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Database: UniProt
Entry: Q36775
LinkDB: Q36775
Original site: Q36775 
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   11-JUN-2014, entry version 91.
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; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; 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.
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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   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: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    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
//
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