ID A0A0C4ZQV2_9TELE Unreviewed; 516 AA. AC A0A0C4ZQV2; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 02-NOV-2016, entry version 11. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=COI {ECO:0000313|EMBL:AJJ48725.1}; OS Cyprinus carpio 'Furong' x Carassius auratus red var. OG Mitochondrion {ECO:0000313|EMBL:AJJ48725.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprinidae hybrid sp.. OX NCBI_TaxID=1610701 {ECO:0000313|EMBL:AJJ48725.1}; RN [1] {ECO:0000313|EMBL:AJJ48725.1} RP NUCLEOTIDE SEQUENCE. RA Peng H.Z., Xiao T.Y.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AJJ48725.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25648921; RA Peng H., Liu Q., Xiao T.; RT "Inheritance of the complete mitochondrial genomes Cyprinus capio RT furong(female symbol) x Cyprinus carpio var.singguonensis(male RT symbol)."; RL Mitochondrial DNA 1-2:0-0(2015). 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; KP210473; AJJ48725.1; -; Genomic_DNA. DR RefSeq; YP_009122667.1; NC_026543.1. DR GeneID; 23630067; -. DR CTD; 4512; -. 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 Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR023616; 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:AJJ48725.1}; 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 15 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 261 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 268 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 327 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 412 436 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 473 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 511 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 516 AA; 56831 MW; 77296CA834C47529 CRC64; MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGSLLGD DQIYNVIVTA HAFVMIFFMV MPILIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTTIK MKPPAISQYQ TPLFVWSVLV TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG FGIISHVVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPMLW ALGFIFLFTV GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AAFVHWFPLL TGYTLHSTWT KIHFGVMFIG VNLTFFPQHF LGLAGMPRRY SDYPDAYALW NTVSSIGSLI SLVAVIMFLF ILWEAFAAKR EVLSVELTAT NVEWLHGCPP PYHTYEEPAF VQIQSN //