ID   A0A343CWY9_ORYCU        Unreviewed;       518 AA.
AC   A0A343CWY9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   07-APR-2021, entry version 13.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
GN   Name=COI {ECO:0000313|EMBL:ARO89801.1};
OS   Oryzias curvinotus (Hynann ricefish) (Aplocheilus curvinotus).
OG   Mitochondrion {ECO:0000313|EMBL:ARO89801.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=104658 {ECO:0000313|EMBL:ARO89801.1};
RN   [1] {ECO:0000313|EMBL:ARO89801.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang Z., Long S., Liao J., Huang C., Zhang H., Liu L., Guo Y.;
RT   "Complete mitogenome of Hainan medaka Oryzias curvinotus (Teleostei:
RT   Beloniformes) and transcriptional differences between male and female
RT   liver.";
RL   Mitochondrial DNA Part B Resour 2:157-158(2017).
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] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC         + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC         COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000256|RuleBase:RU000369};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane
CC       protein {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; KY364884; ARO89801.1; -; 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:0045277; C:respiratory chain complex IV; IEA:InterPro.
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:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000369};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369};
KW   Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:ARO89801.1};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW   ECO:0000256|RuleBase:RU000369}; Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000369};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        450..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..511
FT                   /note="COX1"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   518 AA;  57284 MW;  75819676AA76567A CRC64;
     MAITRWFFST NHKDIGTLYL IFGAWAGMVG TALSLLIRAE LSQPGSLLGD DQIYNVIVTA
     HAFVMIFFMV MPIMIGGFGN WLIPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA
     GAGTGWTVYP PLSGNLAHAG ASVDLTIFSL HLAGISSILG AINFITTIIN MKPPAISQYQ
     TPLFVWAVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
     PEVYILILPG FGMISHIVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD
     TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPLLW ALGFIFLFTV GGLTGIVLAN
     SSLDIMLHDT YYVVAHFHYV LSMGAVFAIM GAFVHWFPLF SGYTLHNTWT KIHFGVMFVG
     VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NTISSLGSLI SLIAVIMFLF IIWEAFAAKR
     EVLSVELTAT NVEWLHGCPP PYHTFEEPAF VQIQQSKF
//