COX2_ARATH
ID COX2_ARATH Reviewed; 260 AA.
AC P93285;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
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; Synonyms=COXII; OrderedLocusNames=AtMg00160;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. C24;
RX PubMed=8988169; DOI=10.1038/ng0197-57;
RA Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT 366,924 nucleotides.";
RL Nat. Genet. 15:57-61(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RX PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA Giege P., Brennicke A.;
RT "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT ORFs.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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=9 {ECO:0000269|PubMed:10611383}, 24
CC {ECO:0000269|PubMed:10611383}, 85 {ECO:0000269|PubMed:10611383}, 93
CC {ECO:0000269|PubMed:10611383}, 127 {ECO:0000269|PubMed:10611383}, 159
CC {ECO:0000269|PubMed:10611383}, 186 {ECO:0000269|PubMed:10611383}, 194
CC {ECO:0000269|PubMed:10611383}, 233 {ECO:0000269|PubMed:10611383}, 241
CC {ECO:0000269|PubMed:10611383}, 248 {ECO:0000269|PubMed:10611383};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; Y08501; CAA69761.3; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_085487.1; NC_001284.2.
DR AlphaFoldDB; P93285; -.
DR SMR; P93285; -.
DR BioGRID; 7; 1.
DR STRING; 3702.ATMG00160.1; -.
DR PaxDb; P93285; -.
DR PeptideAtlas; P93285; -.
DR PRIDE; P93285; -.
DR Araport; ATMG00160; -.
DR eggNOG; KOG4767; Eukaryota.
DR InParanoid; P93285; -.
DR OrthoDB; 1432833at2759; -.
DR BioCyc; ARA:ATMG00160-MON; -.
DR BioCyc; MetaCyc:ATMG00160-MON; -.
DR PRO; PR:P93285; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P93285; baseline and differential.
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 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; -; 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 1: Evidence at protein level;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; RNA editing; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..260
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183502"
FT TOPO_DOM 1..41
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..86
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..260
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 187
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 222
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 222
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 224
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 226
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 226
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 230
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 233
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
SQ SEQUENCE 260 AA; 29674 MW; 7D2D75A093973985 CRC64;
MIVLKWLFFT ISPCDAAEPW QLGFQDAATP IMQGIIDLHH DIFFFLILIL VFVLWILVRA
LWHFHYKKNA IPQRIVHGTT IEILWTIFPS IILMFIAIPS FALLYSMDEV VVDPAITIKA
IGHQWYWTYE YSDYNSSDEQ SLTFDSYMIP EEDLELGQLR LLEVDNRVVV PAKTHLRIIV
TSADVLHSWA VPSLGVKCDA VPGRLNQISI LVQREGVYYG QCSEICGTNH AFMSIVVEAV
SRKDYGSWVS NQLIPQTGEA
