ID A0A3S8V8I1_CLYJA Unreviewed; 425 AA. AC A0A3S8V8I1; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 29-MAY-2024, entry version 19. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COX1 {ECO:0000313|EMBL:AZM32309.1}; OS Clypeaster japonicus (Sand dollar). OG Mitochondrion {ECO:0000313|EMBL:AZM32309.1}. OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea; OC Euechinoidea; Gnathostomata; Clypeasteroida; Clypeasteridae; Clypeaster. OX NCBI_TaxID=7644 {ECO:0000313|EMBL:AZM32309.1}; RN [1] {ECO:0000313|EMBL:AZM32309.1} RP NUCLEOTIDE SEQUENCE. RA Lee H., Lin J.-P., Li H.-C., Chang L.-Y., Lee K.-S., Lee S.-J., Chen W.-J., RA Sankar A., Kang S.-C.; RT "Young colonization history of a widespread sand dollar (Echinodermata; RT Clypeasteroida) in western Taiwan."; RL Quat Int 0:0-0(2018). 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|RuleBase:RU000369}; 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; MH837530; AZM32309.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3S8V8I1; -. DR UniPathway; UPA00705; -. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:TreeGrafter. 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:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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 PANTHER; PTHR10422:SF18; 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 Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; 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:AZM32309.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..29 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 41..63 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 137..159 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 171..198 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 231..249 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 256..279 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 291..314 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 326..347 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 367..388 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 400..419 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..425 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AZM32309.1" FT NON_TER 425 FT /evidence="ECO:0000313|EMBL:AZM32309.1" SQ SEQUENCE 425 AA; 46544 MW; D297639F9744DA66 CRC64; KDIGTLYLIF GAWAGMVGTA MSVIIRAELA QPGSLLQDDQ IYNVIVTAHA LVMIFFMVMP IMIGGFGNWL IPLMIGAPDM AFPRMNNMSF WLVPPSFILL LASAGVESGA GTGWTIYPPL SSNIAHAGGS VDLAIFSLHL AGASSILASI NFITTIINMR TPGISFDRLP LFVWSVFVTA FLLLLSLPVL AGAITMLLTD RNINTTFFDP AGGGDPILFQ HLFWFFGHPE VYILILPGFG MISHVIAHYS GKREPFGYLG MVYAMIAIGI LGFLVWAHHM FTVGMDVDTR AYFTAATMII AVPTGIKVFS WMATLQGSNL QWETPLLWAL GFVFLFTLGG LTGIVLANSS IDVVLHDTYY VVAHFHYVLS MGAVFAIFAG FTHWFPLFSG YSLHPLWSKA HFFIMFIGVN LTFFPQHFLG LAGMP //