ID A0A172QFW4_9CNID Unreviewed; 218 AA. AC A0A172QFW4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 17-JUN-2020, entry version 10. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375}; DE Flags: Fragment; GN Name=cox3 {ECO:0000313|EMBL:AND94745.1}; OS Staurotheca vanhoeffeni. OG Mitochondrion {ECO:0000313|EMBL:AND94745.1}. OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Leptothecata; OC Sertulariidae; Staurotheca. OX NCBI_TaxID=1848364 {ECO:0000313|EMBL:AND94745.1}; RN [1] {ECO:0000313|EMBL:AND94745.1} RP NUCLEOTIDE SEQUENCE. RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AND94745.1} RP NUCLEOTIDE SEQUENCE. RA Pena Cantero A.L., Sentandreu V.; RT "Phylogenetic relationships of endemic Antarctic species of Staurotheca RT Allman, 1888 (Cnidaria, Hydrozoa)."; RL Polar Biol. 0:0-0(2016). 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:RU003375}. 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; EC=7.1.1.9; CC Evidence={ECO:0000256|SAAS:SAAS01254563}; CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|RuleBase:RU003375, ECO:0000256|SAAS:SAAS00709834}. 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; KT824454; AND94745.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.20.120.80; -; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR033945; Cyt_c_oxase_su3_dom. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR PANTHER; PTHR11403; PTHR11403; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; SSF81452; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAAS:SAAS00709742, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:AND94745.1}; KW Translocase {ECO:0000256|SAAS:SAAS01254569}; KW Transmembrane {ECO:0000256|RuleBase:RU003375, KW ECO:0000256|SAAS:SAAS00709762, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00709799, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 23..41 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 62..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 110..130 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 142..162 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 182..203 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..218 FT /note="COX3" FT /evidence="ECO:0000259|PROSITE:PS50253" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AND94745.1" FT NON_TER 218 FT /evidence="ECO:0000313|EMBL:AND94745.1" SQ SEQUENCE 218 AA; 24210 MW; 217CBE3A1798EF91 CRC64; YVMGCAVFLT TLGAVIYFHY SQLFLFLLGL ISIIVCMFIW LKDVIREATY QGFHTLAAVK GLKMGFILFI ISEILFFVSF FWAFFHSSLS PSIEIGVIWP PTGINPLNPF SVPLLNTAIL LSSGATVTWA HHSIVSGEKS EALIGLSTTV ILGLIFTSLQ AFEYVEAPFC IADSVYGSTF FVATGFHGFH VIIGTIFLFV CLIRLNNSHF TRSHHFGF //