COX4_SCHPO
ID COX4_SCHPO Reviewed; 164 AA.
AC P79010;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c oxidase subunit 4, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide IV;
DE Flags: Precursor;
GN Name=cox4; ORFNames=SPAC1296.02;
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 [MRNA].
RA Kawamukai M.;
RT "S.pombe cox4 gene.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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:P04037}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04037}.
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:P04037}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04037}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04037}; Matrix side
CC {ECO:0000250|UniProtKB:P04037}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family.
CC {ECO:0000305}.
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DR EMBL; AB000399; BAA19097.1; -; mRNA.
DR EMBL; CU329670; CAB36508.1; -; Genomic_DNA.
DR PIR; T37563; T37563.
DR RefSeq; NP_593042.1; NM_001018441.2.
DR AlphaFoldDB; P79010; -.
DR SMR; P79010; -.
DR BioGRID; 279461; 3.
DR IntAct; P79010; 3.
DR MINT; P79010; -.
DR STRING; 4896.SPAC1296.02.1; -.
DR iPTMnet; P79010; -.
DR MaxQB; P79010; -.
DR PaxDb; P79010; -.
DR EnsemblFungi; SPAC1296.02.1; SPAC1296.02.1:pep; SPAC1296.02.
DR GeneID; 2543025; -.
DR KEGG; spo:SPAC1296.02; -.
DR PomBase; SPAC1296.02; cox4.
DR VEuPathDB; FungiDB:SPAC1296.02; -.
DR eggNOG; KOG3352; Eukaryota.
DR HOGENOM; CLU_091071_0_0_1; -.
DR InParanoid; P79010; -.
DR OMA; DSHDTIY; -.
DR PhylomeDB; P79010; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P79010; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS00848; COX5B_1; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 34..164
FT /note="Cytochrome c oxidase subunit 4, mitochondrial"
FT /id="PRO_0000006113"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04037"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
SQ SEQUENCE 164 AA; 18162 MW; 0FFEA62B4E5A39F5 CRC64;
MFMNSMLRVS RQRAAVRSTV SLYRGFVSAS IRRNEQNVVK AAAQELANAK EPSDLIGPGG
RDGEVPTDLE QATGLERYEL LSELSGRDAF DMKPLDASRK GTLTDPIMVT SLDPYRHIGC
TGSPSGSHNL IWMTVYKDKL RRCPECGSVY KLKFMGDPNA EHSH
