ID A0A0N7AR72_ONCCL Unreviewed; 230 AA. AC A0A0N7AR72; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 17-FEB-2016, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457}; 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; OC Salmoniformes; 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 RT PCR amplification and whole mitochondrial genome assembly using next- RT generation 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- CC 3 form the functional core of the enzyme complex. Subunit 2 CC transfers the electrons from cytochrome c via its binuclear copper CC A center to the bimetallic center of the catalytic subunit 1 (By CC similarity). {ECO:0000256|SAAS:SAAS00235091}. 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:SAAS00400050}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000457, CC ECO:0000256|SAAS:SAAS00400050}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|RuleBase:RU000457}. 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 Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR014222; Cyt_c_oxidase_su2. DR InterPro; IPR002429; Cyt_c_oxidase_su2_C. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. 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:SAAS00515163}; KW Electron transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00517827}; KW Membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00517788, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00515158}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00278823, ECO:0000313|EMBL:AJW75497.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00278827}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00439018}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00470865, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00470972, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00517787}. FT TRANSMEM 27 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 85 Helical. {ECO:0000256|SAM:Phobius}. 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 //