ID   A0A9E8LPZ7_9CHON        Unreviewed;       196 AA.
AC   A0A9E8LPZ7;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   02-OCT-2024, entry version 8.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COI {ECO:0000313|EMBL:UZZ46385.1};
OS   Centrophorus cf. uyato RC-2022.
OG   Mitochondrion {ECO:0000313|EMBL:UZZ46385.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Squalomorphii; Squaliformes; Centrophoridae; Centrophorus.
OX   NCBI_TaxID=2998149 {ECO:0000313|EMBL:UZZ46385.1};
RN   [1] {ECO:0000313|EMBL:UZZ46385.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bellodi A., Benvenuto A., Melis R., Mulas A., Barone M., Barria C.,
RA   Cariani A., Carugati L., Chatzispyrou A., Desrochers M., Ferrari A.,
RA   Guallart J., Hemida F., Mancusi C., Mazzoldi C., Ramirez-Amaro S., Rey J.,
RA   Scannella D., Serena F., Tinti F., Vella A., Follesa M.C., Cannas R.;
RT   "Call me by my name: unravelling the taxonomy of the gulper shark genus
RT   Centrophorus in the Mediterranean Sea through an integrated taxonomic
RT   approach.";
RL   Zool. J. Linn. Soc. 195:815-840(2022).
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|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: 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; OL670323; UZZ46385.1; -; Genomic_DNA.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:TreeGrafter.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter.
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|ARBA:ARBA00023008, 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:UZZ46385.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
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        23..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..196
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:UZZ46385.1"
FT   NON_TER         196
FT                   /evidence="ECO:0000313|EMBL:UZZ46385.1"
SQ   SEQUENCE   196 AA;  20860 MW;  704AA0D84A2920AC CRC64;
     TALSLLIRTE LSQPGTLLGD DQIYNVIVTA HAFVMIFFMV MPVMIGGFGN WLVPLMIGAP
     DMAFPRMNNM SFWLLPPSLL LLLASAGVEA GAGTGWTVYP PLAGNMAHAG TSVDLAIFSL
     HLAGISSILA SINFITTIIN MKPPAISQYQ TPLFVWSILV TTILLLLALP VLAAAITMLL
     TDRNLNTTFF DPAGGG
//