ID   G9B2Z2_9PERC            Unreviewed;       229 AA.
AC   G9B2Z2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   16-APR-2014, entry version 13.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   Flags: Fragment;
GN   Name=COI;
OS   Pholis nebulosa (tidepool gunnel).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Pholidae; Pholis.
OX   NCBI_TaxID=283027;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Kim D.-W., Kim R.N., Kang D.W., Min H.K., Park H.C., Park Y.-H.,
RA   Paek W.-K., Lim J.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23166532; DOI=10.5808/GI.2012.10.3.206;
RA   Kim D.W., Yoo W.G., Park H.C., Yoo H.S., Kang D.W., Jin S.D.,
RA   Min H.K., Paek W.K., Lim J.;
RT   "DNA barcoding of fish, insects, and shellfish in Korea.";
RL   Genomics Inform 10:206-211(2012).
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 (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
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DR   EMBL; HM180566; AEW29179.1; -; Genomic_DNA.
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: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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR000883; Cyt_c_Oxase_su1.
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.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Respiratory chain; Transmembrane; Transport.
FT   NON_TER       1      1
FT   NON_TER     229    229
SQ   SEQUENCE   229 AA;  24561 MW;  5A3B0D491FABFB7A CRC64;
     HKDIGTLYLV FGAWAGMVGT ALSLLIRAXL SQPGXLLGDD QINVIVTAHA FVMIFFMVMP
     IMIGGFGNWL IPLMIGAPDM AFPRMNNMSF WLLPPSFLLL LASSGVEAGA GTGWTVYPPL
     SGNLAHAGAS VDLTIFSLHL AGISSILGAI NFITTIINMK PPAISQYQTP LFVWSVLITA
     VLLLLSLPVL AAGITMLLTD RNLNTTFFDP AGGGDPILQH LFWFFGHLK
//