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COX2_STRCA
ID   COX2_STRCA              Reviewed;         229 AA.
AC   O21400; O03894;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
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, COXII, MTCO2;
OS   Struthio camelus (Common ostrich).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9214748; DOI=10.1093/oxfordjournals.molbev.a025815;
RA   Harlid A., Janke A., Arnason U.;
RT   "The mtDNA sequence of the ostrich and the divergence between paleognathous
RT   and neognathous birds.";
RL   Mol. Biol. Evol. 14:754-761(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sorenson M.D., Dimcheff D.E., Ast J.C., Yuri T., Mindell D.P.;
RT   "Primers for a PCR-based approach to complete mitochondrial genome
RT   sequencing.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11370967; DOI=10.1098/rspb.2001.1587;
RA   Haddrath O., Baker A.J.;
RT   "Complete mitochondrial DNA genome sequences of extinct birds: ratite
RT   phylogenetics and the vicariance biogeography hypothesis.";
RL   Proc. R. Soc. B 268:939-945(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-229.
RA   Lee K., Feinstein J., Cracraft J.;
RT   "Phylogenetic relationships of the ratite birds: resolving conflicts
RT   between molecular and morphological data sets.";
RL   (In) Mindell D.P. (eds.);
RL   Avian molecular evolution and systematics, pp.1-1, Academic Press, New York
RL   (1997).
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; Y12025; CAA72747.1; -; Genomic_DNA.
DR   EMBL; AF069429; AAD09386.1; -; Genomic_DNA.
DR   EMBL; AF338715; AAK53348.1; -; Genomic_DNA.
DR   EMBL; U76069; AAB61329.1; ALT_TERM; Genomic_DNA.
DR   PIR; D90612; D90612.
DR   PIR; T12412; T12412.
DR   RefSeq; NP_115444.1; NC_002785.1.
DR   AlphaFoldDB; O21400; -.
DR   SMR; O21400; -.
DR   GeneID; 803280; -.
DR   CTD; 4513; -.
DR   OrthoDB; 1432833at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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; Respiratory chain;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..229
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000183696"
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..58
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   TRANSMEM        59..86
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   TOPO_DOM        87..229
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         160
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         195
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         195
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         197
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         197
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         199
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         199
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         203
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
FT   BINDING         206
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P68530"
SQ   SEQUENCE   229 AA;  25700 MW;  B9377617BACB14EF CRC64;
     MANPSQFGFQ DASSPIMEEL VEFHDHALMV ALAICSLVLY LLALMLVEKL SSNTVDAQEV
     ELIWTILPAI VLILLALPSL QILYMMDEID EPDLTLKAIG HQWYWSYEYT DFKDLTFDSY
     MIPTSELPPG HFRLLEVDHR VVVPMESPIR VIITAGDVLH SWAVPTLGVK TDAIPGRLNQ
     TSFITTRPGI FYGQCSEICG ANHSYMPIVV ESTPLTYFES WSSLLSTDS
 
 
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