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COX2_ANOGA
ID   COX2_ANOGA              Reviewed;         228 AA.
AC   P34840; A6MCV5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
GN   Name=COII;
OS   Anopheles gambiae (African malaria mosquito).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17270468; DOI=10.1016/j.ympev.2006.12.005;
RA   Roe A.D., Sperling F.A.;
RT   "Patterns of evolution of mitochondrial cytochrome c oxidase I and II DNA
RT   and implications for DNA barcoding.";
RL   Mol. Phylogenet. Evol. 44:325-345(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3;
RX   PubMed=9087549; DOI=10.1111/j.1365-2583.1993.tb00131.x;
RA   Beard C.B., Hamm D.M., Collins F.H.;
RT   "The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence,
RT   genome organization, and comparisons with mitochondrial sequences of other
RT   insects.";
RL   Insect Mol. Biol. 2:103-124(1993).
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:0000250|UniProtKB:P00410}.
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:0000250|UniProtKB:P00410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00410};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00410};
CC       Note=Binds a dinuclear copper A center per subunit.
CC       {ECO:0000250|UniProtKB:P00410};
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:0000250|UniProtKB:P00410}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00410}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ792577; ABH07858.1; -; Genomic_DNA.
DR   EMBL; DQ792578; ABH07860.1; -; Genomic_DNA.
DR   EMBL; L20934; AAD12192.1; -; Genomic_DNA.
DR   PIR; T09802; T09802.
DR   RefSeq; NP_008071.1; NC_002084.1.
DR   AlphaFoldDB; P34840; -.
DR   SMR; P34840; -.
DR   STRING; 7165.AGAP028366-PA; -.
DR   GeneID; 1267415; -.
DR   KEGG; aga:COX2; -.
DR   CTD; 4513; -.
DR   VEuPathDB; VectorBase:AGAP028366; -.
DR   eggNOG; KOG4767; Eukaryota.
DR   HOGENOM; CLU_036876_2_3_1; -.
DR   InParanoid; P34840; -.
DR   OMA; WSYEYTD; -.
DR   OrthoDB; 1432833at2759; -.
DR   Proteomes; UP000007062; Mitochondrion.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR045187; CcO_II.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR034210; CcO_II_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   TIGRFAMs; TIGR02866; CoxB; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..228
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000183494"
FT   TOPO_DOM        1..26
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..62
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..228
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   BINDING         161
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         196
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         196
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         198
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         200
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         200
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         204
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         207
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
SQ   SEQUENCE   228 AA;  26222 MW;  CFF0D681E9ACC99F CRC64;
     MATWANLGLQ DSSSPLMEQL NFFHDHTLLI LTMITILVGY IMGMLSFNKF TNRFLLHGQT
     IEIIWTVLPA IILMFIAFPS LRLLYLMDEI NTPSITLKSI GHQWYWSYEY SDFLNLEFDS
     YMVPTNELET NGFRLLDVDN RVVLPMNNQI RILVTATDVL HSWTVPSLGV KVDATPGRLN
     QLNFLINRPG LFFGQCSEIC GANHSFMPIV IESIPMNYFI KWITSMTN
 
 
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