ID A0A1W5G325_9PRIM Unreviewed; 227 AA. AC A0A1W5G325; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 30-AUG-2017, entry version 2. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lemuriformes; 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=.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) RT Recovered from Mitogenomes with Inferences for Madagascar RT Biogeography."; RL J. Hered. 108:107-119(2017). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. Subunit 2 CC transfers the electrons from cytochrome c via its binuclear copper CC A center to the bimetallic center of the catalytic subunit 1. CC {ECO:0000256|RuleBase:RU000457}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|SAAS:SAAS00709542}; Multi-pass membrane protein 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}. 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 GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR CDD; cd13912; CcO_II_C; 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 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:SAAS00517791}; KW Electron transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00517827}; KW Membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00809509, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00517846}; 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 Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709567}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00809546, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00809553, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00517787}. FT TRANSMEM 27 46 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 85 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 91 COX2_TM. {ECO:0000259|PROSITE:PS50999}. FT DOMAIN 92 225 COX2_CUA. {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 //