ID COX2_LYCSM Reviewed; 228 AA. AC O79549; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 13-SEP-2023, entry version 114. 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 Lycodon semicarinatus (Ryukyu odd-tooth snake) (Eumesodon semicarinatus). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Colubridae; Colubrinae; Lycodon. OX NCBI_TaxID=56549; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=9725849; DOI=10.1093/genetics/150.1.313; RA Kumazawa Y., Ota H., Nishida M., Ozawa T.; RT "The complete nucleotide sequence of a snake (Dinodon semicarinatus) RT mitochondrial genome with two identical control regions."; RL Genetics 150:313-329(1998). 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}. 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; AB008539; BAA33025.1; -; Genomic_DNA. DR PIR; T11091; T11091. DR RefSeq; NP_008422.1; NC_001945.1. DR AlphaFoldDB; O79549; -. DR SMR; O79549; -. DR GeneID; 808270; -. DR CTD; 4513; -. 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; 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; Respiratory chain; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..228 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000183571" 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..228 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 162 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 197 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" 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 199 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 199 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 201 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 201 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 205 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 208 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" SQ SEQUENCE 228 AA; 25648 MW; 61BD618481EFDDB4 CRC64; MPHASQLSLQ EAMGPTMEEV IFLHDHVLLL TCLMTMVITM FTLTATTTAL THNDPTEEVE QLEAAWTVAP IMILILTALP SVRSLYLMEE VFNPYLTIKA TGHQWYWNYE YSDGVKISFD SYMIQTKDLQ NGSPRLLEVD HRMVMPAGLQ TRVVVTAEDV LHSWTIPSLG VKVDAVPGRL NQLPLATSRV GVFYGQCSEI CGANHSFMPI AMEATPLHHF EQWLISEQ //