ID A0A3S8V8I1_CLYJA Unreviewed; 425 AA. AC A0A3S8V8I1; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {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; OC Echinoidea; Euechinoidea; Gnathostomata; Clypeasteroida; OC 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., RA Chen W.-J., Sankar A., Kang S.-C.; RT "Young colonization history of a widespread sand dollar RT (Echinodermata; Clypeasteroida) in western Taiwan."; RL Quat Int 0:0-0(2018). 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: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. 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; MH837530; AZM32309.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AZM32309.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; 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}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 159 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 279 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 291 314 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 367 388 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 400 419 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 425 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AZM32309.1}. FT NON_TER 425 425 {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 //