ID   COX5A_MANSE             Reviewed;          63 AA.
AC   O61694;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide Va;
DE   Flags: Precursor; Fragment;
GN   Name=COVA;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fat body;
RA   Scholz F.R., Trenczek T., Kanost M.R.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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 a catalytic core of 3 subunits and
CC       several supernumerary subunits. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC       complex, complex III, CIII). {ECO:0000250|UniProtKB:P00427}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00427}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00427}; Matrix side
CC       {ECO:0000250|UniProtKB:P00427}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC       {ECO:0000305}.
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DR   EMBL; AF060794; AAC15761.1; -; mRNA.
DR   AlphaFoldDB; O61694; -.
DR   SMR; O61694; -.
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   Gene3D; 1.25.40.40; -; 1.
DR   InterPro; IPR003204; Cyt_c_oxidase_su5A/6.
DR   InterPro; IPR036545; Cyt_c_oxidase_su5A/6_sf.
DR   Pfam; PF02284; COX5A; 1.
DR   SUPFAM; SSF48479; SSF48479; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..>63
FT                   /note="Cytochrome c oxidase subunit 5A, mitochondrial"
FT                   /id="PRO_0000006105"
FT   NON_TER         63
SQ   SEQUENCE   63 AA;  7045 MW;  57689072F6D2F593 CRC64;
     MLKSASGALA NVLKRSLVPA ARVTAVVPLR RSHGGPVESD EEFDSRYEAF FNRKDIDGWE
     IRK