ID I3WSD9_NOTSA Unreviewed; 200 AA. AC I3WSD9; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 03-AUG-2022, entry version 40. 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=COI {ECO:0000313|EMBL:AFL45856.1}; OS Notochthamalus scabrosus (Scabrous barnacle) (Chthamalus scabrosus). OG Mitochondrion {ECO:0000313|EMBL:AFL45856.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Cirripedia; Thoracica; Thoracicalcarea; Balanomorpha; Chthamaloidea; OC Chthamalidae; Notochthamalus. OX NCBI_TaxID=261896 {ECO:0000313|EMBL:AFL45856.1}; RN [1] {ECO:0000313|EMBL:AFL45856.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GuanHX13 {ECO:0000313|EMBL:AFL45799.1}, GuanHX23 RC {ECO:0000313|EMBL:AFL45801.1}, GuanLX10 {ECO:0000313|EMBL:AFL45803.1}, RC GuanLX31 {ECO:0000313|EMBL:AFL45811.1}, GuanLX35 RC {ECO:0000313|EMBL:AFL45813.1}, LCrLx22 {ECO:0000313|EMBL:AFL45904.1}, RC LCrLx7 {ECO:0000313|EMBL:AFL45905.1}, PtaMX12 RC {ECO:0000313|EMBL:AFL45836.1}, Tem25HX1 {ECO:0000313|EMBL:AFL45837.1}, RC Tem25HX3 {ECO:0000313|EMBL:AFL45840.1}, Tem25HX4 RC {ECO:0000313|EMBL:AFL45841.1}, Tem25HX5 {ECO:0000313|EMBL:AFL45842.1}, RC Tem25HX6 {ECO:0000313|EMBL:AFL45843.1}, Tem25HX9 RC {ECO:0000313|EMBL:AFL45844.1}, Tem47LX18 RC {ECO:0000313|EMBL:AFL45850.1}, Tem47LX21 RC {ECO:0000313|EMBL:AFL45852.1}, Tem47LX23 RC {ECO:0000313|EMBL:AFL45853.1}, Tem47LX26 RC {ECO:0000313|EMBL:AFL45856.1}, Tem47LX28 RC {ECO:0000313|EMBL:AFL45857.1}, Tem47LX32 RC {ECO:0000313|EMBL:AFL45860.1}, Tem47LX35 RC {ECO:0000313|EMBL:AFL45861.1}, Tem47LX36 RC {ECO:0000313|EMBL:AFL45862.1}, Tem47LX4 {ECO:0000313|EMBL:AFL45863.1}, RC Tem47LX5 {ECO:0000313|EMBL:AFL45864.1}, Tem47LX9 RC {ECO:0000313|EMBL:AFL45867.1}, Tem9HX10 {ECO:0000313|EMBL:AFL45868.1}, RC Tem9HX12 {ECO:0000313|EMBL:AFL45869.1}, Tem9HX13 RC {ECO:0000313|EMBL:AFL45870.1}, Tem9HX14 {ECO:0000313|EMBL:AFL45871.1}, RC Tem9HX16 {ECO:0000313|EMBL:AFL45873.1}, Tem9HX18 RC {ECO:0000313|EMBL:AFL45874.1}, Tem9HX19 {ECO:0000313|EMBL:AFL45875.1}, RC Tem9HX2 {ECO:0000313|EMBL:AFL45876.1}, Tem9HX21 RC {ECO:0000313|EMBL:AFL45877.1}, Tem9HX23 {ECO:0000313|EMBL:AFL45878.1}, RC Tem9HX27 {ECO:0000313|EMBL:AFL45880.1}, Tem9HX3 RC {ECO:0000313|EMBL:AFL45883.1}, Tem9HX30 {ECO:0000313|EMBL:AFL45884.1}, RC Tem9HX8 {ECO:0000313|EMBL:AFL45887.1}, Tem9HX9 RC {ECO:0000313|EMBL:AFL45888.1}, ValUX18 {ECO:0000313|EMBL:AFL45889.1}, RC ValUX19 {ECO:0000313|EMBL:AFL45890.1}, ValUX23 RC {ECO:0000313|EMBL:AFL45892.1}, ValUX24 {ECO:0000313|EMBL:AFL45893.1}, RC ValUX25 {ECO:0000313|EMBL:AFL45894.1}, ValUX26 RC {ECO:0000313|EMBL:AFL45895.1}, ValUX28 {ECO:0000313|EMBL:AFL45896.1}, RC and ValUX30 {ECO:0000313|EMBL:AFL45898.1}; RA Wares J., Laughlin K., Ewers C.; RT "Mitochondrial lineages in Notochthamalus scabrosus as indicators of RT coastal recruitment and interactions."; RL Submitted (APR-2012) 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 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=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: 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|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; JQ950758; AFL45799.1; -; Genomic_DNA. DR EMBL; JQ950760; AFL45801.1; -; Genomic_DNA. DR EMBL; JQ950762; AFL45803.1; -; Genomic_DNA. DR EMBL; JQ950770; AFL45811.1; -; Genomic_DNA. DR EMBL; JQ950772; AFL45813.1; -; Genomic_DNA. DR EMBL; JQ950795; AFL45836.1; -; Genomic_DNA. DR EMBL; JQ950796; AFL45837.1; -; Genomic_DNA. DR EMBL; JQ950799; AFL45840.1; -; Genomic_DNA. DR EMBL; JQ950800; AFL45841.1; -; Genomic_DNA. DR EMBL; JQ950801; AFL45842.1; -; Genomic_DNA. DR EMBL; JQ950802; AFL45843.1; -; Genomic_DNA. DR EMBL; JQ950803; AFL45844.1; -; Genomic_DNA. DR EMBL; JQ950809; AFL45850.1; -; Genomic_DNA. DR EMBL; JQ950811; AFL45852.1; -; Genomic_DNA. DR EMBL; JQ950812; AFL45853.1; -; Genomic_DNA. DR EMBL; JQ950815; AFL45856.1; -; Genomic_DNA. DR EMBL; JQ950816; AFL45857.1; -; Genomic_DNA. DR EMBL; JQ950819; AFL45860.1; -; Genomic_DNA. DR EMBL; JQ950820; AFL45861.1; -; Genomic_DNA. DR EMBL; JQ950821; AFL45862.1; -; Genomic_DNA. DR EMBL; JQ950822; AFL45863.1; -; Genomic_DNA. DR EMBL; JQ950823; AFL45864.1; -; Genomic_DNA. DR EMBL; JQ950826; AFL45867.1; -; Genomic_DNA. DR EMBL; JQ950827; AFL45868.1; -; Genomic_DNA. DR EMBL; JQ950828; AFL45869.1; -; Genomic_DNA. DR EMBL; JQ950829; AFL45870.1; -; Genomic_DNA. DR EMBL; JQ950830; AFL45871.1; -; Genomic_DNA. DR EMBL; JQ950832; AFL45873.1; -; Genomic_DNA. DR EMBL; JQ950833; AFL45874.1; -; Genomic_DNA. DR EMBL; JQ950834; AFL45875.1; -; Genomic_DNA. DR EMBL; JQ950835; AFL45876.1; -; Genomic_DNA. DR EMBL; JQ950836; AFL45877.1; -; Genomic_DNA. DR EMBL; JQ950837; AFL45878.1; -; Genomic_DNA. DR EMBL; JQ950839; AFL45880.1; -; Genomic_DNA. DR EMBL; JQ950842; AFL45883.1; -; Genomic_DNA. DR EMBL; JQ950843; AFL45884.1; -; Genomic_DNA. DR EMBL; JQ950846; AFL45887.1; -; Genomic_DNA. DR EMBL; JQ950847; AFL45888.1; -; Genomic_DNA. DR EMBL; JQ950848; AFL45889.1; -; Genomic_DNA. DR EMBL; JQ950849; AFL45890.1; -; Genomic_DNA. DR EMBL; JQ950851; AFL45892.1; -; Genomic_DNA. DR EMBL; JQ950852; AFL45893.1; -; Genomic_DNA. DR EMBL; JQ950853; AFL45894.1; -; Genomic_DNA. DR EMBL; JQ950854; AFL45895.1; -; Genomic_DNA. DR EMBL; JQ950855; AFL45896.1; -; Genomic_DNA. DR EMBL; JQ950857; AFL45898.1; -; Genomic_DNA. DR EMBL; JQ950863; AFL45904.1; -; Genomic_DNA. DR EMBL; JQ950864; AFL45905.1; -; 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:AFL45856.1}; 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 20..46 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 67..91 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 111..134 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 146..173 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..200 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFL45856.1" FT NON_TER 200 FT /evidence="ECO:0000313|EMBL:AFL45856.1" SQ SEQUENCE 200 AA; 21676 MW; 01AF5BB89383E6DF CRC64; RAELGQPGSL IGDDQIYNVI VTAHAFIMIF FMVMPIMIGG FGNWLLPLML GAPDMAFPRL NNMSFWLLPP ALMLLISGSL VEAGAGTGWT VYPPLASNIA HSGASVDLSI FSLHLAGASS ILGAINFMST VINMRAETLT FDRLPLFVWS VFVTVILLLL SLPVLAGAIT MLLTDRNLNT SFFDPTGGGD PILYQHLFWF //