ID   COX2_DANRE              Reviewed;         230 AA.
AC   Q9MIY7;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
GN   Name=mt-co2; Synonyms=coii, cox2, coxii, mtco2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX   PubMed=11691861; DOI=10.1101/gr.156801;
RA   Broughton R.E., Milam J.E., Roe B.A.;
RT   "The complete sequence of the zebrafish (Danio rerio) mitochondrial genome
RT   and evolutionary patterns in vertebrate mitochondrial DNA.";
RL   Genome Res. 11:1958-1967(2001).
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:P68530};
CC       Note=Binds a dinuclear copper A center per subunit.
CC       {ECO:0000250|UniProtKB:P68530};
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of 14 subunits. The complex is composed of
CC       a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC       the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC       COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC       are encoded in the nuclear genome. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC       III, CIII), resulting in different assemblies (supercomplex
CC       SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity).
CC       Found in a complex with TMEM177, COA6, COX18, COX20, SCO1 and SCO2.
CC       Interacts with TMEM177 in a COX20-dependent manner. Interacts with
CC       COX20. Interacts with COX16 (By similarity).
CC       {ECO:0000250|UniProtKB:P00403, ECO:0000250|UniProtKB:P68530}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P68530}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P68530}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AC024175; AAF74300.1; -; Genomic_DNA.
DR   RefSeq; NP_059334.1; NC_002333.2.
DR   AlphaFoldDB; Q9MIY7; -.
DR   SMR; Q9MIY7; -.
DR   STRING; 7955.ENSDARP00000087872; -.
DR   PaxDb; 7955-ENSDARP00000087872; -.
DR   GeneID; 140540; -.
DR   KEGG; dre:140540; -.
DR   AGR; ZFIN:ZDB-GENE-011205-15; -.
DR   CTD; 4513; -.
DR   ZFIN; ZDB-GENE-011205-15; mt-co2.
DR   eggNOG; KOG4767; Eukaryota.
DR   HOGENOM; CLU_036876_2_3_1; -.
DR   InParanoid; Q9MIY7; -.
DR   OMA; WSYEYTD; -.
DR   OrthoDB; 5390623at2759; -.
DR   PhylomeDB; Q9MIY7; -.
DR   TreeFam; TF344269; -.
DR   Reactome; R-DRE-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-DRE-611105; Respiratory electron transport.
DR   Reactome; R-DRE-9707564; Cytoprotection by HMOX1.
DR   PRO; PR:Q9MIY7; -.
DR   Proteomes; UP000000437; Mitochondrion MT.
DR   Bgee; ENSDARG00000063908; Expressed in pharyngeal gill and 22 other cell types or tissues.
DR   ExpressionAtlas; Q9MIY7; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 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   NCBIfam; TIGR02866; CoxB; 1.
DR   PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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..230
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000183520"
FT   TOPO_DOM        1..14
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   TRANSMEM        15..45
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   TOPO_DOM        46..59
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   TRANSMEM        60..87
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   TOPO_DOM        88..230
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         161
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         196
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         196
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         198
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with MT-CO1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         200
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         200
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         204
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         207
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
SQ   SEQUENCE   230 AA;  25985 MW;  91BC51E34D22DDC5 CRC64;
     MAHPAQLGFQ DAASPVMEEL LCFHDHALMI VFLISTLVLY IIIAMVSTKL TNKFILDSQE
     IEIVWTVLPA IILILIALPS LRILYLMDEI NDPHVTIKAV GHQWYWSYEY TDYENLEFDS
     YMVPTQDLTP GGFRLLETDH RMVVPKESPI RILVSAEDVL HSWAVPSLGI KMDAVPGRLN
     QTAFIVSRPG VFYGQCSEIC GANHSFMPIV VEAVPLEFFE NWSSAMLEDA
//