ID   COX5_SCHPO              Reviewed;         186 AA.
AC   O74988;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Cytochrome c oxidase polypeptide 5, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide V;
DE   Flags: Precursor;
GN   Name=cox5; ORFNames=SPCC338.10c;
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   REVISION OF GENE MODEL.
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).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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:P00424}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00424}.
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       seevral 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:P00424}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00424}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA19341.2; -; Genomic_DNA.
DR   PIR; T41733; T41733.
DR   RefSeq; NP_588158.2; NM_001023147.2.
DR   PDB; 8C8Q; EM; 3.36 A; E=1-186.
DR   PDB; 8Q1B; EM; 3.40 A; e=1-186.
DR   PDBsum; 8C8Q; -.
DR   PDBsum; 8Q1B; -.
DR   AlphaFoldDB; O74988; -.
DR   EMDB; EMD-18062; -.
DR   SMR; O74988; -.
DR   BioGRID; 275442; 2.
DR   STRING; 284812.O74988; -.
DR   iPTMnet; O74988; -.
DR   MaxQB; O74988; -.
DR   PaxDb; 4896-SPCC338-10c-1; -.
DR   EnsemblFungi; SPCC338.10c.1; SPCC338.10c.1:pep; SPCC338.10c.
DR   GeneID; 2538862; -.
DR   KEGG; spo:SPCC338.10c; -.
DR   PomBase; SPCC338.10c; cox5.
DR   VEuPathDB; FungiDB:SPCC338.10c; -.
DR   eggNOG; KOG4075; Eukaryota.
DR   HOGENOM; CLU_070101_2_0_1; -.
DR   InParanoid; O74988; -.
DR   OMA; WYISYGA; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:O74988; -.
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; cd00922; Cyt_c_Oxidase_IV; 1.
DR   Gene3D; 1.10.442.10; Cytochrome c oxidase subunit IV; 1.
DR   InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR   InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR   PANTHER; PTHR10707:SF10; CYTOCHROME C OXIDASE SUBUNIT 4; 1.
DR   PANTHER; PTHR10707; CYTOCHROME C OXIDASE SUBUNIT IV; 1.
DR   Pfam; PF02936; COX4; 1.
DR   SUPFAM; SSF81406; Mitochondrial cytochrome c oxidase subunit IV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..186
FT                   /note="Cytochrome c oxidase polypeptide 5, mitochondrial"
FT                   /id="PRO_0000006096"
FT   TOPO_DOM        21..107
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00424"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..186
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00424"
FT   REGION          149..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   186 AA;  20735 MW;  19202F28597BE9CC CRC64;
     MYLSKIICKK VPMKLLCTRN AATVSAAATN ALQKEQPSGE AMIARPRLVD LDKRWGIMSQ
     EEKDGLITDL YARQKQPWTT LSIEEKKAAY WIAFGEHGPR AFSHISQKTV FWGTVAGLTI
     GVVLFGLIRT QAAPSPRTMT REWQEKSNEY MKENKINPIS GEASEGFKGR GQISGGIFSP
     SEKDKK
//