ID K4K2Z3_SALFO Unreviewed; 421 AA. AC K4K2Z3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 18-JAN-2017, entry version 23. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=CO1 {ECO:0000313|EMBL:AFU93385.1}; OS Salvelinus fontinalis (Brook trout) (Salmo fontinalis). OG Mitochondrion {ECO:0000313|EMBL:AFU93385.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; OC Salmoniformes; Salmonidae; Salmoninae; Salvelinus. OX NCBI_TaxID=8038 {ECO:0000313|EMBL:AFU93385.1}; RN [1] {ECO:0000313|EMBL:AFU93385.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=#89 {ECO:0000313|EMBL:AFU93384.1}, and #90 RC {ECO:0000313|EMBL:AFU93385.1}; RX PubMed=23071608; DOI=10.1371/journal.pone.0046662; RA Crete-Lafreniere A., Weir L.K., Bernatchez L.; RT "Framing the salmonidae family phylogenetic portrait: a more complete RT picture from increased taxon sampling."; RL PLoS ONE 7:e46662-e46662(2012). 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. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. 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; JX960958; AFU93384.1; -; Genomic_DNA. DR EMBL; JX960959; AFU93385.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AFU93385.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 285 308 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 320 341 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 361 382 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 413 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 421 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFU93385.1}. FT NON_TER 421 421 {ECO:0000313|EMBL:AFU93385.1}. SQ SEQUENCE 421 AA; 46048 MW; DD407E029C55AAEE CRC64; YLVFGAWAGM VGTALSLLIR AELSQPGALL GDDQIYNVIV TAHAFVMIFF MVMPIMIGGF GNWLIPLMIG APDMAFPRMN NMSFWLLPPS FLLLLASSGV EAGAGTGWTV YPPLAGNLAH AGASVDLTIF SLHLAGISSI LGAINFITTI INMKPPAISQ YQTPLFVWAV LVTAVLLLLS LPVLAAGITM LLTDRNLNTT FFDPAGGGDP ILYQHLFWFF GHPEVYILIL PGFGMISHIV AYYSGKKEPF GYMGMVWAMM AIGLLGFIVW AHHMFTVGMD VDTRAYFTSA TMIIAIPTGV KVFSWLATLH GGSIKWETPL LWALGFIFLF TVGGLTGIVL ANSSLDIVLH DTYYVVAHFH YVLSMGAVFA IMGAFVHWFP LFTGYTLHST WTKIHFGIMF IGVNLTFFPQ HFLGLAGMPR R //