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Database: UniProt
Entry: P14544
LinkDB: P14544
Original site: P14544 
ID   COX1_LEITA              Reviewed;         549 AA.
AC   P14544;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   16-APR-2014, entry version 81.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=COI;
OS   Leishmania tarentolae (Sauroleishmania tarentolae).
OG   Mitochondrion.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leishmania; lizard Leishmania.
OX   NCBI_TaxID=5689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=6096360;
RA   de la Cruz V.F., Neckelmann N., Simpson L.;
RT   "Sequences of six genes and several open reading frames in the
RT   kinetoplast maxicircle DNA of Leishmania tarentolae.";
RL   J. Biol. Chem. 259:15136-15147(1984).
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   PIR; D30010; D30010.
DR   ProteinModelPortal; P14544; -.
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:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-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: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; SSF81442; 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    549       Cytochrome c oxidase subunit 1.
FT                                /FTId=PRO_0000183350.
FT   TRANSMEM     18     38       Helical; (Potential).
FT   TRANSMEM     42     62       Helical; (Potential).
FT   TRANSMEM     66     86       Helical; (Potential).
FT   TRANSMEM    100    120       Helical; (Potential).
FT   TRANSMEM    148    168       Helical; (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TRANSMEM    222    242       Helical; (Potential).
FT   TRANSMEM    246    266       Helical; (Potential).
FT   TRANSMEM    269    289       Helical; (Potential).
FT   TRANSMEM    306    326       Helical; (Potential).
FT   TRANSMEM    340    360       Helical; (Potential).
FT   TRANSMEM    379    399       Helical; (Potential).
FT   TRANSMEM    402    422       Helical; (Potential).
FT   TRANSMEM    460    480       Helical; (Potential).
FT   TRANSMEM    484    504       Helical; (Potential).
FT   TRANSMEM    520    540       Helical; (Potential).
FT   METAL        64     64       Iron (heme A axial ligand) (Probable).
FT   METAL       243    243       Copper B (Probable).
FT   METAL       247    247       Copper B (Probable).
FT   METAL       292    292       Copper B (Probable).
FT   METAL       293    293       Copper B (Probable).
FT   METAL       378    378       Iron (heme A3 axial ligand) (Probable).
FT   METAL       380    380       Iron (heme A axial ligand) (Probable).
FT   CROSSLNK    243    247       1'-histidyl-3'-tyrosine (His-Tyr) (By
FT                                similarity).
SQ   SEQUENCE   549 AA;  63272 MW;  F6DD04815A4917C2 CRC64;
     MFWLCLVCLS VSHKMIGLCY LLVAILSGFV GYVYSLFIRL ELSLIGCGIL FGDYQFYNVL
     ITSHGLIMVF AFIMPVMMGG LVNYFIPVMA GFPDMVFPRL NNMSFWMYLA GFGCVVNGFL
     TEEGMGVGWT LYPTLICIDF HSSLACDFVM FAVHLLGISS ILNSINLLGT LFCCRRKFFS
     FLSWSLFIWA ALITAILLII TLPVLAGGVT LILCDRNFNT SFYDVVGGGD LILFQHIFWF
     FGHPEVYIIL LPVFGLISTI VEVIGFRCVF STVAMIYSMI LIAILGMFVW AHHMFVVGMD
     VDSRAYFGGV SILIGLPTCV KLFNWIYSFL YTDMIITFEV YFVIMFIFMF LIGAVTGLFL
     SNVGIDIMLH DTYFVVGHFH YVLSLGAVVG FFTGFIHFLA KWLPIELYLF WMFYFISTLF
     IGSNMLFFPM HSLGMYAFPR RISDYPVSFL FWSSFMLYGM LLLASLILFL CALFCVFLFW
     DYCLFFVSLF VFSLYCFFYF STWLPCVMVL YLLLVDFAHI VLDYLFLILC FCFVFFIFFW
     QSLFLFFYI
//
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