ID A0A3Q8TN87_9EUCA Unreviewed; 185 AA. AC A0A3Q8TN87; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 08-MAY-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:AZL49208.1}; OS Planes major. OG Mitochondrion {ECO:0000313|EMBL:AZL49208.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; OC Brachyura; Eubrachyura; Grapsoidea; Grapsidae; Planes. OX NCBI_TaxID=1581164 {ECO:0000313|EMBL:AZL49208.1}; RN [1] {ECO:0000313|EMBL:AZL49208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RNANA212223CR1 {ECO:0000313|EMBL:AZL49208.1}; RX PubMed=30503417; DOI=10.1016/j.marpolbul.2018.10.015; RA Rech S., Thiel M., Borrell Pichs Y.J., Garcia-Vazquez E.; RT "Travelling light: Fouling biota on macroplastics arriving on beaches RT of remote Rapa Nui (Easter Island) in the South Pacific Subtropical RT Gyre. ."; RL Mar. Pollut. Bull. 137:119-128(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; MH536247; AZL49208.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. 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 PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 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, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AZL49208.1}; 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|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 20 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 135 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 174 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 185 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AZL49208.1}. FT NON_TER 185 185 {ECO:0000313|EMBL:AZL49208.1}. SQ SEQUENCE 185 AA; 19934 MW; 1B0D8445D33E281B CRC64; IRAELSQPGS LIGDDQIYNV VVTAHAFVMI FFMVMPIMIG GFGNWLVPLM LGAPDMAFPR MNNMSFWLLP PSLSLLLTSS MVESGVGTGW TVYPPLAAAI AHAGASVDLG IFSLHLAGVS SILGAVNFMT TVINMRSYGM TMDQMPLFVW AVFITAILLL LSLPVLAGAI TMLLTDRNLN TSFFD //