COX42_MOUSE
ID COX42_MOUSE Reviewed; 172 AA.
AC Q91W29;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytochrome c oxidase subunit 4 isoform 2, mitochondrial;
DE AltName: Full=Cytochrome c oxidase subunit IV isoform 2;
DE Short=COX IV-2;
DE Flags: Precursor;
GN Name=Cox4i2; Synonyms=Cox4b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=11311561; DOI=10.1016/s0378-1119(01)00385-7;
RA Huettemann M., Kadenbach B., Grossman L.I.;
RT "Mammalian subunit IV isoforms of cytochrome c oxidase.";
RL Gene 267:111-123(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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)).
CC {ECO:0000250|UniProtKB:P00423}.
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; AF271382; AAK49433.1; -; mRNA.
DR EMBL; BC049623; AAH49623.1; -; mRNA.
DR CCDS; CCDS16898.1; -.
DR RefSeq; NP_444321.1; NM_053091.2.
DR RefSeq; XP_017174836.1; XM_017319347.1.
DR AlphaFoldDB; Q91W29; -.
DR SMR; Q91W29; -.
DR STRING; 10090.ENSMUSP00000105446; -.
DR PhosphoSitePlus; Q91W29; -.
DR MaxQB; Q91W29; -.
DR PaxDb; Q91W29; -.
DR PRIDE; Q91W29; -.
DR ProteomicsDB; 284103; -.
DR Antibodypedia; 25206; 182 antibodies from 30 providers.
DR DNASU; 84682; -.
DR Ensembl; ENSMUST00000010020; ENSMUSP00000010020; ENSMUSG00000009876.
DR Ensembl; ENSMUST00000109821; ENSMUSP00000105446; ENSMUSG00000009876.
DR GeneID; 84682; -.
DR KEGG; mmu:84682; -.
DR UCSC; uc008ngg.1; mouse.
DR CTD; 84701; -.
DR MGI; MGI:2135755; Cox4i2.
DR VEuPathDB; HostDB:ENSMUSG00000009876; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00390000002407; -.
DR HOGENOM; CLU_117340_1_1_1; -.
DR InParanoid; Q91W29; -.
DR OMA; MLSRATW; -.
DR OrthoDB; 1591226at2759; -.
DR PhylomeDB; Q91W29; -.
DR TreeFam; TF105061; -.
DR BRENDA; 7.1.1.9; 3474.
DR UniPathway; UPA00705; -.
DR BioGRID-ORCS; 84682; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cox4i2; mouse.
DR PRO; PR:Q91W29; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91W29; protein.
DR Bgee; ENSMUSG00000009876; Expressed in retinal neural layer and 105 other tissues.
DR Genevisible; Q91W29; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISA:MGI.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:MGI.
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 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..172
FT /note="Cytochrome c oxidase subunit 4 isoform 2,
FT mitochondrial"
FT /id="PRO_0000006090"
FT TOPO_DOM 35..101
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00423"
FT TRANSMEM 102..127
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00423"
FT TOPO_DOM 128..172
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00423"
FT REGION 13..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 20206 MW; A2395EF4FD68CEA6 CRC64;
MFSRAARSLV MRTGLRTRGT GTHSPGDAAG SQRRMTPYVD CYAQRSYPMP DEPFCTELSE
EQRALKEKEK GSWTQLSQAE KVALYRLQFH ETFAEMNHRS NEWKTVMGCV FFFIGFTALV
IWWQRVYVFP KKVVTLTEER KAQQLQRLLD MKSNPIQGLA AHWDYEKKEW KK
