ID C7BWV0_HOMNE Unreviewed; 513 AA. AC C7BWV0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 26-FEB-2020, entry version 55. 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}; GN Synonyms=COI {ECO:0000313|EMBL:QAU54308.1}; OS Homo sapiens neanderthalensis (Neanderthal). OG Mitochondrion {ECO:0000313|EMBL:CAR95855.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Schmitz R., RA Doronichev V.B., Golovanova L.V., de la Rasilla M., Fortea J., Rosas A., RA 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 Denisova RT 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 using RT 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=10.1038/ncomms16046; RA Posth C., Wissing C., Kitagawa K., Pagani L., van Holstein L., Racimo F., RA Wehrberger K., Conard N.J., Kind C.J., Bocherens H., Krause J.; RT "Deeply divergent archaic mitochondrial genome provides lower time boundary RT for African gene flow into Neanderthals."; RL Nat. Commun. 8:16046-16046(2017). RN [6] {ECO:0000313|EMBL:AMQ34013.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DC1227 {ECO:0000313|EMBL:AMQ34013.1}, and Denisova15 RC {ECO:0000313|EMBL:QAU54308.1}; RX PubMed=30700871; DOI=.1038/s41586-018-0870-z; RA Douka K., Slon V., Jacobs Z., Bronk Ramsey C., Shunkov M.V., RA Derevianko A.P., Mafessoni F., Kozlikin M.B., Li B., Grun R., Kinsley L., RA Comeskey D., Deviese T., Brown S., Viola B., Kinsley L., Buckley M., RA Meyer M., Roberts R.G., Paabo S., Kelso J., Higham T.; RT "Age estimates for hominin fossils and the onset of the Upper Palaeolithic RT at Denisova Cave."; RL Nature 565:640-644(2019). RN [7] {ECO:0000313|EMBL:ASK06267.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Scladina I-4A {ECO:0000313|EMBL:QEE94730.1}; RX PubMed=31249872; DOI=.1126/sciadv.aaw5873; RA Peyregne S., Slon V., Mafessoni F., de Filippo C., Hajdinjak M., Nagel S., RA Nickel B., Essel E., Le Cabec A., Wehrberger K., Conard N.J., Kind C.J., RA Posth C., Krause J., Abrams G., Bonjean D., Di Modica K., Toussaint M., RA Kelso J., Meyer M., Paeaebo S., Pruefer K.; RT "Nuclear DNA from two early Neandertals reveals 80,000 years of genetic RT continuity in Europe."; RL Sci. Adv. 5:eaaw5873-eaaw5873(2019). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369, CC ECO:0000256|SAAS:SAAS01116619}; 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 EMBL; MK033602; QAU54308.1; -; Genomic_DNA. DR EMBL; MK123269; QEE94730.1; -; Genomic_DNA. DR SMR; C7BWV0; -. 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, ECO:0000256|SAAS:SAAS00711163, KW 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, ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 18..37 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..83 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..128 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 148..171 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 183..210 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 243..261 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 268..291 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 303..325 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 337..359 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 379..400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 412..430 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 450..473 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..511 FT /note="COX1" FT /evidence="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 //