COX3_RAT
ID COX3_RAT Reviewed; 261 AA.
AC P05505;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=Mtco3; Synonyms=Coiii, mt-Co3;
OS Rattus norvegicus (Rat).
OG Mitochondrion.
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 [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=24185961; DOI=10.1007/bf00365694;
RA Grosskopf R., Feldmann H.;
RT "Analysis of a DNA segment from rat liver mitochondria containing the genes
RT for the cytochrome oxidase subunits I, II and III, ATPase subunit 6, and
RT several tRNA genes.";
RL Curr. Genet. 4:151-158(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=6091655;
RA Pepe G., Holtrop M., Gadaleta G., Kroon A.M., Cantatore P., Gallerani R.,
RA de Benedetto C., Quagliariello C., Sbisa E., Saccone C.;
RT "Non-random patterns of nucleotide substitutions and codon strategy in the
RT mammalian mitochondrial genes coding for identified and unidentified
RT reading frames.";
RL Biochem. Int. 6:553-563(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=2504926; DOI=10.1007/bf02602930;
RA Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.;
RT "The complete nucleotide sequence of the Rattus norvegicus mitochondrial
RT genome: cryptic signals revealed by comparative analysis between
RT vertebrates.";
RL J. Mol. Evol. 28:497-516(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-11.
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).
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:P00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
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:P00415}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00415}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00415}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; J01435; AAD15020.1; -; Genomic_DNA.
DR EMBL; M27315; AAB00994.1; -; Genomic_DNA.
DR EMBL; X14848; CAA32960.1; -; Genomic_DNA.
DR EMBL; AY172581; AAN77600.1; -; Genomic_DNA.
DR PIR; S04753; S04753.
DR RefSeq; AP_004898.1; AC_000022.2.
DR RefSeq; YP_665635.1; NC_001665.2.
DR AlphaFoldDB; P05505; -.
DR SMR; P05505; -.
DR CORUM; P05505; -.
DR STRING; 10116.ENSRNOP00000051326; -.
DR CarbonylDB; P05505; -.
DR iPTMnet; P05505; -.
DR PhosphoSitePlus; P05505; -.
DR PaxDb; P05505; -.
DR PRIDE; P05505; -.
DR Ensembl; ENSRNOT00000049683; ENSRNOP00000051326; ENSRNOG00000030700.
DR GeneID; 26204; -.
DR KEGG; rno:26204; -.
DR CTD; 4514; -.
DR RGD; 621873; mt-Co3.
DR eggNOG; KOG4664; Eukaryota.
DR GeneTree; ENSGT00390000013064; -.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; P05505; -.
DR OMA; SIYWWGS; -.
DR OrthoDB; 1304563at2759; -.
DR PhylomeDB; P05505; -.
DR TreeFam; TF343435; -.
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 PRO; PR:P05505; -.
DR Proteomes; UP000002494; Mitochondrion.
DR Bgee; ENSRNOG00000030700; Expressed in heart and 18 other tissues.
DR ExpressionAtlas; P05505; baseline and differential.
DR Genevisible; P05505; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7601105"
FT CHAIN 2..261
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183844"
FT TOPO_DOM 2..15
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 16..34
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 35..40
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 41..66
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 67..72
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 73..105
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 106..128
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 129..152
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 153..155
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 156..183
FT /note="Helical; Name=V"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 184..190
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 191..223
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 224..232
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 233..256
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 257..261
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT CONFLICT 2
FT /note="T -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29871 MW; 8B5CF8B2AF36F3D3 CRC64;
MTHQTHAYHM VNPSPWPLTG ALSALLLTSG LVMWFHYNST ILLSLGLLTN ILTMYQWWRD
IIREGTYQGH HTPIVQKGLR YGMILFIVSE VFFFAGFFWA FYHSSLVPTH DLGGCWPPTG
ITPLNPLEVP LLNTSVLLAS GVSITWAHHS LMEGNRNHMN QALLITILLG LYFTILQASE
YFETSFSISD GIYGSTFFMA TGFHGLHVII GSTFLIVCLL RQLKFHFTSK HHFGFEAAAW
YWHFVDVVWL FLYVSIYWWG S
