ID Q6VHV2_HUMAN Unreviewed; 513 AA. AC Q6VHV2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 03-MAR-2009, entry version 37. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; GN Name=COX1; OS Homo sapiens (Human). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F164; RX MEDLINE=21313109; PubMed=11349229; DOI=10.1086/320591; 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. RC STRAIN=F164; 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). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F164; RA Moilanen J.S., Finnila S., Lehtonen M.S., Majamaa K.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=39_M1a5; RX PubMed=17170302; DOI=10.1126/science.1135566; RA Olivieri A., Achilli A., Pala M., Battaglia V., Fornarino S., RA Al-Zahery N., Scozzari R., Cruciani F., Behar D.M., Dugoujon J.M., RA Coudray C., Santachiara-Benerecetti A.S., Semino O., Bandelt H.J., RA Torroni A.; RT "The mtDNA legacy of the Levantine early Upper Palaeolithic in RT Africa."; RL Science 314:1767-1770(2006). RN [5] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Am012, and AM038; RX PubMed=18359946; DOI=10.1093/molbev/msn068; RA Soares P., Trejaut J.A., Loo J.H., Hill C., Mormina M., Lee C.L., RA Chen Y.M., Hudjashov G., Forster P., Macaulay V., Bulbeck D., RA Oppenheimer S., Lin M., Richards M.B.; RT "Climate change and postglacial human dispersals in southeast Asia."; RL Mol. Biol. Evol. 25:1209-1218(2008). RN [6] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MTDNA361; RX MEDLINE=21947462; PubMed=11938495; DOI=10.1086/339933; RA Herrnstadt C., Elson J.L., Fahy E., Preston G., Turnbull D.M., RA Anderson C., Ghosh S.S., Olefsky J.M., Beal M.F., Davis R.E., RA Howell N.; RT "Reduced-median-network analysis of complete mitochondrial DNA coding- RT region sequences for the major African, Asian, and European RT haplogroups."; RL Am. J. Hum. Genet. 70:1152-1171(2002). RN [7] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MTDNA361; RA Herrnstadt C., Fahy E., Preston G., Anderson C., Ghosh S.S., RA Davis R.E., Howell N.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MTDNA361; RG HmtDB; RL Submitted (JUN-2007) 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. 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 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (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 EMBL; EF060350; ABJ89449.1; -; Genomic_DNA. DR EMBL; EF093535; ABL61582.1; -; Genomic_DNA. DR EMBL; EF093536; ABL61595.1; -; Genomic_DNA. DR EMBL; EF657522; ABR96749.1; -; Genomic_DNA. DR IPI; IPI00464968; -. DR HSSP; P98002; 1AR1. DR SMR; Q6VHV2; 1-511. DR Ensembl; ENSG00000198804; Homo sapiens. DR HOVERGEN; Q6VHV2; -. DR GO; GO:0016021; C:integral to membrane; IEA:InterPro. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 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 InterPro; IPR000883; Cyt_c_oxidase_su1. DR Gene3D; G3DSA:1.20.210.10; COX1; 1. 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. PE 3: Inferred from homology; KW Copper; Electron transport; Heme; Membrane; Mitochondrion; KW Oxidoreductase; Respiratory chain; Transmembrane; 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 //