COX7_YEAST
ID COX7_YEAST Reviewed; 60 AA.
AC P10174; D6W082;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cytochrome c oxidase subunit 7, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VII;
GN Name=COX7; OrderedLocusNames=YMR256C; ORFNames=YM9920.10C;
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=2168889; DOI=10.1016/s0021-9258(17)46235-1;
RA Aggeler R., Capaldi R.A.;
RT "Yeast cytochrome c oxidase subunit VII is essential for assembly of an
RT active enzyme. Cloning, sequencing, and characterization of the nuclear-
RT encoded gene.";
RL J. Biol. Chem. 265:16389-16393(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=2158084; DOI=10.1093/nar/18.6.1632;
RA Calder K.M., McEwen J.E.;
RT "Nucleotide sequence of the gene encoding cytochrome c oxidase subunit VII
RT from Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 18:1632-1632(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-58.
RX PubMed=3013877; DOI=10.1016/s0021-9258(18)67640-9;
RA Power S.D., Lochrie M.A., Poyton R.O.;
RT "The nuclear-coded subunits of yeast cytochrome c oxidase. The amino acid
RT sequences of subunits VII and VIIa, structural similarities between the
RT three smallest polypeptides of the holoenzyme, and implications for
RT biogenesis.";
RL J. Biol. Chem. 261:9206-9209(1986).
RN [7]
RP PROTEIN SEQUENCE OF 2-4, 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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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. {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). {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}; Single-pass membrane protein
CC {ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIa family.
CC {ECO:0000305}.
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DR EMBL; X51506; CAA35871.1; -; Genomic_DNA.
DR EMBL; M31620; AAA34550.1; -; Genomic_DNA.
DR EMBL; Z48639; CAA88583.1; -; Genomic_DNA.
DR EMBL; AY558129; AAS56455.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10156.1; -; Genomic_DNA.
DR PIR; S22248; OBBY7.
DR RefSeq; NP_013983.1; NM_001182763.1.
DR PDB; 6GIQ; EM; 3.23 A; g=1-60.
DR PDB; 6HU9; EM; 3.35 A; g/s=2-60.
DR PDB; 6T0B; EM; 2.80 A; g/t=2-60.
DR PDB; 6T15; EM; 3.29 A; g=2-60.
DR PDB; 6YMX; EM; 3.17 A; g=3-57.
DR PDB; 6YMY; EM; 3.41 A; g=3-57.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; P10174; -.
DR SMR; P10174; -.
DR BioGRID; 35434; 321.
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-7133N; -.
DR IntAct; P10174; 6.
DR MINT; P10174; -.
DR STRING; 4932.YMR256C; -.
DR TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P10174; -.
DR PRIDE; P10174; -.
DR EnsemblFungi; YMR256C_mRNA; YMR256C; YMR256C.
DR GeneID; 855298; -.
DR KEGG; sce:YMR256C; -.
DR SGD; S000004869; COX7.
DR VEuPathDB; FungiDB:YMR256C; -.
DR eggNOG; ENOG502S7M1; Eukaryota.
DR HOGENOM; CLU_169147_2_1_1; -.
DR InParanoid; P10174; -.
DR OMA; WWRHPRS; -.
DR BioCyc; MetaCyc:YMR256C-MON; -.
DR BioCyc; YEAST:YMR256C-MON; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P10174; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P10174; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 InterPro; IPR014367; Cox7_yeast.
DR InterPro; IPR039297; COX7a.
DR Pfam; PF02238; COX7a; 1.
DR PIRSF; PIRSF000282; COX7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3013877,
FT ECO:0000269|PubMed:7851399"
FT CHAIN 2..60
FT /note="Cytochrome c oxidase subunit 7, mitochondrial"
FT /id="PRO_0000183907"
FT TOPO_DOM 2..29
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 54..60
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6YMX"
FT HELIX 26..53
FT /evidence="ECO:0007829|PDB:6T0B"
SQ SEQUENCE 60 AA; 6932 MW; 5798C96AF8134D6D CRC64;
MANKVIQLQK IFQSSTKPLW WRHPRSALYL YPFYAIFAVA VVTPLLYIPN AIRGIKAKKA
