ID Q6VHV2_HUMAN PRELIMINARY; PRT; 513 AA. AC Q6VHV2; DT 05-JUL-2004 (TrEMBLrel. 27, Created) DT 05-JUL-2004 (TrEMBLrel. 27, Last sequence update) DT 05-JUL-2004 (TrEMBLrel. 27, Last annotation update) DE Cytochrome c oxidase subunit I. GN Name=COX1; OS Homo sapiens (Human). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21313109; PubMed=11349229; RA Finnila S., Lehtonen M.S., Majamaa K.; RT "Phylogenetic network for European mtDNA."; RL Am. J. Hum. Genet. 68:1475-1484(2001). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=12949126; DOI=10.1093/molbev/msg230; RA Moilanen J.S., Finnila S., Majamaa K.; RT "Lineage-specific selection in human mtDNA: lack of polymorphisms in a RT segment of MTND5 gene in haplogroup J."; RL Mol. Biol. Evol. 20:2132-2142(2003). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O. CC -!- PATHWAY: Respiratory chain; terminal step. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial CC inner membrane (By similarity). CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. 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; AY339565; AAP91157.1; -; Genomic_DNA. DR HSSP; P98002; 1AR1. DR SMR; Q6VHV2; 1-511. DR GO; GO:0016020; C:membrane; IEA. DR GO; GO:0005739; C:mitochondrion; IEA. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA. DR GO; GO:0006118; P:electron transport; IEA. DR InterPro; IPR000883; COX1. DR PANTHER; PTHR10422; COX1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. KW Copper; Electron transport; Heme; Inner membrane; Membrane; KW Mitochondrion; Oxidoreductase; Respiratory chain; Transmembrane; KW Transport. SQ SEQUENCE 513 AA; 57053 MW; D08B485E89A3A1F1 CRC64; MFADRWLFST NHKDIGTLYL LFGAWAGVLG TALSLLIRAE LGQPGNLLGN DHIYNVIVTA HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSLL LLLASAMVEA GAGTGWTVYP PLAGNYSHPG ASVDLIIFSL HLAGVSSILG AINFITTIIN MKPPAMTQYQ TPLFVWSVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGS NMKWSAAVLW ALGFIFLFTV GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF SGYTLDQTYA KIHFTIMFIG VNLTFFPQHF LGLSGMPRRY SDYPDAYTTW NILSSVGSFI SLTAVMLMIF MIWEAFASKR KVLMVEEPSM NLEWLYGCPP PYHTFEEPVY MKS //