ID   COX7_SCHPO              Reviewed;          59 AA.
AC   G2TRP5;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   02-SEP-2026, entry version 60.
DE   RecName: Full=Cytochrome c oxidase subunit 7;
GN   Name=cox7; ORFNames=SPBC2F12.17;
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).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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:P10174}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P10174}.
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:P10174}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P10174}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P10174}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 7 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CCD31364.1; -; Genomic_DNA.
DR   PDB; 8C8Q; EM; 3.36 A; G=1-59.
DR   PDB; 8Q1B; EM; 3.40 A; g=1-59.
DR   AlphaFoldDB; G2TRP5; -.
DR   EMDB; EMD-16491; -.
DR   EMDB; EMD-18062; -.
DR   SMR; G2TRP5; -.
DR   ComplexPortal; CPX-9641; Mitochondrial respiratory chain complex IV.
DR   FunCoup; G2TRP5; 67.
DR   STRING; 284812.G2TRP5; -.
DR   iPTMnet; G2TRP5; -.
DR   PaxDb; 284812-G2TRP5; -.
DR   PomBase; SPBC2F12.17; cox7.
DR   VEuPathDB; FungiDB:SPBC2F12.17; -.
DR   HOGENOM; CLU_2997749_0_0_1; -.
DR   InParanoid; G2TRP5; -.
DR   OMA; YPYYAAM; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:G2TRP5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; NAS:ComplexPortal.
DR   GO; GO:0045277; C:respiratory chain complex IV; IDA:PomBase.
DR   GO; GO:0045333; P:cellular respiration; NAS:ComplexPortal.
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   InterPro; IPR039297; COX7a.
DR   Pfam; PF02238; COX7a; 1.
DR   PDBsum; 8C8Q; -.
DR   PDBsum; 8Q1B; -.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..59
FT                   /note="Cytochrome c oxidase subunit 7"
FT                   /id="PRO_0000416680"
FT   TOPO_DOM        1..24
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P10174"
FT   TRANSMEM        25..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..59
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P10174"
FT   HELIX           5..11
FT                   /evidence="ECO:0007829|PDB:8C8Q"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:8C8Q"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:8C8Q"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:8C8Q"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:8C8Q"
FT   HELIX           31..52
FT                   /evidence="ECO:0007829|PDB:8C8Q"
SQ   SEQUENCE   59 AA;  6734 MW;  94DCEB158FA821E4 CRC64;
     MKNTIVQQQR FLQSIHKPTY LQRPGSFALV YPYYAVMAGL GLYSLYASGR VIFGKKDAF
//