ID   COX1_CANSI              Reviewed;         196 AA.
AC   Q33375;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-APR-2013, entry version 77.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
DE   Flags: Fragment;
GN   Name=MT-CO1; Synonyms=COI, COXI, MTCO1;
OS   Canis simensis (Ethiopian wolf) (Simenia simensis).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=32534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7921357; DOI=10.1111/j.1365-294X.1994.tb00070.x;
RA   Gottelli D., Sillero-Zubiri C., Applebaum G.D., Roy M.S., Girman D.J.,
RA   Garcia-Moreno J., Ostrander E.A., Wayne R.K.;
RT   "Molecular genetics of the most endangered canid: the Ethiopian wolf
RT   Canis simensis.";
RL   Mol. Ecol. 3:301-312(1994).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC       3 form the functional core of the enzyme complex. CO I is the
CC       catalytic subunit of the enzyme. Electrons originating in
CC       cytochrome c are transferred via the copper A center of subunit 2
CC       and heme A of subunit 1 to the bimetallic center formed by heme A3
CC       and copper B.
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
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DR   EMBL; L29413; AAA53663.2; ALT_SEQ; Genomic_DNA.
DR   ProteinModelPortal; Q33375; -.
DR   SMR; Q33375; 2-196.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR000883; Cyt_c_Oxase_su1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; COX1; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN        <1   >196       Cytochrome c oxidase subunit 1.
FT                                /FTId=PRO_0000183301.
FT   TRANSMEM      9     29       Helical; (Potential).
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TRANSMEM     76     96       Helical; (Potential).
FT   TRANSMEM    104    124       Helical; (Potential).
FT   TRANSMEM    146    166       Helical; (Potential).
FT   TRANSMEM    176    196       Helical; (Potential).
FT   METAL         6      6       Copper B (Probable).
FT   METAL        10     10       Copper B (Probable).
FT   METAL        56     56       Copper B (Probable).
FT   METAL        57     57       Copper B (Probable).
FT   METAL       142    142       Iron (heme A3 axial ligand) (Probable).
FT   METAL       144    144       Iron (heme A axial ligand) (Probable).
FT   CROSSLNK      6     10       1'-histidyl-3'-tyrosine (His-Tyr) (By
FT                                similarity).
FT   NON_TER       1      1
FT   NON_TER     196    196
SQ   SEQUENCE   196 AA;  22107 MW;  8C5CE47EC8CE515C CRC64;
     XWFFGHPEVY ILILPGFGMI SHIVTYYSGK KEPFGYMGMV WAMMSIGFLG FIVWAHHMFT
     VGMDVDTRAY FTSATMIIAI PTGVKVFSWL ATLHGGNIKW SPAMLWALGF IFLFTVGGLT
     GIVLANSSLD IVLHDTYYVV AHFHYVLSMG AVFAIMGGFA HWFPLFSGYT LNDTWAKIHF
     TIMFVGVNMT FFPQHF
//