COX6_YEAST
ID COX6_YEAST Reviewed; 148 AA.
AC P00427; D3DL00;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Cytochrome c oxidase subunit 6, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VI;
DE Flags: Precursor;
GN Name=COX6; OrderedLocusNames=YHR051W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6210289; DOI=10.1016/s0021-9258(17)42563-4;
RA Wright R.M., Ko C., Cumsky M.G., Poyton R.O.;
RT "Isolation and sequence of the structural gene for cytochrome c oxidase
RT subunit VI from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 259:15401-15407(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=2537949; DOI=10.1093/nar/17.3.1103;
RA Wright R.M., Rosenzweig B., Poyton R.O.;
RT "Organization and expression of the COX6 genetic locus in Saccharomyces
RT cerevisiae: multiple mRNAs with different 3' termini are transcribed from
RT COX6 and regulated differentially.";
RL Nucleic Acids Res. 17:1103-1120(1989).
RN [6]
RP PROTEIN SEQUENCE OF 41-148.
RX PubMed=6290493; DOI=10.1016/s0021-9258(18)33625-1;
RA Gregor I., Tsugita A.;
RT "The amino acid sequence of cytochrome c oxidase subunit VI from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 257:13081-13087(1982).
RN [7]
RP PROTEIN SEQUENCE OF 41-54, AND COMPOSITION OF THE CYTOCHROME C OXIDASE
RP COMPLEX.
RX PubMed=1331058; DOI=10.1016/s0021-9258(18)41697-3;
RA Taanman J.-W., Capaldi R.A.;
RT "Purification of yeast cytochrome c oxidase with a subunit composition
RT resembling the mammalian enzyme.";
RL J. Biol. Chem. 267:22481-22485(1992).
RN [8]
RP PROTEIN SEQUENCE OF 41-43, AND COMPOSITION OF THE CYTOCHROME C OXIDASE
RP COMPLEX.
RX PubMed=7851399; DOI=10.1111/j.1432-1033.1995.tb20388.x;
RA Geier B.M., Schagger H., Ortwein C., Link T.A., Hagen W.R., Brandt U.,
RA Von Jagow G.;
RT "Kinetic properties and ligand binding of the eleven-subunit cytochrome-c
RT oxidase from Saccharomyces cerevisiae isolated with a novel large-scale
RT purification method.";
RL Eur. J. Biochem. 227:296-302(1995).
RN [9]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777;
RA Schaegger H., Pfeiffer K.;
RT "Supercomplexes in the respiratory chains of yeast and mammalian
RT mitochondria.";
RL EMBO J. 19:1777-1783(2000).
RN [10]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10764779; DOI=10.1074/jbc.m001901200;
RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.;
RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a
RT single supracomplex in yeast mitochondria.";
RL J. Biol. Chem. 275:18093-18098(2000).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS).
RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7;
RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M.,
RA Brzezinski P., Ott M.;
RT "Cryo-EM structure of the yeast respiratory supercomplex.";
RL Nat. Struct. Mol. Biol. 26:50-57(2019).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS), AND FUNCTION.
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(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 COX2 and heme A of COX1 to the
CC active site in COX1, a binuclear center (BNC) formed by heme A3 and
CC copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules
CC using 4 electrons from cytochrome c in the IMS and 4 protons from the
CC mitochondrial matrix (Probable). COX6 may stabilize the region of CIV
CC at the interface with CIII, supporting a role in formation or stability
CC of the CIII(2)IV(2) SC (PubMed:30598554). {ECO:0000269|PubMed:30598554,
CC ECO:0000305|PubMed:30598554}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 12 subunits. The complex is composed of
CC a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the
CC mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B),
CC COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in
CC the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554).
CC The complex exists as a monomer or a dimer and forms supercomplexes
CC (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and
CC III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556,
CC PubMed:30598554). COX26 interacts with COX1, COX2, COX6 and COX9
CC (PubMed:30598554). {ECO:0000269|PubMed:10764779,
CC ECO:0000269|PubMed:10775262, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:30598556, ECO:0000269|PubMed:7851399}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30598554}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30598554}; Matrix side
CC {ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 12500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M10138; AAA66900.1; -; Genomic_DNA.
DR EMBL; U00062; AAB68899.1; -; Genomic_DNA.
DR EMBL; AY558278; AAS56604.1; -; Genomic_DNA.
DR EMBL; X14452; CAA32622.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06744.1; -; Genomic_DNA.
DR PIR; A22853; OTBY6.
DR RefSeq; NP_011918.1; NM_001179181.1.
DR PDB; 6GIQ; EM; 3.23 A; f=1-148.
DR PDB; 6HU9; EM; 3.35 A; f/r=41-148.
DR PDB; 6T0B; EM; 2.80 A; f/s=41-148.
DR PDB; 6T15; EM; 3.29 A; f=41-148.
DR PDB; 6YMX; EM; 3.17 A; f=47-145.
DR PDB; 6YMY; EM; 3.41 A; f=47-145.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; P00427; -.
DR SMR; P00427; -.
DR BioGRID; 36483; 438.
DR ComplexPortal; CPX-1721; Mitochondrial respiratory chain complex IV, COX5A variant.
DR ComplexPortal; CPX-1722; Mitochondrial respiratory chain complex IV, COX5B variant.
DR DIP; DIP-6606N; -.
DR IntAct; P00427; 6.
DR MINT; P00427; -.
DR STRING; 4932.YHR051W; -.
DR TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR MaxQB; P00427; -.
DR PaxDb; P00427; -.
DR PRIDE; P00427; -.
DR EnsemblFungi; YHR051W_mRNA; YHR051W; YHR051W.
DR GeneID; 856448; -.
DR KEGG; sce:YHR051W; -.
DR SGD; S000001093; COX6.
DR VEuPathDB; FungiDB:YHR051W; -.
DR eggNOG; KOG4077; Eukaryota.
DR GeneTree; ENSGT00390000001424; -.
DR HOGENOM; CLU_099086_0_1_1; -.
DR InParanoid; P00427; -.
DR OMA; DPHHEES; -.
DR BioCyc; MetaCyc:YHR051W-MON; -.
DR BioCyc; YEAST:YHR051W-MON; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P00427; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P00427; protein.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:ComplexPortal.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR CDD; cd00923; Cyt_c_Oxidase_Va; 1.
DR Gene3D; 1.25.40.40; -; 1.
DR InterPro; IPR003204; Cyt_c_oxidase_su5A/6.
DR InterPro; IPR036545; Cyt_c_oxidase_su5A/6_sf.
DR PANTHER; PTHR14200; PTHR14200; 1.
DR Pfam; PF02284; COX5A; 1.
DR SUPFAM; SSF48479; SSF48479; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1331058,
FT ECO:0000269|PubMed:6290493, ECO:0000269|PubMed:7851399"
FT CHAIN 41..148
FT /note="Cytochrome c oxidase subunit 6, mitochondrial"
FT /id="PRO_0000006108"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6T15"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6T0B"
SQ SEQUENCE 148 AA; 17342 MW; 91F2AF286BD2FB1A CRC64;
MLSRAIFRNP VINRTLLRAR PGAYHATRLT KNTFIQSRKY SDAHDEETFE EFTARYEKEF
DEAYDLFEVQ RVLNNCFSYD LVPAPAVIEK ALRAARRVND LPTAIRVFEA LKYKVENEDQ
YKAYLDELKD VRQELGVPLK EELFPSSS
