ID   I3WSD9_NOTSA            Unreviewed;       200 AA.
AC   I3WSD9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   22-FEB-2023, entry version 43.
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|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}.
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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   AlphaFoldDB; I3WSD9; -.
DR   UniPathway; UPA00705; -.
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; 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   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.
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="Cytochrome oxidase subunit I profile"
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
//