COX41_RABIT
ID COX41_RABIT Reviewed; 169 AA.
AC Q9TTT8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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: Precursor;
GN Name=COX4I1; Synonyms=COX4, COXIV;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RA Wu X., Hudson A.P.;
RT "Cloning and characterization of genes coxIV and coxVIa2 from the rabbit
RT genome.";
RL Submitted (OCT-1999) 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: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; AF198088; AAF13254.1; -; mRNA.
DR RefSeq; NP_001164353.1; NM_001170882.1.
DR AlphaFoldDB; Q9TTT8; -.
DR SMR; Q9TTT8; -.
DR STRING; 9986.ENSOCUP00000001489; -.
DR iPTMnet; Q9TTT8; -.
DR KEGG; ocu:100327269; -.
DR eggNOG; KOG4075; Eukaryota.
DR InParanoid; Q9TTT8; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001811; Unplaced.
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 2: Evidence at transcript level;
KW Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT CHAIN 23..169
FT /note="Cytochrome c oxidase subunit 4 isoform 1,
FT mitochondrial"
FT /id="PRO_0000006087"
FT TOPO_DOM 23..98
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00423"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00423"
FT TOPO_DOM 125..169
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00423"
FT MOD_RES 29
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT MOD_RES 29
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13073"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10888"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13073"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19783"
SQ SEQUENCE 169 AA; 19599 MW; 0E5C08CF577FFB32 CRC64;
MLPTRLLSFS GSRAISTSFC LRAHGSVVKS EDYALPSYVD RRDYPLPDVA HVKQLSAGQK
ALKEKEKAPW GSLTRDEKVE LYRIQFNESF AEMNRGTNEW KTVVGTALFF IGFTALILIW
EKHYVYGPIP HTFDKEWVAM QTKRMLDMKV SPIQGFSAKW DYNKNEWRK
