ID A0A1W5G325_9PRIM Unreviewed; 227 AA. AC A0A1W5G325; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 14-DEC-2022, entry version 21. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|ARBA:ARBA00015946, ECO:0000256|RuleBase:RU000457}; 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 -!- 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=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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000457}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007866, ECO:0000256|RuleBase:RU000457}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HQ171085; ADP68443.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1W5G325; -. 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 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; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000457}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000457}; Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000457}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000457}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, ECO:0000313|EMBL:ADP68443.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000457}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000457}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000457}. 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 //