COX41_RAT
ID COX41_RAT Reviewed; 169 AA.
AC P10888;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 160.
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, Cox4a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=2541414; DOI=10.1093/nar/17.7.2851;
RA Goto Y., Amuro N., Okazaki T.;
RT "Nucleotide sequence of cDNA for rat brain and liver cytochrome c oxidase
RT subunit IV.";
RL Nucleic Acids Res. 17:2851-2851(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2544859; DOI=10.1093/nar/17.11.4376;
RA Gopalan G., Droste M., Kadenbach B.;
RT "Nucleotide sequence of cDNA encoding subunit IV of cytochrome c oxidase
RT from fetal rat liver.";
RL Nucleic Acids Res. 17:4376-4376(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2159010; DOI=10.1016/s0021-9258(19)39169-0;
RA Yamada M., Amuro N., Goto Y., Okazaki T.;
RT "Structural organization of the rat cytochrome c oxidase subunit IV gene.";
RL J. Biol. Chem. 265:7687-7692(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2165254; DOI=10.1093/nar/18.13.3992;
RA Amuro N., Yamada M., Goto Y., Okazaki T.;
RT "Complete nucleotide sequence of the gene encoding rat cytochrome c oxidase
RT subunit IV.";
RL Nucleic Acids Res. 18:3992-3992(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2174541; DOI=10.1093/nar/18.22.6581;
RA Virbasius J.V., Scarpulla R.C.;
RT "The rat cytochrome c oxidase subunit IV gene family: tissue-specific and
RT hormonal differences in subunit IV and cytochrome c mRNA expression.";
RL Nucleic Acids Res. 18:6581-6586(1990).
RN [6]
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 [7]
RP PROTEIN SEQUENCE OF 23-32.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7601105; DOI=10.1111/j.1432-1033.1995.tb20556.x;
RA Schaegger H., Noack H., Halangk W., Brandt U., von Jagow G.;
RT "Cytochrome-c oxidase in developing rat heart. Enzymic properties and
RT amino-terminal sequences suggest identity of the fetal heart and the adult
RT liver isoform.";
RL Eur. J. Biochem. 230:235-241(1995).
RN [8]
RP PROTEIN SEQUENCE OF 68-75 AND 150-159, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-58, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP INTERACTION WITH ABCB7.
RX PubMed=31511561; DOI=10.1038/s41598-019-49666-0;
RA Kumar V., Kumar A., Sanawar R., Jaleel A., Santhosh Kumar T.R.,
RA Kartha C.C.;
RT "Chronic Pressure Overload Results in Deficiency of Mitochondrial Membrane
RT Transporter ABCB7 Which Contributes to Iron Overload, Mitochondrial
RT Dysfunction, Metabolic Shift and Worsens Cardiac Function.";
RL Sci. Rep. 9:13170-13170(2019).
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 (PubMed:31511561). {ECO:0000250|UniProtKB:P00423,
CC ECO:0000250|UniProtKB:P13073, ECO:0000250|UniProtKB:P19783,
CC ECO:0000269|PubMed:31511561}.
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; X14209; CAA32426.1; -; mRNA.
DR EMBL; X15029; CAA33133.1; -; mRNA.
DR EMBL; J05425; AAA40949.1; -; Genomic_DNA.
DR EMBL; X54081; CAA38018.1; -; Genomic_DNA.
DR EMBL; BC084719; AAH84719.1; -; mRNA.
DR PIR; A35209; A35209.
DR PIR; S65374; S65374.
DR RefSeq; NP_058898.1; NM_017202.1.
DR AlphaFoldDB; P10888; -.
DR SMR; P10888; -.
DR BioGRID; 248090; 3.
DR CORUM; P10888; -.
DR IntAct; P10888; 2.
DR MINT; P10888; -.
DR STRING; 10116.ENSRNOP00000024033; -.
DR CarbonylDB; P10888; -.
DR iPTMnet; P10888; -.
DR PhosphoSitePlus; P10888; -.
DR SwissPalm; P10888; -.
DR jPOST; P10888; -.
DR PaxDb; P10888; -.
DR PRIDE; P10888; -.
DR DNASU; 29445; -.
DR GeneID; 29445; -.
DR KEGG; rno:29445; -.
DR UCSC; RGD:68374; rat.
DR CTD; 1327; -.
DR RGD; 68374; Cox4i1.
DR VEuPathDB; HostDB:ENSRNOG00000017817; -.
DR eggNOG; KOG4075; Eukaryota.
DR HOGENOM; CLU_117340_1_0_1; -.
DR InParanoid; P10888; -.
DR OMA; ESYAEMN; -.
DR OrthoDB; 1591226at2759; -.
DR PhylomeDB; P10888; -.
DR TreeFam; TF105061; -.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR PRO; PR:P10888; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000017817; Expressed in heart and 20 other tissues.
DR Genevisible; P10888; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
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:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
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 Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7601105"
FT CHAIN 23..169
FT /note="Cytochrome c oxidase subunit 4 isoform 1,
FT mitochondrial"
FT /id="PRO_0000006088"
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:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 19515 MW; F0187C76B7A1A9FE CRC64;
MLATRALSLI GKRAISTSVC LRAHGSVVKS EDYALPSYVD RRDYPLPDVA HVKLLSASQK
ALKEKEKADW SSLSRDEKVQ LYRIQFNESF AEMNKGTNEW KTVVGLAMFF IGFTALVLIW
EKSYVYGPIP HTFDRDWVAM QTKRMLDMKV NPIQGFSAKW DYNKNEWKK
