COX6_SCHPO
ID COX6_SCHPO Reviewed; 140 AA.
AC Q9UTF6;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Cytochrome c oxidase subunit 6, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VI;
DE Flags: Precursor;
GN Name=cox6; ORFNames=SPAC1B2.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00427}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00427}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00427}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00427}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00427}; Matrix side
CC {ECO:0000250|UniProtKB:P00427}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB61471.1; -; Genomic_DNA.
DR PIR; T50140; T50140.
DR RefSeq; NP_593931.1; NM_001019360.2.
DR AlphaFoldDB; Q9UTF6; -.
DR SMR; Q9UTF6; -.
DR BioGRID; 278952; 4.
DR STRING; 4896.SPAC1B2.04.1; -.
DR MaxQB; Q9UTF6; -.
DR PaxDb; Q9UTF6; -.
DR EnsemblFungi; SPAC1B2.04.1; SPAC1B2.04.1:pep; SPAC1B2.04.
DR GeneID; 2542493; -.
DR KEGG; spo:SPAC1B2.04; -.
DR PomBase; SPAC1B2.04; cox6.
DR VEuPathDB; FungiDB:SPAC1B2.04; -.
DR eggNOG; KOG4077; Eukaryota.
DR HOGENOM; CLU_099086_0_1_1; -.
DR InParanoid; Q9UTF6; -.
DR OMA; DPHHEES; -.
DR PhylomeDB; Q9UTF6; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:Q9UTF6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:PomBase.
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 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..140
FT /note="Cytochrome c oxidase subunit 6, mitochondrial"
FT /id="PRO_0000006107"
SQ SEQUENCE 140 AA; 15938 MW; CA04C3CEF41DB867 CRC64;
MKAVQRIFQT GRFSVAAGPS VRFQAGFLAA NRQVRFSSNH GVSLEEINTK YNDFFSNVQD
QFELQRGLNN CFAYDIVPSS DVIEQALRAA RRVNDFPTAV RIFEGIKVKL PTKEQYQAYV
KELKPVCNEL GIVLKEDLFK
