ID A0A0N9GCA2_9ARAC Unreviewed; 195 AA.
AC A0A0N9GCA2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 11-DEC-2019, entry version 14.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE EC=1.9.3.1 {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: 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 -!- 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 Oxidoreductase {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
//