ID A0A347ZJS0_9TELE Unreviewed; 232 AA. AC A0A347ZJS0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 08-MAY-2019, entry version 6. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709560}; GN Name=COII {ECO:0000313|EMBL:BBA85485.1}; OS Notacanthus chemnitzii (spiny eel). OG Mitochondrion {ECO:0000313|EMBL:BBA85485.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Notacanthiformes; OC Notacanthidae; Notacanthus. OX NCBI_TaxID=143895 {ECO:0000313|EMBL:BBA85485.1}; RN [1] {ECO:0000313|EMBL:BBA85485.1} RP NUCLEOTIDE SEQUENCE. RA Poulsen JY.; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BBA85485.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30044814; DOI=10.1371/journal.pone.0199982; RA Poulsen J.Y., Miller M.J., Sado T., Hanel R., Tsukamoto T., Miya M.; RT "Resolving deep-sea pelagic saccopharyngiform eel mysteries: RT Identification of Neocyema and Monognathidae leptocephali and RT establishment of a new fish family "Neocyematidae" based on larvae, RT adults and mitogenomic gene orders."; RL PLoS ONE 13:e0199982-e0199982(2018). 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 -!- 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}; CC Multi-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}. 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; AP018344; BBA85485.1; -; 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}; KW Membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00883094, 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:BBA85485.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709564}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS: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, KW ECO:0000256|SAAS:SAAS01155879}. FT TRANSMEM 27 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 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 232 AA; 26296 MW; ADB009D8010EA0A2 CRC64; MAHPSQLGFQ DAASPVMEEL LHFHDHALMI VFLISTLVVY IIVAMVTTKL TNKYILDSQE IEIIWTVLPA VILILIALPS LRILYLMDEI NDPHLTIKAM GHQWYWSYEY TDYEDLGFDS YMIPTQDLTP GQFRLLETDH RMVVPMEAPV RMLISAEDVL HSWAVPALGV KMDAVPGRLN QSAFIASRPG VYYGQCSEIC GANHSFMPIV VEAVPLQHFE NWSSLMMEDA SL //