ID   COX5A_PLEDO             Reviewed;         150 AA.
AC   B0VYY1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide Va;
DE   Flags: Precursor;
GN   Name=COX5A;
OS   Plecturocebus donacophilus (Bolivian gray titi monkey) (Callicebus
OS   donacophilus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC   Pitheciidae; Callicebinae; Plecturocebus.
OX   NCBI_TaxID=230833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18197981; DOI=10.1186/1471-2148-8-8;
RA   Uddin M., Opazo J.C., Wildman D.E., Sherwood C.C., Hof P.R., Goodman M.,
RA   Grossman L.I.;
RT   "Molecular evolution of the cytochrome c oxidase subunit 5A gene in
RT   primates.";
RL   BMC Evol. Biol. 8:8-8(2008).
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; DQ987248; ABK92295.1; -; mRNA.
DR   AlphaFoldDB; B0VYY1; -.
DR   SMR; B0VYY1; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
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; 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_0000355976"
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;  16470 MW;  7F817E3C6149259F CRC64;
     MLGAALRRCA VAAAARAGPR GLLHSAPTPG PAAAIQSVRC YSHGSSETDE EFDARWVTYF
     NKPDIDAWEL RKGINTLVTY DLVPEPKIID AALRACRRLN DFASTVRILE AVKDKAGPHK
     EIYPYVIQEL RPTLNELGIS TPEELGLDKV