ID COX2_ARATH Reviewed; 260 AA. AC P93285; A0A2P2CLF0; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2023, sequence version 3. DT 04-NOV-2026, entry version 160. 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 [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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING. RC STRAIN=cv. Columbia; RX PubMed=29519893; DOI=10.1105/tpc.18.00024; RA Sloan D.B., Wu Z., Sharbrough J.; RT "Correction of persistent errors in Arabidopsis reference mitochondrial RT genomes."; RL Plant Cell 30:525-527(2018). RN [4] 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] + O2 + 8 H(+)(in) = 4 Fe(III)- CC [cytochrome c] + 2 H2O + 4 H(+)(out); 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, CC ECO:0000269|PubMed:29519893}, 24 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 85 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 93 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 127 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 159 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 186 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 194 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 233 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 241 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}, 248 {ECO:0000269|PubMed:10611383, CC ECO:0000269|PubMed:29519893}; CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y08501; CAA69761.3; ALT_SEQ; Genomic_DNA. DR EMBL; BK010421; DAB41495.2; -; Genomic_DNA. DR RefSeq; YP_009472098.2; NC_037304.1. DR AlphaFoldDB; P93285; -. DR SMR; P93285; -. DR BioGRID; 7; 1. DR FunCoup; P93285; 156. DR STRING; 3702.A0A2P2CLF0; -. DR PaxDb; 3702-A0A2P2CLF0; -. DR GeneID; 36335641; -. DR KEGG; ath:DA397_mgp01; -. DR Araport; ATMG00160; -. DR TAIR; ATMG00160; COX2. DR eggNOG; KOG4767; Eukaryota. DR InParanoid; P93285; -. DR OMA; AAGFNWW; -. DR BioCyc; ARA:ATMG00160-MONOMER; -. DR BioCyc; MetaCyc:ATMG00160-MONOMER; -. DR CD-CODE; 4299E36E; Nucleolus. DR PRO; PR:P93285; -. DR Proteomes; UP001984100; Mitochondrion. DR GO; GO:0009507; C:chloroplast; ISM:TAIR. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HDA:TAIR. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0045277; C:respiratory chain complex IV; IBA:GO_Central. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISS:UniProtKB. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central. DR CDD; cd13912; CcO_II_C; 1. DR FunFam; 1.10.287.90:FF:000004; Cytochrome c oxidase subunit 2; 1. DR FunFam; 2.60.40.420:FF:000001; Cytochrome c oxidase subunit 2; 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 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" FT CONFLICT 234 FT /note="P -> S (in Ref. 2; CAA69761)" FT /evidence="ECO:0000305" SQ SEQUENCE 260 AA; 29685 MW; 7D2D7690A0973985 CRC64; MIVLKWLFFT ISPCDAAEPW QLGFQDAATP IMQGIIDLHH DIFFFLILIL VFVLWILVRA LWHFHYKKNA IPQRIVHGTT IEILWTIFPS IILMFIAIPS FALLYSMDEV VVDPAITIKA IGHQWYWTYE YSDYNSSDEQ SLTFDSYMIP EEDLELGQLR LLEVDNRVVV PAKTHLRIIV TSADVLHSWA VPSLGVKCDA VPGRLNQISI LVQREGVYYG QCSEICGTNH AFMPIVVEAV SRKDYGSWVS NQLIPQTGEA //