ID COX1_GADMO Reviewed; 516 AA.
AC Q36775;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-APR-2013, entry version 85.
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 Gadus morhua (Atlantic cod).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Norwegian coastal 1;
RX PubMed=8018725; DOI=10.1016/0167-4781(94)90015-9;
RA Johansen S., Johansen T.;
RT "Sequence analysis of 12 structural genes and a novel non-coding
RT region from mitochondrial DNA of Atlantic cod, Gadus morhua.";
RL Biochim. Biophys. Acta 1218:213-217(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Norwegian coastal 1;
RX PubMed=8817926;
RA Johansen S., Bakke I.;
RT "The complete mitochondrial DNA sequence of Atlantic cod (Gadus
RT morhua): relevance to taxonomic studies among codfishes.";
RL Mol. Mar. Biol. Biotechnol. 5:203-214(1996).
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 -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X76364; CAA53965.1; -; Genomic_DNA.
DR EMBL; X99772; CAA68108.1; -; Genomic_DNA.
DR PIR; S45351; S45351.
DR RefSeq; NP_008615.1; NC_002081.1.
DR ProteinModelPortal; Q36775; -.
DR SMR; Q36775; 3-514.
DR GeneID; 808455; -.
DR CTD; 4512; -.
DR HOVERGEN; HBG003841; -.
DR ProtClustDB; MTH00183; -.
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 1 516 Cytochrome c oxidase subunit 1.
FT /FTId=PRO_0000183335.
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 456 476 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).
SQ SEQUENCE 516 AA; 57085 MW; 6B9948C48D363834 CRC64;
MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGALLGD DQIYNVIVTA
HAFVMIFFMV MPLMIGGFGN WLIPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA
GAGTGWTLYP PLAGNLAHAG ASVDLTIFSL HLAGISSILG AINFITTIIN MKPPAISQYQ
TPLFVWAVLI TAVLLLLSLP VLAAGITMLL TDRNLNTSFF DPAGGGDPIL YQHLFWFFGH
PEVYILILPG FGMISHIVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD
TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPLLW ALGFIFLFTV GGLTGIVLAN
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AAFVHWFPLF TGYTLHDTWT KIHFGVMFVG
VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NTVSSIGSLI SLMAVIMFLF ILWEAFAAKR
EVMAVEMTMT NVEWLHGCPP PYHTFEEPAF VQIQTR
//
