COX12_YEAST
ID COX12_YEAST Reviewed; 83 AA.
AC Q01519; D6VY41; Q9URA6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Cytochrome c oxidase subunit 12, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIb;
GN Name=COX12; OrderedLocusNames=YLR038C;
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], AND PROTEIN SEQUENCE OF 2-8; 11-13 AND
RP 14.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1331057; DOI=10.1016/s0021-9258(18)41696-1;
RA Lamarche A.E., Abate M.I., Chan S.H., Trumpower B.L.;
RT "Isolation and characterization of COX12, the nuclear gene for a previously
RT unrecognized subunit of Saccharomyces cerevisiae cytochrome c oxidase.";
RL J. Biol. Chem. 267:22473-22480(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 PROTEIN SEQUENCE OF 2-20, 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
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 unsing 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}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30598554}; Intermembrane side
CC {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:30598554}.
CC Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1
CC machinery.
CC -!- DOMAIN: The Cx9C/Cx10C motifs are involved in the recognition by the
CC mitochondrial MIA40-ERV1 disulfide relay system and the subsequent
CC transfer of disulfide bonds by dithiol/disulfide exchange reactions to
CC the newly imported protein. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC {ECO:0000305}.
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DR EMBL; M98332; AAA34510.1; -; Genomic_DNA.
DR EMBL; Z73210; CAA97566.1; -; Genomic_DNA.
DR EMBL; AY557925; AAS56251.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09357.1; -; Genomic_DNA.
DR PIR; S31256; S31256.
DR RefSeq; NP_013139.1; NM_001181925.1.
DR PDB; 6GIQ; EM; 3.23 A; j=1-83.
DR PDB; 6HU9; EM; 3.35 A; j/v=2-83.
DR PDB; 6T0B; EM; 2.80 A; j/w=2-83.
DR PDB; 6T15; EM; 3.29 A; j=2-83.
DR PDB; 6YMX; EM; 3.17 A; j=6-83.
DR PDB; 6YMY; EM; 3.41 A; j=6-83.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; Q01519; -.
DR SMR; Q01519; -.
DR BioGRID; 31314; 299.
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-4520N; -.
DR IntAct; Q01519; 24.
DR STRING; 4932.YLR038C; -.
DR TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR iPTMnet; Q01519; -.
DR UCD-2DPAGE; Q01519; -.
DR MaxQB; Q01519; -.
DR PaxDb; Q01519; -.
DR PRIDE; Q01519; -.
DR EnsemblFungi; YLR038C_mRNA; YLR038C; YLR038C.
DR GeneID; 850727; -.
DR KEGG; sce:YLR038C; -.
DR SGD; S000004028; COX12.
DR VEuPathDB; FungiDB:YLR038C; -.
DR eggNOG; KOG3057; Eukaryota.
DR GeneTree; ENSGT00940000174930; -.
DR HOGENOM; CLU_133964_2_0_1; -.
DR InParanoid; Q01519; -.
DR OMA; CPNEWIA; -.
DR BioCyc; MetaCyc:YLR038C-MON; -.
DR BioCyc; YEAST:YLR038C-MON; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:Q01519; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q01519; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
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:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:SGD.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR Gene3D; 1.10.10.140; -; 1.
DR InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR PANTHER; PTHR11387; PTHR11387; 1.
DR Pfam; PF02297; COX6B; 1.
DR PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR SUPFAM; SSF47694; SSF47694; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1331057,
FT ECO:0000269|PubMed:1331058, ECO:0000269|PubMed:7851399"
FT CHAIN 2..83
FT /note="Cytochrome c oxidase subunit 12, mitochondrial"
FT /id="PRO_0000194925"
FT DOMAIN 24..67
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 27..37
FT /note="Cx9C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 48..59
FT /note="Cx10C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT DISULFID 27..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 37..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:6T0B"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:6T0B"
SQ SEQUENCE 83 AA; 9788 MW; 57A8FAD93756577E CRC64;
MADQENSPLH TVGFDARFPQ QNQTKHCWQS YVDYHKCVNM KGEDFAPCKV FWKTYNALCP
LDWIEKWDDQ REKGIFAGDI NSD
