ID A0A0N7AR72_ONCCL Unreviewed; 230 AA. AC A0A0N7AR72; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 11-DEC-2019, entry version 22. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709560}; GN Name=COII {ECO:0000313|EMBL:AJW75497.1}; OS Oncorhynchus clarkii stomias (greenback cutthroat trout). OG Mitochondrion {ECO:0000313|EMBL:AJW75497.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=453929 {ECO:0000313|EMBL:AJW75497.1}; RN [1] {ECO:0000313|EMBL:AJW75497.1} RP NUCLEOTIDE SEQUENCE. RA Renshaw M.A., Olds B.P., Li Y., Pfrender M.E., Lodge D.M.; RT "Introduction of universal fish and amphibian primers for long-range PCR RT amplification and whole mitochondrial genome assembly using next-generation RT sequencing techniques."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. Subunit 2 transfers the CC electrons from cytochrome c via its binuclear copper A center to the CC bimetallic center of the catalytic subunit 1. CC {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709549}. CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709542}; Multi- CC pass membrane protein {ECO:0000256|RuleBase:RU000457, CC ECO:0000256|SAAS:SAAS00709542}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709553}. 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; KP013107; AJW75497.1; -; Genomic_DNA. DR EMBL; KP013117; AJW75627.1; -; Genomic_DNA. 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:InterPro. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. 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 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 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00477878}; KW Electron transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS01155864}; KW Membrane {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00883094, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00119299}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709499, ECO:0000313|EMBL:AJW75497.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709564}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS01154861}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00883111, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS01155879}. FT TRANSMEM 27..51 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 63..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..91 FT /note="COX2_TM" FT /evidence="ECO:0000259|PROSITE:PS50999" FT DOMAIN 92..225 FT /note="COX2_CUA" FT /evidence="ECO:0000259|PROSITE:PS50857" SQ SEQUENCE 230 AA; 26026 MW; 97D6B80F72127F91 CRC64; MAHPSQLGFQ DAASPVMEEL LHFHDHALMI VLLISTLVLY IIVAMVSTKL TNKYILDSQE IEIVWTVLPA VILILIALPS LRILYLMDEI NDPHLTIKAM GHQWYWSYEY TDYEDLGFDS YMVPTQDLVP GQFRLLETDH RMVVPVESPI RVLVSAEDVL HSWAVPSLGV KMDAVPGRLN QTAFIASRPG VFYGQCSEIC GANHSFMPIV VEAVPLEHFE KWSTMMLEDA //