ID   COX13_SCHPO             Reviewed;         130 AA.
AC   O74471;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Cytochrome c oxidase subunit 13, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIa;
DE   Flags: Precursor;
GN   Name=cox13; ORFNames=SPCC1739.09c;
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 unsing 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P32799}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P32799}.
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:P32799}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P32799}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P32799}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA20783.1; -; Genomic_DNA.
DR   PIR; T41117; T41117.
DR   RefSeq; NP_588417.1; NM_001023408.2.
DR   AlphaFoldDB; O74471; -.
DR   SMR; O74471; -.
DR   STRING; 4896.SPCC1739.09c.1; -.
DR   MaxQB; O74471; -.
DR   PaxDb; O74471; -.
DR   EnsemblFungi; SPCC1739.09c.1; SPCC1739.09c.1:pep; SPCC1739.09c.
DR   GeneID; 2538807; -.
DR   KEGG; spo:SPCC1739.09c; -.
DR   PomBase; SPCC1739.09c; cox13.
DR   VEuPathDB; FungiDB:SPCC1739.09c; -.
DR   eggNOG; KOG3469; Eukaryota.
DR   HOGENOM; CLU_122515_0_1_1; -.
DR   InParanoid; O74471; -.
DR   OMA; WRKLSLY; -.
DR   PhylomeDB; O74471; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:O74471; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:PomBase.
DR   CDD; cd00925; Cyt_c_Oxidase_VIa; 1.
DR   Gene3D; 4.10.95.10; -; 1.
DR   InterPro; IPR001349; Cyt_c_oxidase_su6a.
DR   InterPro; IPR018507; Cyt_c_oxidase_su6a_CS.
DR   InterPro; IPR036418; Cyt_c_oxidase_su6a_sf.
DR   PANTHER; PTHR11504; PTHR11504; 1.
DR   Pfam; PF02046; COX6A; 1.
DR   PIRSF; PIRSF000277; COX6A1; 1.
DR   SUPFAM; SSF81411; SSF81411; 1.
DR   PROSITE; PS01329; COX6A; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..130
FT                   /note="Cytochrome c oxidase subunit 13, mitochondrial"
FT                   /id="PRO_0000006126"
FT   TOPO_DOM        32..61
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        62..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..130
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   130 AA;  15199 MW;  95127039255F3293 CRC64;
     MSMMNRNIGF LSRTLKTSVP KRAGLLSFRA YSNEAKVNWL EEVQAEEEHA KRSSEFWKKV
     TYYIGGPALI LASANAYYIY CKHQEHAKHV EDTDPGYSFE NLRFKKYPWG DGSKTLFWND
     KVNHLKKDDE