COX5A_MACMU
ID COX5A_MACMU Reviewed; 150 AA.
AC Q53CF8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Va;
DE Flags: Precursor;
GN Name=COX5A;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15851671; DOI=10.1073/pnas.0409714102;
RA Schmidt T.R., Wildman D.E., Uddin M., Opazo J.C., Goodman M.,
RA Grossman L.I.;
RT "Rapid electrostatic evolution at the binding site for cytochrome c on
RT cytochrome c oxidase in anthropoid primates.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6379-6384(2005).
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; AY585861; AAW03189.1; -; mRNA.
DR RefSeq; NP_001035369.1; NM_001040279.1.
DR AlphaFoldDB; Q53CF8; -.
DR SMR; Q53CF8; -.
DR STRING; 9544.ENSMMUP00000015328; -.
DR Ensembl; ENSMMUT00000071252; ENSMMUP00000052933; ENSMMUG00000011677.
DR GeneID; 692061; -.
DR KEGG; mcc:692061; -.
DR CTD; 9377; -.
DR VEuPathDB; HostDB:ENSMMUG00000011677; -.
DR VGNC; VGNC:84327; COX5A.
DR eggNOG; KOG4077; Eukaryota.
DR GeneTree; ENSGT00390000001424; -.
DR HOGENOM; CLU_099086_2_0_1; -.
DR InParanoid; Q53CF8; -.
DR OrthoDB; 1286549at2759; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000006718; Chromosome 7.
DR Bgee; ENSMMUG00000011677; Expressed in skeletal muscle tissue and 22 other tissues.
DR ExpressionAtlas; Q53CF8; baseline.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00426"
FT CHAIN 42..150
FT /note="Cytochrome c oxidase subunit 5A, mitochondrial"
FT /id="PRO_0000253608"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12787"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12787"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20674"
SQ SEQUENCE 150 AA; 16669 MW; 2C026451B3D14674 CRC64;
MLGAALRRCA VAATTWAGPR GLLHSARTPG PAAAIQSVRC YSHGSHETDE EFDARWVTYF
NKPDIDAWEL RKGINTLVTY DLVPEPKIID AALRACRRLN DFASTVRILE AVKDKAGPHK
EIYPYVIQEL RPTLNELGIS TPEELGLDKV
