ID S0ASK7_FICAL Unreviewed; 519 AA.
AC S0ASK7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369};
GN Name=cox1 {ECO:0000313|EMBL:AGO65339.1};
GN Synonyms=COX1 {ECO:0000313|EMBL:QOD98109.1,
GN ECO:0000313|Ensembl:ENSFALP00000015973.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OG Mitochondrion {ECO:0000313|EMBL:AGO65339.1,
OG ECO:0000313|Ensembl:ENSFALP00000015973.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|EMBL:AGO65339.1};
RN [1] {ECO:0000313|EMBL:AGO65339.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OC2 {ECO:0000313|EMBL:AGO65339.1};
RX PubMed=24923674;
RA Ekblom R., Smeds L., Ellegren H.;
RT "Patterns of sequencing coverage bias revealed by ultra-deep sequencing of
RT vertebrate mitochondria.";
RL BMC Genomics 15:467-467(2014).
RN [2] {ECO:0000313|EMBL:QOD98109.1}
RP NUCLEOTIDE SEQUENCE.
RG B10K project Consortium;
RA Feng S., Stiller J., Andreu-Sanchez S., Margaryan A., Chen W., Paten B.,
RA Zhang G.;
RT "Densely sampling genomes across the diversity of birds increases power of
RT comparative genomics analyses.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFALP00000015973.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000256|RuleBase:RU000369};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane
CC protein {ECO:0000256|RuleBase:RU000369}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000369}.
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DR EMBL; KF293721; AGO65339.1; -; Genomic_DNA.
DR EMBL; MN356390; QOD98109.1; -; Genomic_DNA.
DR RefSeq; YP_008144959.1; NC_021621.1.
DR STRING; 59894.ENSFALP00000015973; -.
DR Ensembl; ENSFALT00000016925.1; ENSFALP00000015973.1; ENSFALG00000016245.1.
DR GeneID; 16027872; -.
DR KEGG; fab:16027872; -.
DR CTD; 4512; -.
DR eggNOG; KOG4769; Eukaryota.
DR GeneTree; ENSGT00390000001518; -.
DR HOGENOM; CLU_011899_7_3_1; -.
DR OMA; WAMMSIG; -.
DR OrthoDB; 5387269at2759; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000016665; Mitochondrion.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl.
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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Copper {ECO:0000256|RuleBase:RU000369};
KW Electron transport {ECO:0000256|RuleBase:RU000369};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000369};
KW Iron {ECO:0000256|RuleBase:RU000369};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369};
KW Metal-binding {ECO:0000256|RuleBase:RU000369};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AGO65339.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000369};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..515
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 519 AA; 57150 MW; 66B5A20CFC193251 CRC64;
MLPVTFINRW LFSTNHKDIG TLYLIFGAWA GMVGTALSLL IRAELGQPGA LLGDDQVYNV
VVTAHAFVMI FFMVMPIMIG GFGNWLVPLM IGAPDMAFPR MNNMSFWLLP PSFLLLLASS
TVEAGVGTGW TVYPPLAGNL AHAGASVDLA IFSLHLAGIS SILGAINFIT TAINMKPPAL
SQYQTPLFVW SVLITAVLLL LSLPVLAAGI TMLLTDRNLN TTFFDPAGGG DPVLYQHLFW
FFGHPEVYIL ILPGFGIISH VVAYYAGKKE PFGYMGMVWA MLSIGFLGFI VWAHHMFTVG
MDVDTRAYFT SATMIIAIPT GIKVFSWLAT LHGGTIKWDP PMLWALGFIF LFTIGGLTGI
VLANSSLDIA LHDTYYVVAH FHYVLSMGAV FAILAGFTHW FPLFTGYTLH STWAKAHFGV
MFVGVNLTFF PQHFLGLAGM PRRYSDYPDA YTLWNTISSI GSLISLTAVI MLVFIIWEAF
ASKRKAFQPE LTSTNIEWIH GCPPPFHTFE EPAFVQVQE
//
