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Database: UniProt
Entry: P11947
LinkDB: P11947
Original site: P11947 
ID   COX1_TETPY              Reviewed;         698 AA.
AC   P11947;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   01-OCT-2014, entry version 90.
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   Tetrahymena pyriformis.
OG   Mitochondrion.
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ST;
RX   PubMed=2833363; DOI=10.1007/BF00405758;
RA   Ziaie Z., Suyama Y.;
RT   "The cytochrome oxidase subunit I gene of Tetrahymena: a 57 amino acid
RT   NH2-terminal extension and a 108 amino acid insert.";
RL   Curr. Genet. 12:357-368(1987).
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.
CC       {ECO:0000305}.
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DR   EMBL; L28677; AAA32102.2; -; Genomic_DNA.
DR   EMBL; X06133; CAB57808.1; -; Genomic_DNA.
DR   PIR; S00742; S00742.
DR   ProteinModelPortal; P11947; -.
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: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; -; 2.
DR   InterPro; IPR000883; COX1.
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; 2.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 2.
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    698       Cytochrome c oxidase subunit 1.
FT                                /FTId=PRO_0000183425.
FT   TRANSMEM     65     85       Helical. {ECO:0000255}.
FT   TRANSMEM    113    133       Helical. {ECO:0000255}.
FT   TRANSMEM    147    167       Helical. {ECO:0000255}.
FT   TRANSMEM    304    324       Helical. {ECO:0000255}.
FT   TRANSMEM    349    369       Helical. {ECO:0000255}.
FT   TRANSMEM    395    415       Helical. {ECO:0000255}.
FT   TRANSMEM    434    454       Helical. {ECO:0000255}.
FT   TRANSMEM    468    488       Helical. {ECO:0000255}.
FT   TRANSMEM    498    518       Helical. {ECO:0000255}.
FT   TRANSMEM    533    553       Helical. {ECO:0000255}.
FT   TRANSMEM    574    594       Helical. {ECO:0000255}.
FT   TRANSMEM    613    633       Helical. {ECO:0000255}.
FT   METAL       111    111       Iron (heme A axial ligand).
FT                                {ECO:0000305}.
FT   METAL       401    401       Copper B. {ECO:0000305}.
FT   METAL       405    405       Copper B. {ECO:0000305}.
FT   METAL       450    450       Copper B. {ECO:0000305}.
FT   METAL       451    451       Copper B. {ECO:0000305}.
FT   METAL       536    536       Iron (heme A3 axial ligand).
FT                                {ECO:0000305}.
FT   METAL       538    538       Iron (heme A axial ligand).
FT                                {ECO:0000305}.
FT   CROSSLNK    401    405       1'-histidyl-3'-tyrosine (His-Tyr).
FT                                {ECO:0000250}.
SQ   SEQUENCE   698 AA;  81747 MW;  D6B0F488A3109A72 CRC64;
     MLYIFNSFDN MWVDFIEQTK SFKVSVNNYF YYLNKIKKLF TYLNDLRKHI LKKYVYTINH
     KRIAINYLYF SMVTGLSGAA LATMIRMELA HPESPFFKGD SLRYLQVVTA HGLIMVFFVV
     VPILFGGFAN FLIPYHVGSK DVAYPRLNSI GFWIQPCGYI LLAKIGFLRP QFWRYYDKTS
     FSFPFLEKMK YNQYKEYKND YLFYLDFLKK EITDDHSFFW KARKVIKLPQ YSVFSFVPLK
     LMMWKTMINY PESFWYAASR VVQSRRKKVF VTKCSARTLT TAGWTFITPF SSNIKYTGVG
     SQDILILSVV FAGISTTISF TNLLITRRTL AMPGMRHRRV LMPFVTISIF LTLRMLATIT
     PVLGAAVIMM AFDRHWQTTF FEYAYGGDPI LSQHLFWFFG HPEVYVLIIP TFGFINMIVP
     HNNTRRVASK HHMIWAIYVM AYMGYLVWGH HMYLVGLDHR SRTMYSTITI MISMPATIKV
     VNWTLSLVNG ALKVDLPFLF SMSFLLLFLV AGFTGMWLSH VSLNVSMHDT FYVVAHFHIM
     LSGAAITGIF SGFYYYFNAL FGIKFSRMFG YMHLIYYSGG QWVAFVPQFY LGFSGMPRRI
     HDYPVVFMGW HSMSTAGHFI TLIGIMFFFL MIFDSHIERR AATSSTLGLP RWYKRISYYI
     FKIRYLQHNK AKMNGIPGST VRLMLIDRHF AEFEVFKK
//
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