ID A0A1U9G5H2_CHLPG Unreviewed; 522 AA.
AC A0A1U9G5H2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 11-DEC-2019, entry version 8.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369};
GN Name=COX1 {ECO:0000313|EMBL:AOR40688.1};
OS Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
OG Mitochondrion {ECO:0000313|EMBL:AOR40688.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60710 {ECO:0000313|EMBL:AOR40688.1};
RN [1] {ECO:0000313|EMBL:AOR40688.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C8 {ECO:0000313|EMBL:AOR40688.1};
RA Dolotovskaya S., Torroba Bordallo J., Haus T., Zinner D., Roos C.;
RT "Mitogenomic Phylogeny of African Savanna Monkeys (Chlorocebus).";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. CO I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme A of subunit
CC 1 to the bimetallic center formed by heme A3 and copper B.
CC {ECO:0000256|RuleBase:RU000369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1;
CC Evidence={ECO:0000256|RuleBase:RU000369,
CC ECO:0000256|SAAS:SAAS01116628};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00939438}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU000369}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|RuleBase:RU000369}.
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DR EMBL; KU682698; AOR40688.1; -; 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:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR033944; 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 {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00939258};
KW Electron transport {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAAS:SAAS00711094};
KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161};
KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183};
KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163,
KW ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAAS:SAAS00711155};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:AOR40688.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAAS:SAAS00711097};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAAS:SAAS00711106};
KW Transmembrane {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711099}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..512
FT /note="COX1"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 522 AA; 57901 MW; A9AA26DC9863593C CRC64;
MFINRWLFST NHKDIGTLYL LFGAWAGITG TALSLLIRAE LGQPGSLLGS DHIYNVIVTA
HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRLNNM SFWLLPPSFL LLMASTMIEA
GAGTGWTVYP PLAGNLSHPG ASVDLVIFSL HLAGISSILG AINFITTIIN MKPPAMSQYQ
TPLFVWSVLI TAILLLLSLP VLAAGITMLL TDRNLNTTFF DPTGGGDPIL YQHLFWFFGH
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMTWAMMSI GFLGFIVWAH HMFTVGMDVD
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSAAMLW ALGFIFLFTM GGLTGIILAN
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF SGYTLDQTYA KAHFIIMFVG
VNLTFFPQHF LGLSGMPRRY SDYPDAYTTW NILSSIGSFI SLVAVILMIY MIWEAFASKR
KVSMTEQSPT NLEWLNGCPP PYHTFEEPAY IKLNEKGGSR TP
//