
DR BioGRID-ORCS; 12864; 33 hits in 75 CRISPR screens.
DR ChiTaRS; Cox6c; mouse.
DR PRO; PR:Q9CPQ1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9CPQ1; protein.
DR Bgee; ENSMUSG00000014313; Expressed in gonadal fat pad and 266 other tissues.
DR ExpressionAtlas; Q9CPQ1; baseline and differential.
DR Genevisible; Q9CPQ1; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR CDD; cd00927; Cyt_c_Oxidase_VIc; 1.
DR Gene3D; 4.10.93.10; -; 1.
DR InterPro; IPR004204; COX6C.
DR InterPro; IPR034884; Cytochrome_c_oxidase_VIc/VIIs.
DR InterPro; IPR037169; Cytochrome_c_oxidase_VIc_sf.
DR Pfam; PF02937; COX6C; 1.
DR SUPFAM; SSF81415; SSF81415; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..76
FT /note="Cytochrome c oxidase subunit 6C"
FT /id="PRO_0000191302"
FT TOPO_DOM 4..14
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT TRANSMEM 15..55
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT TOPO_DOM 56..76
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT HELIX 15..55
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:7O37"
SQ SEQUENCE 76 AA; 8469 MW; BE02A028CF77D5F4 CRC64;
MSSGALLPKP QMRGLLAKRL RVHIAGAFIV ALGVAAAYKF GVAEPRKKAY AEFYRNYDSM
KDFEEMRKAG IFQSAK
