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 06-MAR-2013, entry version 43.
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.
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DR EMBL; AY331082; AAR02583.1; -; Genomic_DNA.
DR EMBL; AY331083; AAR02584.1; -; Genomic_DNA.
DR HSSP; P00396; 2OCC.
DR ProteinModelPortal; Q6EGI2; -.
DR SMR; Q6EGI2; 1-511.
DR HOVERGEN; HBG003841; -.
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 1 514 Cytochrome c oxidase subunit 1.
FT /FTId=PRO_0000254910.
FT TRANSMEM 17 37 Helical; (Potential).
FT TRANSMEM 63 83 Helical; (Potential).
FT TRANSMEM 102 122 Helical; (Potential).
FT TRANSMEM 145 165 Helical; (Potential).
FT TRANSMEM 183 203 Helical; (Potential).
FT TRANSMEM 234 254 Helical; (Potential).
FT TRANSMEM 268 288 Helical; (Potential).
FT TRANSMEM 310 330 Helical; (Potential).
FT TRANSMEM 338 358 Helical; (Potential).
FT TRANSMEM 380 400 Helical; (Potential).
FT TRANSMEM 414 434 Helical; (Potential).
FT TRANSMEM 453 473 Helical; (Potential).
FT METAL 61 61 Iron (heme A axial ligand) (Probable).
FT METAL 240 240 Copper B (Probable).
FT METAL 244 244 Copper B (Probable).
FT METAL 290 290 Copper B (Probable).
FT METAL 291 291 Copper B (Probable).
FT METAL 376 376 Iron (heme A3 axial ligand) (Probable).
FT METAL 378 378 Iron (heme A axial ligand) (Probable).
FT CROSSLNK 240 244 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
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
//
