COX4_NEUCR
ID COX4_NEUCR Reviewed; 186 AA.
AC P06809; Q7SBP9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cytochrome c oxidase subunit 4, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide IV;
DE AltName: Full=Cytochrome c oxidase subunit Cox4 {ECO:0000303|PubMed:31316820};
DE Flags: Precursor;
GN Name=cox-4; ORFNames=NCU05689;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-45.
RX PubMed=3001085; DOI=10.1016/s0021-9258(17)36176-8;
RA Sachs M.S., David M., Werner S., RajBhandary U.L.;
RT "Nuclear genes for cytochrome c oxidase subunits of Neurospora crassa.
RT Isolation and characterization of cDNA clones for subunits IV, V, VI, and
RT possibly VII.";
RL J. Biol. Chem. 261:869-873(1986).
RN [3]
RP COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [4]
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:P04037}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04037}.
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}; Peripheral membrane protein
CC {ECO:0000269|PubMed:31316820}; Matrix side
CC {ECO:0000269|PubMed:31316820}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family.
CC {ECO:0000305}.
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DR EMBL; CM002238; EAA33815.1; -; Genomic_DNA.
DR EMBL; M12116; AAA33574.1; -; Genomic_DNA.
DR PIR; A25629; A25629.
DR RefSeq; XP_963051.1; XM_957958.3.
DR AlphaFoldDB; P06809; -.
DR SMR; P06809; -.
DR STRING; 5141.EFNCRP00000007638; -.
DR EnsemblFungi; EAA33815; EAA33815; NCU05689.
DR GeneID; 3879200; -.
DR KEGG; ncr:NCU05689; -.
DR VEuPathDB; FungiDB:NCU05689; -.
DR HOGENOM; CLU_091071_0_0_1; -.
DR InParanoid; P06809; -.
DR OMA; DHKPYWM; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:EnsemblFungi.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:EnsemblFungi.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IEA:EnsemblFungi.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 32..186
FT /note="Cytochrome c oxidase subunit 4, mitochondrial"
FT /id="PRO_0000006112"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04037"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04037"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04037"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04037"
FT CONFLICT 16
FT /note="A -> R (in Ref. 2; AAA33574)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..45
FT /note="HIKRLS -> PHQASL (in Ref. 2; AAA33574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 20613 MW; 7E8675B3E879E505 CRC64;
MLLSRTAVAV ARRATAAPAL RRSIATTVVR CNAETKPVPH IKRLSEIKTK DDLFGPGAAP
GTVPTDLEQA TGLERLEILG KMEGVDVFDM KPLDASRRGT MENPISVRSA GDEQYAGCTG
FPADSHNVIW LTMTRERPVE RCPECGNVYK MDYVGPQDDH AHDHGHDHHG FEEPKTFADY
VKPEYW
