CX7A2_MOUSE
ID CX7A2_MOUSE Reviewed; 83 AA.
AC P48771; O54969; Q545J7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cytochrome c oxidase subunit 7A2, mitochondrial;
DE AltName: Full=Cytochrome c oxidase subunit VIIa-liver/heart;
DE Short=Cytochrome c oxidase subunit VIIa-L;
DE Flags: Precursor;
GN Name=Cox7a2; Synonyms=Cox7a3, Cox7al;
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=Testis;
RX PubMed=1659684; DOI=10.1093/nar/19.22.6123;
RA Hoeoeg C.;
RT "Isolation of a large number of novel mammalian genes by a differential
RT cDNA library screening strategy.";
RL Nucleic Acids Res. 19:6123-6127(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Jaradat S.A., Grossman L.I.;
RT "Mouse liver cytochrome c oxidase subunit VIIa cDNA.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [5]
RP PROTEIN SEQUENCE OF 34-56, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, 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:P10174}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P10174}.
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)). Interacts with
CC PET100. {ECO:0000250|UniProtKB:P14406}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P14406}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P14406}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIa family.
CC {ECO:0000305}.
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DR EMBL; X58486; CAA41396.1; -; mRNA.
DR EMBL; AF037371; AAB92615.1; -; mRNA.
DR EMBL; AK007875; BAB25324.1; -; mRNA.
DR EMBL; AK011269; BAB27507.1; -; mRNA.
DR EMBL; AK019210; BAB31602.1; -; mRNA.
DR EMBL; AK153173; BAE31778.1; -; mRNA.
DR EMBL; BC010979; AAH10979.1; -; mRNA.
DR CCDS; CCDS23366.1; -.
DR PIR; I48286; I48286.
DR RefSeq; NP_034075.2; NM_009945.3.
DR AlphaFoldDB; P48771; -.
DR SMR; P48771; -.
DR BioGRID; 198847; 30.
DR CORUM; P48771; -.
DR IntAct; P48771; 1.
DR STRING; 10090.ENSMUSP00000034881; -.
DR iPTMnet; P48771; -.
DR PhosphoSitePlus; P48771; -.
DR EPD; P48771; -.
DR jPOST; P48771; -.
DR MaxQB; P48771; -.
DR PaxDb; P48771; -.
DR PeptideAtlas; P48771; -.
DR PRIDE; P48771; -.
DR ProteomicsDB; 285404; -.
DR TopDownProteomics; P48771; -.
DR Antibodypedia; 31505; 182 antibodies from 19 providers.
DR DNASU; 12866; -.
DR Ensembl; ENSMUST00000034881; ENSMUSP00000034881; ENSMUSG00000032330.
DR GeneID; 12866; -.
DR KEGG; mmu:12866; -.
DR UCSC; uc009quv.1; mouse.
DR CTD; 1347; -.
DR MGI; MGI:1316715; Cox7a2.
DR VEuPathDB; HostDB:ENSMUSG00000032330; -.
DR eggNOG; ENOG502S4DT; Eukaryota.
DR GeneTree; ENSGT00940000154550; -.
DR HOGENOM; CLU_173437_0_0_1; -.
DR InParanoid; P48771; -.
DR OMA; MWRNVQA; -.
DR OrthoDB; 1548349at2759; -.
DR PhylomeDB; P48771; -.
DR TreeFam; TF105067; -.
DR UniPathway; UPA00705; -.
DR BioGRID-ORCS; 12866; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cox7a2; mouse.
DR PRO; PR:P48771; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P48771; protein.
DR Bgee; ENSMUSG00000032330; Expressed in floor plate of midbrain and 260 other tissues.
DR Genevisible; P48771; 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:0005746; C:mitochondrial respirasome; IBA:GO_Central.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR GO; GO:0097250; P:mitochondrial respirasome assembly; IBA:GO_Central.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IBA:GO_Central.
DR CDD; cd00928; Cyt_c_Oxidase_VIIa; 1.
DR Gene3D; 4.10.91.10; -; 1.
DR InterPro; IPR039297; COX7a.
DR InterPro; IPR036539; Cyt_c_oxidase_su7a_sf.
DR InterPro; IPR003177; Cytc_oxidase_su7a_met.
DR PANTHER; PTHR10510; PTHR10510; 1.
DR Pfam; PF02238; COX7a; 1.
DR SUPFAM; SSF81419; SSF81419; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P14406"
FT CHAIN 24..83
FT /note="Cytochrome c oxidase subunit 7A2, mitochondrial"
FT /id="PRO_0000006146"
FT TOPO_DOM 24..48
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P14406"
FT TRANSMEM 49..77
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07470"
FT TOPO_DOM 78..83
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P14406"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 10
FT /note="Q -> K (in Ref. 1; CAA41396)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="D -> N (in Ref. 1; CAA41396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 83 AA; 9291 MW; 06A3766E23ED69ED CRC64;
MLRNLLALRQ IAQRTISTTS RRHFENKVPE KQKLFQEDNG MPVHLKGGAS DALLYRATMA
LTLGGTAYAI YLLAMAAFPK KQN
