ID   A0A1W5G325_9PRIM        Unreviewed;       227 AA.
AC   A0A1W5G325;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   22-APR-2020, entry version 13.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709560};
GN   Name=COX2 {ECO:0000313|EMBL:ADP68443.1};
OS   Lepilemur hollandorum.
OG   Mitochondrion {ECO:0000313|EMBL:ADP68443.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Lepilemuridae; Lepilemur.
OX   NCBI_TaxID=886961 {ECO:0000313|EMBL:ADP68443.1};
RN   [1] {ECO:0000313|EMBL:ADP68443.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NARA8.5 {ECO:0000313|EMBL:ADP68443.1};
RX   PubMed=28173059; DOI=10.1093/jhered/esw072;
RA   Lei R., Frasier C.L., Hawkins M.T., Engberg S.E., Bailey C.A.,
RA   Johnson S.E., McLain A.T., Groves C.P., Perry G.H., Nash S.D.,
RA   Mittermeier R.A., Louis E.E.;
RT   "Phylogenomic Reconstruction of Sportive Lemurs (genus Lepilemur) Recovered
RT   from Mitogenomes with Inferences for Madagascar Biogeography.";
RL   J. Hered. 108:107-119(2017).
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:RU000457,
CC       ECO:0000256|SAAS:SAAS01246537}.
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;
CC         Evidence={ECO:0000256|SAAS:SAAS01246534};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000256|SAAS:SAAS01246534};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000457};
CC       Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709542}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU000457,
CC       ECO:0000256|SAAS:SAAS00709542}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709553}.
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DR   EMBL; HQ171085; ADP68443.1; -; Genomic_DNA.
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:InterPro.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
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   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 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00477878};
KW   Electron transport {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS01155864}; Magnesium {ECO:0000256|SAAS:SAAS01246526};
KW   Membrane {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00883094,
KW   ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00119299};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00709499, ECO:0000313|EMBL:ADP68443.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00709564};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01250488};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS01154861};
KW   Transmembrane {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00883111,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS01155879}.
FT   TRANSMEM        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..91
FT                   /note="COX2_TM"
FT                   /evidence="ECO:0000259|PROSITE:PS50999"
FT   DOMAIN          92..225
FT                   /note="COX2_CUA"
FT                   /evidence="ECO:0000259|PROSITE:PS50857"
SQ   SEQUENCE   227 AA;  25994 MW;  260627EBB0F79B06 CRC64;
     MACPVQLGFQ DATSPIMEEL LYFHDHTLMI VFLISSLVLY VISLMLTTKL THTNTVDAQG
     VEMVWTILPA VILILIALPS LRILYMMDEI TTPSLTLKTM GHQWYWSYEY TDYENLNFDS
     YMIPLSDLKP GELRLLEVDN RITLPTEMSI RMLISSEDVL HSWAVPSLGV KTDAIPGRLN
     QVTLMTSRPG IYYGQCSEIC GANHSFMPIV LELVPLKYFE EWLMIMF
//