ID   COX9_SCHPO              Reviewed;          58 AA.
AC   O94705;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Cytochrome c oxidase subunit 9, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIIA;
DE   Flags: Precursor;
GN   Name=cox9; ORFNames=SPCC1259.05c;
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:P07255}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P07255}.
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:P07255}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P07255}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P07255}.
CC   -!- SIMILARITY: Belongs to the fungal cytochrome c oxidase subunit 7a
CC       family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22543.1; -; Genomic_DNA.
DR   PIR; T40894; T40894.
DR   RefSeq; NP_588061.1; NM_001023053.2.
DR   PDB; 8C8Q; EM; 3.36 A; I=1-58.
DR   PDB; 8Q1B; EM; 3.40 A; i=1-58.
DR   PDBsum; 8C8Q; -.
DR   PDBsum; 8Q1B; -.
DR   AlphaFoldDB; O94705; -.
DR   EMDB; EMD-18062; -.
DR   SMR; O94705; -.
DR   STRING; 284812.O94705; -.
DR   MaxQB; O94705; -.
DR   PaxDb; 4896-SPCC1259-05c-1; -.
DR   EnsemblFungi; SPCC1259.05c.1; SPCC1259.05c.1:pep; SPCC1259.05c.
DR   GeneID; 2539086; -.
DR   KEGG; spo:SPCC1259.05c; -.
DR   PomBase; SPCC1259.05c; cox9.
DR   VEuPathDB; FungiDB:SPCC1259.05c; -.
DR   HOGENOM; CLU_196969_0_0_1; -.
DR   InParanoid; O94705; -.
DR   OMA; ASYWWWG; -.
DR   PhylomeDB; O94705; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:O94705; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:PomBase.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR   CDD; cd22888; CcO_VIIa_fungal; 1.
DR   InterPro; IPR014368; Cyt_c_oxidase_su7a_fun.
DR   PANTHER; PTHR28264:SF1; CYTOCHROME C OXIDASE SUBUNIT 6C; 1.
DR   PANTHER; PTHR28264; CYTOCHROME C OXIDASE SUBUNIT 7A; 1.
DR   PIRSF; PIRSF000283; COX9; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..55
FT                   /note="Cytochrome c oxidase subunit 9, mitochondrial"
FT                   /id="PRO_0000041771"
FT   PROPEP          56..58
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P07255"
FT                   /id="PRO_0000041772"
FT   TOPO_DOM        1..14
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P07255"
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..55
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P07255"
SQ   SEQUENCE   58 AA;  6644 MW;  290BA466677C8AD7 CRC64;
     MAVGPVTGMF KRRIVTDFSV TMILGTLGAC YWWFGYHKPA ARQREEFYVK LAAEKNAE
//