ID   A0A097C6W9_9COLE        Unreviewed;       219 AA.
AC   A0A097C6W9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COI {ECO:0000313|EMBL:AIS77891.1};
OS   Anisotoma humeralis.
OG   Mitochondrion {ECO:0000313|EMBL:AIS77891.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Staphyliniformia;
OC   Leiodidae; Leiodinae.
OX   NCBI_TaxID=355579 {ECO:0000313|EMBL:AIS77891.1};
RN   [1] {ECO:0000313|EMBL:ADW98119.1}
RP   NUCLEOTIDE SEQUENCE.
RG   International Barcode of Life (iBOL);
RT   "iBOL Data Release.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AIS77891.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25255319;
RA   Pentinsaari M., Hebert P.D., Mutanen M.;
RT   "Barcoding beetles: a regional survey of 1872 species reveals high
RT   identification success and unusually deep interspecific divergences.";
RL   PLoS ONE 9:E108651-E108651(2014).
RN   [3] {ECO:0000313|EMBL:AJA39373.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rougerie R.;
RT   "PASSIFOR: A reference library of DNA barcodes for French saproxylic
RT   beetles (Insecta, Coleoptera).";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AJB85687.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25469559; DOI=10.1111/1755-0998.12354;
RA   Hendrich L., Moriniere J., Haszprunar G., Hebert P.D., Hausmann A.,
RA   Kohler F., Balke M.;
RT   "A comprehensive DNA barcode database for Central European beetles with a
RT   focus on Germany: adding more than 3500 identified species to BOLD.";
RL   Mol. Ecol. Resour. 15:795-818(2015).
RN   [5] {ECO:0000313|EMBL:ARB55382.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rulik B., Ahrens D.;
RT   "Using taxonomic consistency with semi-automatized data pre-processing for
RT   high quality Barcode data submissions - a case study on German beetles.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:UDU88496.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=34562055;
RA   Roslin T., Somervuo P., Pentinsaari M., Hebert P.D.N., Agda J., Ahlroth P.,
RA   Anttonen P., Aspi J., Blagoev G., Blanco S., Chan D., Clayhills T.,
RA   deWaard J., deWaard S., Elliot T., Elo R., Haapala S., Helve E.,
RA   Ilmonen J., Hirvonen P., Ho C., Itamies J., Ivanov V., Jakovlev J.,
RA   Juslen A., Jussila R., Kahanpaa J., Kaila L., Kaitila J.P., Kakko A.,
RA   Kakko I., Karhu A., Karjalainen S., Kjaerandsen J., Koskinen J.,
RA   Laasonen E.M., Laasonen L., Laine E., Lampila P., Levesque-Beaudin V.,
RA   Lu L., Lahteenaro M., Majuri P., Malmberg S., Manjunath R., Martikainen P.,
RA   Mattila J., McKeown J., Metsala P., Miklasevskaja M., Miller M., Miskie R.,
RA   Muinonen A., Mukkala V.M., Naik S., Nikolova N., Nupponen K.,
RA   Ovaskainen O., Osterblad I., Paasivirta L., Pajunen T., Parkko P.,
RA   Paukkunen J., Penttinen R., Perez K., Pohjoismaki J., Prosser S.,
RA   Raekunnas M., Rahulan M., Rannisto M., Ratnasingham S., Raukko P.,
RA   Rinne A., Rintala T., Romo S.M., Salmela J., Salokannel J., Savolainen R.,
RA   Schulman L., Sihvonen P., Soliman D., Sones J., Steinke C., Stahls G.,
RA   Tabell J., Tiusanen M., Varkonyi G., Vesterinen E.J., Viitanen E.,
RA   Vikberg V., Viitasaari M., Vilen J., Warne C., Wei C., Winqvist K.,
RA   Zakharov E., Mutanen M.;
RT   "A molecular-based identification resource for the arthropods of Finland.";
RL   Mol. Ecol. Resour. 0:0-0(2021).
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|ARBA:ARBA00029331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000256|ARBA:ARBA00029331};
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   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of a catalytic core of 3 subunits and
CC       several supernumerary subunits. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC       complex, complex III, CIII). {ECO:0000256|ARBA:ARBA00011164}.
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|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000369}.
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DR   EMBL; HQ948251; ADW98119.1; -; Genomic_DNA.
DR   EMBL; HQ954453; ADW98322.1; -; Genomic_DNA.
DR   EMBL; HQ953298; ADX11761.1; -; Genomic_DNA.
DR   EMBL; KJ962141; AIS77057.1; -; Genomic_DNA.
DR   EMBL; KJ962690; AIS77606.1; -; Genomic_DNA.
DR   EMBL; KJ962975; AIS77891.1; -; Genomic_DNA.
DR   EMBL; KM286060; AJA39373.1; -; Genomic_DNA.
DR   EMBL; KM439972; AJB85687.1; -; Genomic_DNA.
DR   EMBL; KM443088; AJB88803.1; -; Genomic_DNA.
DR   EMBL; KM443591; AJB89306.1; -; Genomic_DNA.
DR   EMBL; KM451176; AJB96891.1; -; Genomic_DNA.
DR   EMBL; KM452262; AJB97977.1; -; Genomic_DNA.
DR   EMBL; KU908962; ARB55382.1; -; Genomic_DNA.
DR   EMBL; KU910541; ARB56961.1; -; Genomic_DNA.
DR   EMBL; KU911936; ARB58356.1; -; Genomic_DNA.
DR   EMBL; KU911943; ARB58363.1; -; Genomic_DNA.
DR   EMBL; KU915090; ARB61510.1; -; Genomic_DNA.
DR   EMBL; KU916466; ARB62886.1; -; Genomic_DNA.
DR   EMBL; KU918362; ARB64782.1; -; Genomic_DNA.
DR   EMBL; MZ659194; UDU88496.1; -; Genomic_DNA.
DR   EMBL; MZ659768; UDU89070.1; -; 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: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:AIS77891.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..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..219
FT                   /note="COX1"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AIS77891.1"
FT   NON_TER         219
FT                   /evidence="ECO:0000313|EMBL:AIS77891.1"
SQ   SEQUENCE   219 AA;  23597 MW;  F503CE3F85564173 CRC64;
     TLYFIFGAWS GMVGTSLSIL IRAELGTPGS LIGDDQIYNV IVTAHAFVMI FFMVMPIMIG
     GFGNWLVPLM LGAPDMAFPR MNNMSFWLLP PSLTLLLMSS MVENGAGTGW TVYPPLSANI
     SHSGSSVDLA IFSLHLAGIS SILGAVNFIT TVINMRSIGM TFDKMPLFVW SVVITALLLL
     LSLPVLAGAI TMLLTDRNLN TSFFDPAGGG DPILYQHLF
//