COX2_LEITA
ID COX2_LEITA Reviewed; 210 AA.
AC P14545;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
OS Leishmania tarentolae (Sauroleishmania tarentolae).
OG Mitochondrion.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC lizard Leishmania.
OX NCBI_TaxID=5689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6096360; DOI=10.1016/s0021-9258(17)42525-7;
RA de la Cruz V.F., Neckelmann N., Simpson L.;
RT "Sequences of six genes and several open reading frames in the kinetoplast
RT maxicircle DNA of Leishmania tarentolae.";
RL J. Biol. Chem. 259:15136-15147(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2994021; DOI=10.1093/nar/13.16.5977;
RA Simpson A.M., Necklemann N., la Cruz V.F., Muhich M.L., Simpson L.;
RT "Mapping and 5' end determination of kinetoplast maxicircle gene
RT transcripts from Leishmania tarentolae.";
RL Nucleic Acids Res. 13:5977-5993(1985).
RN [3]
RP RNA EDITING.
RX PubMed=2548203; DOI=10.1073/pnas.86.16.6220;
RA Shaw J., Campbell D., Simpson L.;
RT "Internal frameshifts within the mitochondrial genes for cytochrome oxidase
RT subunit II and maxicircle unidentified reading frame 3 of Leishmania
RT tarentolae are corrected by RNA editing: evidence for translation of the
RT edited cytochrome oxidase subunit II mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6220-6224(1989).
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 -!- RNA EDITING: Modified_positions=Not_applicable; Note=Some positions are
CC modified by RNA editing via nucleotide insertion.
CC {ECO:0000269|PubMed:2548203};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; L07544; AAA31876.1; -; mRNA.
DR EMBL; M10126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; I22848; I22848.
DR AlphaFoldDB; P14545; -.
DR SMR; P14545; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
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; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
PE 2: Evidence at transcript level;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW RNA editing; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..210
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183616"
FT TOPO_DOM 1..20
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..60
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..210
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 157
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 192
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 192
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 194
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 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
SQ SEQUENCE 210 AA; 23977 MW; B3A0544E258047C2 CRC64;
MAFILSFWMI FLLDSVIVLL SFVCFVCVWI CALLFSTVLL VSKLNNIYCT WDFTASKFID
VYWFTIGGMF SLGLLLRLCL LLYFGHLNFV SFDLCKVVGF QWYWVYFIFG ETTIFSNLIL
ESDYMIGDLR LLQCNHVLTL LSLVIYKLWL SAVDVIHSFA ISSLGVKVDC IPGRCNEIVL
FSSNNATVYG QCSELCGVLH GFMPIVICFI
