ID A0A0A0R0N8_AMPAM Unreviewed; 204 AA. AC A0A0A0R0N8; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 29-SEP-2021, entry version 23. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AIU93028.1}; OS Amphibalanus amphitrite (Striped barnacle) (Balanus amphitrite). OG Mitochondrion {ECO:0000313|EMBL:AIU93028.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Hexanauplia; Cirripedia; Thoracica; Sessilia; Balanidae; Amphibalanus. OX NCBI_TaxID=1232801 {ECO:0000313|EMBL:AIU93028.1}; RN [1] {ECO:0000313|EMBL:AIU93028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AmpDuk1 {ECO:0000313|EMBL:AIU93028.1}, and AmpDuk2 RC {ECO:0000313|EMBL:AIU93031.1}; RX PubMed=25343722; DOI=10.1080/08927014.2014.967232; RA Chen H.N., Tsang L.M., Chong V.C., Chan B.K.; RT "Worldwide genetic differentiation in the common fouling barnacle, RT Amphibalanus amphitrite."; RL Biofouling 30:1067-1078(2014). RN [2] {ECO:0000313|EMBL:AIU93028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AmpDuk1 {ECO:0000313|EMBL:AIU93028.1}, and AmpDuk2 RC {ECO:0000313|EMBL:AIU93031.1}; RA Chen H.-N., Tsang L.M., Chong V.C., Chan B.K.K.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. 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 CC [Fe(III)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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, CC 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; KM211415; AIU93028.1; -; Genomic_DNA. DR EMBL; KM211418; AIU93031.1; -; Genomic_DNA. 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:0070469; C:respirasome; IEA:UniProtKB-KW. 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 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}; 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, ECO:0000313|EMBL:AIU93028.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 31..61 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 82..106 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 126..149 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 161..188 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..204 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIU93028.1" FT NON_TER 204 FT /evidence="ECO:0000313|EMBL:AIU93028.1" SQ SEQUENCE 204 AA; 21719 MW; AD7CD74D2572F983 CRC64; GAWSAMVGTA LSMLIRAELG QPGSLIGDDQ IYNVIVTAHA FIMIFFMVMP IMIGGFGNWL LPLMLGAPDM AFPRLNNMSF WLLPPALMLL ISGSLVEAGA GTGWTVFPPL SSNIAHSGAS VDLSIFSLHL AGASSILGAI NFMSTVINMR AETLTFDRLP LFVWSVFITV ILLLLSLPVL AGAITMLLTD RNLNTSFFDP TGGG //