COX3_NEUCR
ID COX3_NEUCR Reviewed; 269 AA.
AC P00422; M1R9R0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
DE AltName: Full=Cytochrome c oxidase subunit Cox3 {ECO:0000303|PubMed:31316820};
GN Name=cox-3; Synonyms=cox3, oxi2; ORFNames=NCM012, NCU16003;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6279664; DOI=10.1016/s0021-9258(18)34663-5;
RA Browning K.S., RajBhandary U.L.;
RT "Cytochrome oxidase subunit III gene in Neurospora crassa mitochondria.
RT Location and sequence.";
RL J. Biol. Chem. 257:5253-5256(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA Kennell J.C., Collins R.A., Griffiths A.J.F., Nargang F.E.;
RT "Mitochondrial genetics of Neurospora.";
RL (In) Kueck U. (eds.);
RL The Mycota II, Genetics and Biotechnology (2nd edition), pp.95-112,
RL Springer-Verlag, Berlin-Heidelberg (2004).
RN [4]
RP AMINO-ACID COMPOSITION.
RX PubMed=4359388; DOI=10.1111/j.1432-1033.1973.tb03064.x;
RA Sebald W., Machleidt W., Otto J.;
RT "Products of mitochondrial protein synthesis in Neurospora crassa.
RT Determination of equimolar amounts of three products in cytochrome oxidase
RT on the basis of amino-acid analysis.";
RL Eur. J. Biochem. 38:311-324(1973).
RN [5]
RP SUBUNIT.
RX PubMed=17873079; DOI=10.1128/ec.00149-07;
RA Marques I., Dencher N.A., Videira A., Krause F.;
RT "Supramolecular organization of the respiratory chain in Neurospora crassa
RT mitochondria.";
RL Eukaryot. Cell 6:2391-2405(2007).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=31316820; DOI=10.1107/s2052252519007486;
RA Bausewein T., Nussberger S., Kuehlbrandt W.;
RT "Cryo-EM structure of Neurospora crassa respiratory complex IV.";
RL IUCrJ 6:773-780(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 Cox2 and heme A of Cox1 to the
CC active site in Cox1, a binuclear center (BNC) formed by heme A3 and
CC copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules
CC using 4 electrons from cytochrome c in the IMS and 4 protons from the
CC mitochondrial matrix. {ECO:0000250|UniProtKB:P00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 11 subunits. The complex is composed of
CC a catalytic core of 3 subunits Cox1, Cox2 and Cox3, encoded in the
CC mitochondrial DNA, and 8 supernumerary subunits Cox4, Cox5a/Cox5, Cox6,
CC Cox7, Cox8, Cox7a/Cox9, Cox6b/Cox12 and Cox6a/Cox13, which are encoded
CC in the nuclear genome (PubMed:31316820). The complex exists as a
CC monomer or a dimer and forms respiratory supercomplexes (SCs) in the
CC inner mitochondrial membrane with NADH-ubiquinone oxidoreductase
CC (complex I, CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome
CC b-c1 complex, complex III, CIII), resulting in various different
CC assemblies (supercomplexes I(1)IV(1), I(1)III(3)IV(2), III(2)IV(1) and
CC III(2)IV(2) as well as larger supercomplexes of compositions like
CC I(1)III(2)IV(5-6)) (PubMed:17873079). {ECO:0000269|PubMed:17873079,
CC ECO:0000269|PubMed:31316820}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:31316820}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:31316820}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; V00668; CAA24041.1; -; Genomic_DNA.
DR EMBL; KC683708; AGG15992.1; -; Genomic_DNA.
DR PIR; A00489; OTNC3.
DR RefSeq; YP_009126704.1; NC_026614.1.
DR AlphaFoldDB; P00422; -.
DR SMR; P00422; -.
DR STRING; 367110.P00422; -.
DR EnsemblFungi; AGG15992; AGG15992; NCU16003.
DR GeneID; 23681534; -.
DR KEGG; ncr:NCU16003; -.
DR VEuPathDB; FungiDB:NCU16003; -.
DR InParanoid; P00422; -.
DR Proteomes; UP000001805; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
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 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183813"
FT TOPO_DOM 1..22
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 42..48
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 74..80
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..114
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 115..137
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 162..164
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..188
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 189..201
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..230
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 231..248
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..265
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P00420"
FT TOPO_DOM 266..269
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30089 MW; DADCF118933781BC CRC64;
MTNLIRSNFQ DHPFHLVSPS PWPLNTSVCL LNLTTTGALS MHNFNNIHYL YYIALIGLVS
AMFLWFRDII SEGTFLGDHT LAVQRGLNLG IILFIVSEAL FFLAIFWAFF HSALTPTVEL
GAQWPPIGIE PVNPFELPLL NTVILLSSGA TITYAHHALI KGEREGALYG SIATILLAII
FTGFQGVEYS VSSFTISDGA FGTCFFFSTG FHGIHVIIGT IFLAVALWRI FAYHLTDNHH
VGFEGGILYW HFVDVVWLFL YISVYYWGS
