ID A0A0S0IGF3_ACAPO Unreviewed; 329 AA. AC A0A0S0IGF3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 24-JAN-2024, entry version 19. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|ARBA:ARBA00015944, ECO:0000256|RuleBase:RU003375}; GN Name=cox3 {ECO:0000313|EMBL:ALG41015.1}; OS Acanthamoeba polyphaga (Amoeba). OG Mitochondrion {ECO:0000313|EMBL:ALG41015.1}. OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida; OC Acanthamoebidae; Acanthamoeba. OX NCBI_TaxID=5757 {ECO:0000313|EMBL:ALG41015.1}; RN [1] {ECO:0000313|EMBL:ALG41015.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Linc Ap-1 {ECO:0000313|EMBL:ALG41015.1}; RX PubMed=31221647; RA Karlyshev A.V.; RT "Remarkable Features of Mitochondrial DNA of Acanthamoeba polyphaga Linc RT Ap-1, Revealed by Whole-Genome Sequencing."; RL Microbiol. Resour. Announc. 8:e00430-19(2019). 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|ARBA:ARBA00010581, ECO:0000256|RuleBase:RU003375}. 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; KP054475; ALG41015.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0S0IGF3; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 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:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1. DR PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1. DR Pfam; PF00510; COX3; 2. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:ALG41015.1}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003375}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 54..72 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 119..142 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 171..191 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 217..237 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 257..281 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 301..323 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 42..322 FT /note="Heme-copper oxidase subunit III family profile" FT /evidence="ECO:0000259|PROSITE:PS50253" SQ SEQUENCE 329 AA; 38843 MW; 2384486A69C20628 CRC64; MKLNYDFFLN KFSNVYNNDI RLVDLSNKWW YHNCRVHFAG NQKHSFHIVT RSPWPLYSSI AALMFTFGMV MHMHNYSYGN LLSLAGFLLI LLMMFVWWRD VIRESTFSGY HTKKVQQGLR LGVILFIISE VMFFFSFFWA FFHASLSPSV VLGSVWPPLG INVLNPLKIP LLNTLILLLS GLTVTWSHHV IRDKSWQKFF FSSTDNEEFK TPLLDNYVIC AFALFLTIFL GLEFTVWQGY EYYKASFYIY DGVYGSTFYM TTGLHGLHVI IGTLFLIVCF FRLIDLHFIY NHHFGYEAAI WYWHFVDVVW IFLFLSIYCW GSGVDSFFK //