COX5A_MOUSE
ID COX5A_MOUSE Reviewed; 146 AA.
AC P12787; Q9D2W1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Va;
DE Flags: Precursor;
GN Name=Cox5a;
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=Bone marrow;
RX PubMed=2550898; DOI=10.1093/nar/17.16.6723;
RA Ayane M., Nielson P.J., Koehler G.;
RT "Nucleotide sequence of cDNA encoding mouse cytochrome c oxidase subunit
RT Va.";
RL Nucleic Acids Res. 17:6723-6723(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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=FVB/N-3; TISSUE=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 [4]
RP PROTEIN SEQUENCE OF 69-83 AND 95-103, 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83 AND LYS-109, AND
RP IDENTIFICATION BY MASS 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:P00427}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00427}.
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 AFG1L (By similarity). Interacts with RAB5IF (By
CC similarity). {ECO:0000250|UniProtKB:P00426,
CC ECO:0000250|UniProtKB:P20674}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00426}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00426}; Matrix side
CC {ECO:0000250|UniProtKB:P00426}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC {ECO:0000305}.
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DR EMBL; X15963; CAA34085.1; -; mRNA.
DR EMBL; AK018723; BAB31369.1; -; mRNA.
DR EMBL; BC034302; AAH34302.1; -; mRNA.
DR CCDS; CCDS23223.1; -.
DR PIR; S05495; S05495.
DR RefSeq; NP_031773.2; NM_007747.2.
DR PDB; 7O37; EM; 3.20 A; e=38-146.
DR PDB; 7O3C; EM; 3.30 A; e=38-146.
DR PDB; 7O3E; EM; 3.60 A; e=38-146.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR AlphaFoldDB; P12787; -.
DR SMR; P12787; -.
DR BioGRID; 198841; 44.
DR CORUM; P12787; -.
DR IntAct; P12787; 9.
DR MINT; P12787; -.
DR STRING; 10090.ENSMUSP00000000090; -.
DR iPTMnet; P12787; -.
DR PhosphoSitePlus; P12787; -.
DR SwissPalm; P12787; -.
DR SWISS-2DPAGE; P12787; -.
DR UCD-2DPAGE; P12787; -.
DR EPD; P12787; -.
DR jPOST; P12787; -.
DR MaxQB; P12787; -.
DR PaxDb; P12787; -.
DR PeptideAtlas; P12787; -.
DR PRIDE; P12787; -.
DR ProteomicsDB; 284104; -.
DR TopDownProteomics; P12787; -.
DR Antibodypedia; 27166; 367 antibodies from 32 providers.
DR DNASU; 12858; -.
DR Ensembl; ENSMUST00000000090; ENSMUSP00000000090; ENSMUSG00000000088.
DR GeneID; 12858; -.
DR KEGG; mmu:12858; -.
DR UCSC; uc009puz.1; mouse.
DR CTD; 9377; -.
DR MGI; MGI:88474; Cox5a.
DR VEuPathDB; HostDB:ENSMUSG00000000088; -.
DR eggNOG; KOG4077; Eukaryota.
DR GeneTree; ENSGT00390000001424; -.
DR HOGENOM; CLU_099086_1_1_1; -.
DR InParanoid; P12787; -.
DR OMA; DPHHEES; -.
DR OrthoDB; 1286549at2759; -.
DR PhylomeDB; P12787; -.
DR TreeFam; TF105062; -.
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; 12858; 20 hits in 73 CRISPR screens.
DR ChiTaRS; Cox5a; mouse.
DR PRO; PR:P12787; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P12787; protein.
DR Bgee; ENSMUSG00000000088; Expressed in atrioventricular valve and 249 other tissues.
DR Genevisible; P12787; MM.
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; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00923; Cyt_c_Oxidase_Va; 1.
DR Gene3D; 1.25.40.40; -; 1.
DR InterPro; IPR003204; Cyt_c_oxidase_su5A/6.
DR InterPro; IPR036545; Cyt_c_oxidase_su5A/6_sf.
DR PANTHER; PTHR14200; PTHR14200; 1.
DR Pfam; PF02284; COX5A; 1.
DR SUPFAM; SSF48479; SSF48479; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00426"
FT CHAIN 38..146
FT /note="Cytochrome c oxidase subunit 5A, mitochondrial"
FT /id="PRO_0000006101"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20674"
FT CONFLICT 11
FT /note="Missing (in Ref. 1; CAA34085)"
FT /evidence="ECO:0000305"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:7O37"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:7O37"
SQ SEQUENCE 146 AA; 16101 MW; 8F6AFF91B5C6160F CRC64;
MLAAALRRCT AAAAARGLLH PASAPSPAAA VCSIRCYSHG SHETDEEFDA RWVTYFNKPD
IDAWELRKGM NTLVGYDLVP EPKIIDAALR ACRRLNDFAS AVRILEVVKD KAGPHKEIYP
YVIQELRPTL NELGISTPEE LGLDKV
