ID   COX12_SCHPO             Reviewed;          86 AA.
AC   O94581;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Cytochrome c oxidase subunit 12, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIb;
GN   Name=cox12; ORFNames=SPCC1442.08c;
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:Q01519}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:Q01519}.
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:Q01519}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q01519}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q01519}; Intermembrane side
CC       {ECO:0000250|UniProtKB:Q01519}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA21442.2; -; Genomic_DNA.
DR   PIR; T40973; T40973.
DR   RefSeq; NP_588322.2; NM_001023313.3.
DR   AlphaFoldDB; O94581; -.
DR   SMR; O94581; -.
DR   BioGRID; 275416; 1.
DR   STRING; 4896.SPCC1442.08c.1; -.
DR   MaxQB; O94581; -.
DR   PaxDb; O94581; -.
DR   EnsemblFungi; SPCC1442.08c.1; SPCC1442.08c.1:pep; SPCC1442.08c.
DR   GeneID; 2538835; -.
DR   KEGG; spo:SPCC1442.08c; -.
DR   PomBase; SPCC1442.08c; cox12.
DR   VEuPathDB; FungiDB:SPCC1442.08c; -.
DR   eggNOG; KOG3057; Eukaryota.
DR   HOGENOM; CLU_133964_2_0_1; -.
DR   InParanoid; O94581; -.
DR   OMA; CPNEWIA; -.
DR   PhylomeDB; O94581; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:O94581; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:PomBase.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IC:PomBase.
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   Pfam; PF02297; COX6B; 1.
DR   PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR   SUPFAM; SSF47694; SSF47694; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome.
FT   CHAIN           1..86
FT                   /note="Cytochrome c oxidase subunit 12, mitochondrial"
FT                   /id="PRO_0000194924"
FT   DOMAIN          30..73
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           33..43
FT                   /note="Cx9C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           54..65
FT                   /note="Cx10C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        33..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        43..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   86 AA;  10264 MW;  1B99721A199A4657 CRC64;
     MSEQEDQEAP KQFTFGTVGF DARFPNTNQT KHCFQSYIDY FRCIKAKGED FVPCKQFWHA
     YQSLCPMEWV ERWDEQRENG TFPAPI