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Database: UniProt
Entry: Q6EGI2
LinkDB: Q6EGI2
Original site: Q6EGI2 
ID   COX1_ORTGR              Reviewed;         514 AA.
AC   Q6EGI2; Q6EGI1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   01-OCT-2014, entry version 50.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=MT-CO1; Synonyms=COI, COXI, MTCO1;
OS   Orthogeomys grandis (Giant pocket gopher).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Geomyidae; Orthogeomys.
OX   NCBI_TaxID=249182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate LSUMZ M-3076, and Isolate MSH1572;
RA   Spradling T.A., Brant S.V., Hafner M.S., Dickerson C.J.;
RT   "DNA data support a rapid radiation of pocket gopher genera.";
RL   J. Mammal. Evol. 11:105-125(2004).
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; AY331082; AAR02583.1; -; Genomic_DNA.
DR   EMBL; AY331083; AAR02584.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q6EGI2; -.
DR   SMR; Q6EGI2; 1-511.
DR   HOVERGEN; HBG003841; -.
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; ISS:UniProtKB.
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:1902600; P:hydrogen ion transmembrane transport; ISS:GOC.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; -; 1.
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; 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    514       Cytochrome c oxidase subunit 1.
FT                                /FTId=PRO_0000254910.
FT   TRANSMEM     17     37       Helical. {ECO:0000255}.
FT   TRANSMEM     63     83       Helical. {ECO:0000255}.
FT   TRANSMEM    102    122       Helical. {ECO:0000255}.
FT   TRANSMEM    145    165       Helical. {ECO:0000255}.
FT   TRANSMEM    183    203       Helical. {ECO:0000255}.
FT   TRANSMEM    234    254       Helical. {ECO:0000255}.
FT   TRANSMEM    268    288       Helical. {ECO:0000255}.
FT   TRANSMEM    310    330       Helical. {ECO:0000255}.
FT   TRANSMEM    338    358       Helical. {ECO:0000255}.
FT   TRANSMEM    380    400       Helical. {ECO:0000255}.
FT   TRANSMEM    414    434       Helical. {ECO:0000255}.
FT   TRANSMEM    453    473       Helical. {ECO:0000255}.
FT   METAL        61     61       Iron (heme A axial ligand).
FT                                {ECO:0000305}.
FT   METAL       240    240       Copper B. {ECO:0000305}.
FT   METAL       244    244       Copper B. {ECO:0000305}.
FT   METAL       290    290       Copper B. {ECO:0000305}.
FT   METAL       291    291       Copper B. {ECO:0000305}.
FT   METAL       376    376       Iron (heme A3 axial ligand).
FT                                {ECO:0000305}.
FT   METAL       378    378       Iron (heme A axial ligand).
FT                                {ECO:0000305}.
FT   CROSSLNK    240    244       1'-histidyl-3'-tyrosine (His-Tyr).
FT                                {ECO:0000250}.
FT   VARIANT       3      3       V -> I (in strain: Isolate LSUMZ M-3076).
FT   VARIANT     514    514       T -> A (in strain: Isolate LSUMZ M-3076).
SQ   SEQUENCE   514 AA;  56951 MW;  9F5DA18C6A0658EF CRC64;
     MFVNRWLFST NHKDIGTLYM IFGAWAGMVG TGLSILIRAE LGQPGSLLGD DQIYNVVVTA
     HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA
     GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAITQYQ
     TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
     PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD
     TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTI GGLTGIVLSN
     SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF TGYTLNETWA KIHFTIMFVG
     VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW NTISSMGSFI SLTAVILMIF MIWEALASKR
     LVKSVPLTST NLEWIYGCPP PFHTFEEPVF IKST
//
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