COX9_YEAST
ID COX9_YEAST Reviewed; 59 AA.
AC P07255; D6VRT0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cytochrome c oxidase subunit 9, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIIA;
DE Flags: Precursor;
GN Name=COX9; OrderedLocusNames=YDL067C; ORFNames=D2520;
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=3023385; DOI=10.1016/s0021-9258(19)76017-7;
RA Wright R.M., Dircks L.K., Poyton R.O.;
RT "Characterization of COX9, the nuclear gene encoding the yeast
RT mitochondrial protein cytochrome c oxidase subunit VIIa. Subunit VIIa lacks
RT a leader peptide and is an essential component of the holoenzyme.";
RL J. Biol. Chem. 261:17183-17191(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2158998; DOI=10.1016/s0021-9258(19)39110-0;
RA Duhl D.M., Powell T., Poyton R.O.;
RT "Mitochondrial import of cytochrome c oxidase subunit VIIa in Saccharomyces
RT cerevisiae. Identification of sequences required for mitochondrial
RT localization in vivo.";
RL J. Biol. Chem. 265:7273-7277(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2550765; DOI=10.1007/bf00330565;
RA Forsbach V., Pillar T., Gottenoef T., Roedel G.;
RT "Chromosomal localization and expression of CBS1, a translational activator
RT of cytochrome b in yeast.";
RL Mol. Gen. Genet. 218:57-63(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 2-56.
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 [8]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
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 [14]
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 35500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the fungal cytochrome c oxidase subunit 7a
CC family. {ECO:0000305}.
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DR EMBL; J02633; AAB03896.1; -; Genomic_DNA.
DR EMBL; M35260; AAA34523.1; -; Genomic_DNA.
DR EMBL; X16120; CAA34250.1; -; Genomic_DNA.
DR EMBL; Z74115; CAA98632.1; -; Genomic_DNA.
DR EMBL; AY558525; AAS56851.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11790.1; -; Genomic_DNA.
DR PIR; JQ0325; OBBY7A.
DR RefSeq; NP_010216.1; NM_001180126.1.
DR PDB; 6GIQ; EM; 3.23 A; i=1-59.
DR PDB; 6HU9; EM; 3.35 A; i/u=2-56.
DR PDB; 6T0B; EM; 2.80 A; i/v=2-56.
DR PDB; 6T15; EM; 3.29 A; i=2-56.
DR PDB; 6YMX; EM; 3.17 A; i=3-55.
DR PDB; 6YMY; EM; 3.41 A; i=2-53.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; P07255; -.
DR SMR; P07255; -.
DR BioGRID; 31992; 137.
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-5231N; -.
DR IntAct; P07255; 8.
DR STRING; 4932.YDL067C; -.
DR TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR MaxQB; P07255; -.
DR PaxDb; P07255; -.
DR PRIDE; P07255; -.
DR TopDownProteomics; P07255; -.
DR EnsemblFungi; YDL067C_mRNA; YDL067C; YDL067C.
DR GeneID; 851492; -.
DR KEGG; sce:YDL067C; -.
DR SGD; S000002225; COX9.
DR VEuPathDB; FungiDB:YDL067C; -.
DR eggNOG; ENOG502SBM8; Eukaryota.
DR HOGENOM; CLU_196969_0_0_1; -.
DR InParanoid; P07255; -.
DR OMA; ASYWWWG; -.
DR BioCyc; MetaCyc:YDL067C-MON; -.
DR BioCyc; YEAST:YDL067C-MON; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P07255; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P07255; 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:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:SGD.
DR InterPro; IPR014368; Cyt_c_oxidase_su7a_fun.
DR PIRSF; PIRSF000283; COX9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW 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..56
FT /note="Cytochrome c oxidase subunit 9, mitochondrial"
FT /id="PRO_0000006076"
FT PROPEP 57..59
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:3013877"
FT /id="PRO_0000006077"
FT TOPO_DOM 2..8
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 9..44
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 45..56
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554"
FT CONFLICT 2
FT /note="T -> A (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..54
FT /evidence="ECO:0007829|PDB:6T0B"
SQ SEQUENCE 59 AA; 6963 MW; D228F428EA7DAC7C CRC64;
MTIAPITGTI KRRVIMDIVL GFSLGGVMAS YWWWGFHMDK INKREKFYAE LAERKKQEN
