COX7C_MOUSE
ID COX7C_MOUSE Reviewed; 63 AA.
AC P17665; Q3U5S7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cytochrome c oxidase subunit 7C, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIIc;
DE Flags: Precursor;
GN Name=Cox7c; Synonyms=Cox7c1;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=2163523; DOI=10.1093/nar/18.12.3645;
RA Akamatsu M., Grossman L.I.;
RT "Nucleotide sequence of a cDNA for mouse cytochrome c oxidase subunit
RT VIIc.";
RL Nucleic Acids Res. 18:3645-3645(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Small intestine;
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, and FVB/N; TISSUE=Brain, and Colon;
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 37-57, AND IDENTIFICATION BY MASS 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=Brown adipose tissue, and Kidney;
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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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:P04039}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04039}.
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)) (By similarity).
CC Interacts with RAB5IF (By similarity). {ECO:0000250|UniProtKB:P00430,
CC ECO:0000250|UniProtKB:P15954}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00430}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P00430}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIc family.
CC {ECO:0000305}.
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DR EMBL; X52940; CAA37115.1; -; mRNA.
DR EMBL; AK002494; BAB22142.1; -; mRNA.
DR EMBL; AK027989; BAC25693.1; -; mRNA.
DR EMBL; AK131871; BAE20843.1; -; mRNA.
DR EMBL; AK153444; BAE31999.1; -; mRNA.
DR EMBL; AK168077; BAE40050.1; -; mRNA.
DR EMBL; BC010772; AAH10772.1; -; mRNA.
DR EMBL; BC086792; AAH86792.1; -; mRNA.
DR CCDS; CCDS26668.1; -.
DR PIR; S10303; S10303.
DR RefSeq; NP_031775.1; NM_007749.3.
DR PDB; 7O37; EM; 3.20 A; l=17-63.
DR PDB; 7O3C; EM; 3.30 A; l=17-63.
DR PDB; 7O3E; EM; 3.60 A; l=17-63.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR AlphaFoldDB; P17665; -.
DR SMR; P17665; -.
DR BioGRID; 198848; 10.
DR CORUM; P17665; -.
DR STRING; 10090.ENSMUSP00000115419; -.
DR iPTMnet; P17665; -.
DR PhosphoSitePlus; P17665; -.
DR EPD; P17665; -.
DR jPOST; P17665; -.
DR MaxQB; P17665; -.
DR PaxDb; P17665; -.
DR PeptideAtlas; P17665; -.
DR PRIDE; P17665; -.
DR ProteomicsDB; 283609; -.
DR TopDownProteomics; P17665; -.
DR Antibodypedia; 44491; 57 antibodies from 17 providers.
DR DNASU; 12867; -.
DR Ensembl; ENSMUST00000131011; ENSMUSP00000115419; ENSMUSG00000017778.
DR GeneID; 12867; -.
DR KEGG; mmu:12867; -.
DR UCSC; uc007riy.1; mouse.
DR CTD; 1350; -.
DR MGI; MGI:103226; Cox7c.
DR VEuPathDB; HostDB:ENSMUSG00000017778; -.
DR eggNOG; KOG4527; Eukaryota.
DR GeneTree; ENSGT00390000018086; -.
DR HOGENOM; CLU_194769_0_0_1; -.
DR InParanoid; P17665; -.
DR OMA; MMAAFFG; -.
DR OrthoDB; 1642074at2759; -.
DR PhylomeDB; P17665; -.
DR TreeFam; TF105069; -.
DR BRENDA; 7.1.1.9; 3474.
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 UniPathway; UPA00705; -.
DR BioGRID-ORCS; 12867; 11 hits in 40 CRISPR screens.
DR ChiTaRS; Cox7c; mouse.
DR PRO; PR:P17665; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P17665; protein.
DR Bgee; ENSMUSG00000017778; Expressed in quadriceps femoris and 94 other tissues.
DR ExpressionAtlas; P17665; baseline and differential.
DR Genevisible; P17665; 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; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00929; Cyt_c_Oxidase_VIIc; 1.
DR Gene3D; 4.10.49.10; -; 1.
DR InterPro; IPR004202; COX7C/Cox8.
DR InterPro; IPR036636; COX7C/Cox8_sf.
DR PANTHER; PTHR13313; PTHR13313; 1.
DR Pfam; PF02935; COX7C; 1.
DR SUPFAM; SSF81427; SSF81427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00430"
FT CHAIN 17..63
FT /note="Cytochrome c oxidase subunit 7C, mitochondrial"
FT /id="PRO_0000006166"
FT TOPO_DOM 17..33
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00430"
FT TRANSMEM 34..60
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00430"
FT TOPO_DOM 61..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00430"
FT MOD_RES 25
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 25
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 34..62
FT /evidence="ECO:0007829|PDB:7O37"
SQ SEQUENCE 63 AA; 7333 MW; C6A2AD4ABFEB2C7B CRC64;
MLGQSIRRFT TSVVRRSHYE EGPGKNLPFS VENKWRLLAM MTVYFGSGFA APFFIVRHQL
LKK
