COX2_SCHPO
ID COX2_SCHPO Reviewed; 248 AA.
AC P21534; Q9T653;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 4.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=cox2; ORFNames=SPMIT.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EF2;
RX PubMed=9651494; DOI=10.1016/s0378-1119(98)00204-2;
RA Schaefer B., Kaulich K., Wolf K.;
RT "Mosaic structure of the cox2 gene in the petite negative yeast
RT Schizosaccharomyces pombe: a group II intron is inserted at the same
RT location as the otherwise unrelated group II introns in the mitochondria of
RT higher plants.";
RL Gene 214:101-112(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD7-50;
RA Lang B.F.;
RT "The mitochondrial genome of Schizosaccharomyces pombe.";
RL (In) O'Brien S.J. (eds.);
RL Genetic Maps (6th edition), pp.3118-3119, Cold Spring Harbor Laboratory
RL Press, New York (1993).
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:P00410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC Note=Binds a dinuclear copper A center per subunit.
CC {ECO:0000250|UniProtKB:P00410};
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:P00410}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00410}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; AJ251293; CAB61572.1; -; Genomic_DNA.
DR EMBL; X54421; CAA38293.1; -; Genomic_DNA.
DR RefSeq; NP_039508.1; NC_001326.1.
DR AlphaFoldDB; P21534; -.
DR SMR; P21534; -.
DR STRING; 4896.SPMIT.11.1; -.
DR iPTMnet; P21534; -.
DR PaxDb; P21534; -.
DR GeneID; 1669525; -.
DR KEGG; spo:ScpofMp10; -.
DR PomBase; SPMIT.11; cox2.
DR eggNOG; KOG4767; Eukaryota.
DR HOGENOM; CLU_036876_2_3_1; -.
DR InParanoid; P21534; -.
DR PhylomeDB; P21534; -.
DR PRO; PR:P21534; -.
DR Proteomes; UP000002485; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:PomBase.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:PomBase.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:PomBase.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IMP:PomBase.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IMP:PomBase.
DR CDD; cd13912; CcO_II_C; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR034210; CcO_II_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 3: Inferred from homology;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..248
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183686"
FT TOPO_DOM 1..36
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..75
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..248
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 219
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 221
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 221
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 225
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 228
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT CONFLICT 123
FT /note="T -> S (in Ref. 1; CAA38293)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="G -> S (in Ref. 1; CAA38293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28121 MW; 033A029DBB967871 CRC64;
MLFFNSILND APSSWALYFQ DGASPSYLGV THLNDYLMFY LTFIFIGVIY AICKAVIEYN
YNSHPIAAKY TTHGSIVEFI WTLIPALILI LVALPSFKLL YLLDEVQKPS MTVKAIGRQW
FWTYELNDFV TNENEPVSFD SYMVPEEDLE EGSLRQLEVD NRLVLPIDTR IRLILTSGDV
IHSWAVPSLG IKCDCIPGRL NQVSLSIDRE GLFYGQCSEL CGVLHSSMPI VVQGVSLEDF
LAWLEENS
