ID A0A0N9GCA2_9ARAC Unreviewed; 195 AA.
AC A0A0N9GCA2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 17-JUN-2020, entry version 16.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE Flags: Fragment;
GN Name=COI {ECO:0000313|EMBL:ALF74431.1};
OS Rilaena triangularis.
OG Mitochondrion {ECO:0000313|EMBL:ALF74431.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Opiliones; Palpatores; Phalangioidea; Phalangiidae; Rilaena.
OX NCBI_TaxID=475616 {ECO:0000313|EMBL:ALF74431.1};
RN [1] {ECO:0000313|EMBL:ALF74431.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26379469;
RA Telfer A.C., Young M.R., Quinn J., Perez K., Sobel C.N., Sones J.E.,
RA Levesque-Beaudin V., Derbyshire R., Fernandez-Triana J., Rougerie R.,
RA Thevanayagam A., Boskovic A., Borisenko A.V., Cadel A., Brown A., Pages A.,
RA Castillo A.H., Nicolai A., Glenn Mockford B.M., Bukowski B., Wilson B.,
RA Trojahn B., Lacroix C.A., Brimblecombe C., Hay C., Ho C., Steinke C.,
RA Warne C.P., Garrido Cortes C., Engelking D., Wright D., Lijtmaer D.A.,
RA Gascoigne D., Hernandez Martich D., Morningstar D., Neumann D., Steinke D.,
RA Marco DeBruin D.D., Dobias D., Sears E., Richard E., Damstra E.,
RA Zakharov E.V., Laberge F., Collins G.E., Blagoev G.A., Grainge G.,
RA Ansell G., Meredith G., Hogg I., McKeown J., Topan J., Bracey J.,
RA Guenther J., Sills-Gilligan J., Addesi J., Persi J., Layton K.K.,
RA D'Souza K., Dorji K., Grundy K., Nghidinwa K., Ronnenberg K., Lee K.M.,
RA Xie L., Lu L., Penev L., Gonzalez M., Rosati M.E., Kekkonen M., Kuzmina M.,
RA Iskandar M., Mutanen M., Fatahi M., Pentinsaari M., Bauman M., Nikolova N.,
RA Ivanova N.V., Jones N., Weerasuriya N., Monkhouse N., Lavinia P.D.,
RA Jannetta P., Hanisch P.E., McMullin R.T., Ojeda Flores R., Mouttet R.,
RA Vender R., Labbee R.N., Forsyth R., Lauder R., Dickson R., Kroft R.,
RA Miller S.E., MacDonald S., Panthi S., Pedersen S., Sobek-Swant S., Naik S.,
RA Lipinskaya T., Eagalle T., Decaens T., Kosuth T., Braukmann T.,
RA Woodcock T., Roslin T., Zammit T., Campbell V., Dinca V., Peneva V.,
RA Hebert P.D., deWaard J.R.;
RT "Biodiversity inventories in high gear: DNA barcoding facilitates a rapid
RT biotic survey of a temperate nature reserve.";
RL Biodivers Data J 3:E6313-E6313(2015).
RN [2] {ECO:0000313|EMBL:ALF74431.1}
RP NUCLEOTIDE SEQUENCE.
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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] + 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=7.1.1.9;
CC Evidence={ECO:0000256|RuleBase:RU000369};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|RuleBase:RU000369}.
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; KT703079; ALF74431.1; -; 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:respirasome; IEA:UniProtKB-KW.
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 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 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 {ECO:0000256|RuleBase:RU000369};
KW Electron transport {ECO:0000256|RuleBase:RU000369};
KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369};
KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000369};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:ALF74431.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000369}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..195
FT /note="Cytochrome c oxidase subunit 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006035096"
FT TRANSMEM 42..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..195
FT /note="COX1"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALF74431.1"
FT NON_TER 195
FT /evidence="ECO:0000313|EMBL:ALF74431.1"
SQ SEQUENCE 195 AA; 21166 MW; AA59BD2ADCBB8195 CRC64;
SMYMIFGMWA AMVGTALSMX IRTELGQPGS LMNDDQIYNV IVTAHAFVMI FFMVMPIMIG
GFGNWLVPLM LGAPDMAFPR LNNMSFWLLP PSFLLLLSSA LVENGAGTGW TVYPPLSSNI
AHTGASVDLT IFSLHLAGVS SILGAINFIT TIIXMRTQGM ILERMPLFVW SVKITAILLL
LSLPVLAGAI TMLLT
//