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COX41_PERPO
ID   COX41_PERPO             Reviewed;         137 AA.
AC   O46586;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide IV;
DE   AltName: Full=Cytochrome c oxidase subunit IV isoform 1;
DE            Short=COX IV-1;
DE   Flags: Fragment;
GN   Name=COX4I1; Synonyms=COX4;
OS   Perodicticus potto edwarsi (Potto).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Lorisidae; Perodicticus.
OX   NCBI_TaxID=9473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9115172; DOI=10.1007/pl00006172;
RA   Wu W., Goodman M., Lomax M.I., Grossman L.I.;
RT   "Molecular evolution of cytochrome c oxidase subunit IV: evidence for
RT   positive selection in simian primates.";
RL   J. Mol. Evol. 44:477-491(1997).
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:P00424}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00424}.
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 PHB2; the interaction decreases in absence of SPHK2 (By
CC       similarity). Interacts with AFG1L (By similarity). Interacts with
CC       ABCB7; this interaction allows the regulation of cellular iron
CC       homeostasis and cellular reactive oxygen species (ROS) levels in
CC       cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P00423,
CC       ECO:0000250|UniProtKB:P10888, ECO:0000250|UniProtKB:P13073,
CC       ECO:0000250|UniProtKB:P19783}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00423}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00423}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
CC       {ECO:0000305}.
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DR   EMBL; AH005842; AAB97850.1; -; Genomic_DNA.
DR   AlphaFoldDB; O46586; -.
DR   SMR; O46586; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR   CDD; cd00922; Cyt_c_Oxidase_IV; 1.
DR   Gene3D; 1.10.442.10; -; 1.
DR   InterPro; IPR013288; Cyt_c_oxidase_su4.
DR   InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR   InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR   PANTHER; PTHR10707; PTHR10707; 1.
DR   Pfam; PF02936; COX4; 1.
DR   PRINTS; PR01873; CYTCOXIDASE4.
DR   SUPFAM; SSF81406; SSF81406; 1.
PE   3: Inferred from homology;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..137
FT                   /note="Cytochrome c oxidase subunit 4 isoform 1,
FT                   mitochondrial"
FT                   /id="PRO_0000194078"
FT   TOPO_DOM        <1..66
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00423"
FT   TRANSMEM        67..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00423"
FT   TOPO_DOM        93..137
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00423"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13073"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10888"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10888"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P13073"
FT   MOD_RES         28
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P19783"
FT   MOD_RES         35
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19783"
FT   NON_TER         1
SQ   SEQUENCE   137 AA;  16149 MW;  F5A6A1A9AA09D2A5 CRC64;
     YALPSYVDRR DYPLPDVAHV KHLSASQKAL KEKEKASWSN LSMDEKVELY RIQFKESFAE
     MNRGTNEWKT VVGTAMLFIG FTALIVIWEK RYVYGPIPHT FDPDWVAKQT KKMLDMKVNP
     IQGFAAKWDY EKQEWKK
 
 
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