COX26_YEAST
ID COX26_YEAST Reviewed; 66 AA.
AC Q2V2P9; D6VSA5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cytochrome c oxidase subunit 26, mitochondrial;
DE Flags: Precursor;
GN Name=COX26; OrderedLocusNames=YDR119W-A;
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 [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 [2]
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 [3]
RP GENOME REANNOTATION.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [4]
RP PROTEIN SEQUENCE OF 9-18, FUNCTION, AND IDENTIFICATION IN THE CYTOCHROME C
RP OXIDASE COMPLEX.
RX PubMed=27091403; DOI=10.1016/j.bbamcr.2016.04.012;
RA Strecker V., Kadeer Z., Heidler J., Cruciat C.M., Angerer H., Giese H.,
RA Pfeiffer K., Stuart R.A., Wittig I.;
RT "Supercomplex-associated Cox26 protein binds to cytochrome c oxidase.";
RL Biochim. Biophys. Acta 1863:1643-1652(2016).
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION IN THE CYTOCHROME C OXIDASE
RP COMPLEX, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=27083394; DOI=10.1016/j.bbamcr.2016.04.007;
RA Levchenko M., Wuttke J.M., Roempler K., Schmidt B., Neifer K., Juris L.,
RA Wissel M., Rehling P., Deckers M.;
RT "Cox26 is a novel stoichiometric subunit of the yeast cytochrome c
RT oxidase.";
RL Biochim. Biophys. Acta 1863:1624-1632(2016).
RN [6]
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 -!- 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. The complex exists as a monomer or a dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with a
CC dimer of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII), resulting in 2 different assemblies
CC (supercomplexes III(2)IV and III(2)IV(2)).
CC {ECO:0000269|PubMed:30598554}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27083394, ECO:0000269|PubMed:30598554}; Single-pass
CC membrane protein {ECO:0000269|PubMed:27083394,
CC ECO:0000269|PubMed:30598554}.
CC -!- SIMILARITY: Belongs to the fungal cytochrome c oxidase subunit 26
CC family. {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; Z48758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006938; DAA11965.1; -; Genomic_DNA.
DR RefSeq; NP_001032575.1; NM_001184681.1.
DR PDB; 6HU9; EM; 3.35 A; l/x=1-66.
DR PDB; 6T0B; EM; 2.80 A; l/y=1-66.
DR PDB; 6T15; EM; 3.29 A; l=1-66.
DR PDB; 6YMX; EM; 3.17 A; m=26-63.
DR PDB; 6YMY; EM; 3.41 A; m=26-63.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; Q2V2P9; -.
DR SMR; Q2V2P9; -.
DR BioGRID; 531941; 14.
DR IntAct; Q2V2P9; 3.
DR MINT; Q2V2P9; -.
DR STRING; 4932.YDR119W-A; -.
DR PaxDb; Q2V2P9; -.
DR PRIDE; Q2V2P9; -.
DR EnsemblFungi; YDR119W-A_mRNA; YDR119W-A; YDR119W-A.
DR GeneID; 3799970; -.
DR KEGG; sce:YDR119W-A; -.
DR SGD; S000113555; COX26.
DR VEuPathDB; FungiDB:YDR119W-A; -.
DR eggNOG; ENOG502SFY0; Eukaryota.
DR HOGENOM; CLU_195457_0_0_1; -.
DR InParanoid; Q2V2P9; -.
DR BioCyc; YEAST:G3O-30127-MON; -.
DR ChiTaRS; COX26; yeast.
DR PRO; PR:Q2V2P9; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q2V2P9; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005746; C:mitochondrial respirasome; IDA:SGD.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IMP:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..8
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:27083394,
FT ECO:0000269|PubMed:27091403"
FT CHAIN 9..66
FT /note="Cytochrome c oxidase subunit 26, mitochondrial"
FT /id="PRO_0000253829"
FT TOPO_DOM 9..27
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554,
FT ECO:0000305|PubMed:27083394"
FT TRANSMEM 28..64
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 65..66
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554,
FT ECO:0000305|PubMed:27083394"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6T15"
FT HELIX 28..51
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6T0B"
SQ SEQUENCE 66 AA; 7452 MW; 8DFBD2A4C97963C4 CRC64;
MFFSQVLRSS ARAAPIKRYT GGRIGESWVI TEGRRLIPEI FQWSAVLSVC LGWPGAVYFF
SKARKA
