ID C7BWV0_HOMNE Unreviewed; 513 AA. AC C7BWV0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 14-DEC-2022, entry version 68. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, 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). RN [8] {ECO:0000313|EMBL:QIT06496.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Chagyrskaya8 {ECO:0000313|EMBL:QIT06496.1}; RA Mafessoni F., Grote S., de Filippo C., Slon V., Kolobova K.A., Viola B., RA Markin S.V., Chintalapati M., Peyregne S., Skov L., Skoglund P., RA Krivoshapkin A.I., Derevianko A.P., Meyer M., Kelso J., Peter B., RA Pruefer K., Paeaebo S.; RT "A high-coverage Neandertal genome from Chagyrskaya Cave."; RL J. ISSAAS 0:0-0(2020). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane CC protein {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|ARBA:ARBA00009578, 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 EMBL; MK388903; QIT06496.1; -; Genomic_DNA. DR AlphaFoldDB; C7BWV0; -. DR SMR; C7BWV0; -. DR UniPathway; UPA00705; -. 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: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; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:CAR95855.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000369}; Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000369}. 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 //