ID C7BWV0_HOMNE Unreviewed; 513 AA. AC C7BWV0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-NOV-2018, entry version 46. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=COX1 {ECO:0000313|EMBL:CAR95855.1}; OS Homo sapiens neanderthalensis (Neanderthal). OG Mitochondrion {ECO:0000313|EMBL:CAR95855.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=63221 {ECO:0000313|EMBL:CAR95855.1}; RN [1] {ECO:0000313|EMBL:CAR95855.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mezmaiskaya 1 {ECO:0000313|EMBL:CAR95855.1}; RC TISSUE=Bone {ECO:0000313|EMBL:CAR95855.1}; RX DOI=10.1126/science.1174462; RA Briggs A.W., Good J.M., Green R.E., Krause J., Maricic T., Stenzel U., RA LaLueza-Fox C., Rudan P., Brajkovic D., Kucan Z., Gusic I., RA Schmitz R., Doronichev V.B., Golovanova L.V., de la Rasilla M., RA Fortea J., Rosas A., Paabo S.; RT "Targeted retrieval and analysis of five Neandertal mtDNA genomes."; RL Science 0:0-0(2009). RN [2] {ECO:0000313|EMBL:AGO20282.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Bone {ECO:0000313|EMBL:AGO20282.1}; RA Sawyer S.; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AGO20282.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Bone {ECO:0000313|EMBL:AGO20282.1}; RA Consortium H.C.N.G.; RT "The high-coverage genome sequence of a Neandertal individual from RT Denisova cave in the Altai."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AMQ34013.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DC1227 {ECO:0000313|EMBL:AMQ34013.1}; RX PubMed=27020421; DOI=10.1038/srep23559; RA Brown S., Higham T., Slon V., Paabo S., Meyer M., Douka K., Brock F., RA Comeskey D., Procopio N., Shunkov M., Derevianko A., Buckley M.; RT "Identification of a new hominin bone from Denisova Cave, Siberia RT using collagen fingerprinting and mitochondrial DNA analysis."; RL Sci. Rep. 6:23559-23559(2016). RN [5] {ECO:0000313|EMBL:ASK06267.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28675384; DOI=.1038/ncomms16046; RA Posth C., Wissing C., Kitagawa K., Pagani L., van Holstein L., RA Racimo F., Wehrberger K., Conard N.J., Kind C.J., Bocherens H., RA Krause J.; RT "Deeply divergent archaic mitochondrial genome provides lower time RT boundary for African gene flow into Neanderthals."; RL Nat. Commun. 8:16046-16046(2017). 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 ECO:0000256|SAAS:SAAS00711152}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887552}. 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; KC879692; AGO20282.1; -; Genomic_DNA. DR EMBL; KU131206; AMQ34013.1; -; Genomic_DNA. DR EMBL; KY751400; ASK06267.1; -; Genomic_DNA. DR EMBL; FM865411; CAR95855.1; -; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR036927; Cyt_c_oxase-like_su1_sf. 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, ECO:0000256|SAAS:SAAS00887236}; KW Electron transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711094}; KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161}; KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183}; KW Membrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711155}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:CAR95855.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711097}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711106}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 18 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 171 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 303 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 412 430 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 450 473 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 511 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 513 AA; 57011 MW; 3ADAE32BEBE67560 CRC64; MFADRWLFST NHKDIGTLYL LFGAWAGVLG TALSLLIRAE LGQPGNLLGN DHIYNVIVTA HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSLL LLLASAMVEA GAGTGWTVYP PLAGNYSHPG ASVDLTIFSL 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 KIHFAIMFIG VNLTFFPQHF LGLSGMPRRY SDYPDAYTTW NILSSVGSFI SLTAVMLMIF MIWEAFASKR KVLMVEEPSM NLEWLYGCPP PYHTFEEPVY MKS //