ID A0A060IPI7_9TELE Unreviewed; 230 AA. AC A0A060IPI7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 04-MAR-2015, entry version 7. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457}; GN Name=COX2 {ECO:0000313|EMBL:AIC37356.1}; OS Megalobrama skolkovii. OG Mitochondrion {ECO:0000313|EMBL:AIC37356.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Megalobrama. OX NCBI_TaxID=75353 {ECO:0000313|EMBL:AIC37356.1}; RN [1] {ECO:0000313|EMBL:AIC37356.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24810068; RA Yang H., Li Q., Shu H., Yang L., Wu X., Yue L., Hou L.; RT "The complete mitochondrial genome of the Megalobrama skolkovii RT (Cyprinidae: Cultrinae)."; RL Mitochondrial DNA 0:0-0(2014). 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, ECO:0000256|SAAS:SAAS00057710}. CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457, CC ECO:0000256|SAAS:SAAS00169949}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457, CC ECO:0000256|SAAS:SAAS00169949}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00057545}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000457, CC ECO:0000256|SAAS:SAAS00057545}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {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; KJ630486; AIC37356.1; -; Genomic_DNA. DR RefSeq; YP_009045632.1; NC_024422.1. DR ProteinModelPortal; A0A060IPI7; -. DR GeneID; 19736791; -. 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:respiratory chain; 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 GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR014222; Cyt_c_oxidase_su2. DR InterPro; IPR002429; Cyt_c_oxidase_su2_C. 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:SAAS00106550}; KW Electron transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00119286}; KW Membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00119290}; KW Metal-binding {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00106558}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00057563}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00057661}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00044966}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00106619}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00106576}; KW Transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00119293}. SQ SEQUENCE 230 AA; 26049 MW; 03BA972CA55A636E CRC64; MAHPTQLGFQ DAASPVMEEL LHFHDHALMI VFLISTLVLY IIIAMVSTKL TNKYILDSQE IEIVWTILPA VILVLIALPS LRILYLMDEI NDPHLTIKAM GHQWYWSYEY TDYEDLGFDS YMIPTQDLTP GQFRLLETDH RMVVPMESPV RVLVSAEDVL HSWAVPSLGV KMDAVPGRLN QTAFIASRPG VFYGQCSEIC GANHSFMPIV VEAVPLEHFE SWSSLMLEDA //