ID   COX5_NEUCR              Reviewed;         171 AA.
AC   P06810; Q7RVI9;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Cytochrome c oxidase subunit 5, mitochondrial;
DE   AltName: Full=Cytochrome a-4 protein;
DE   AltName: Full=Cytochrome c oxidase polypeptide V;
DE   AltName: Full=Cytochrome c oxidase subunit Cox5a {ECO:0000303|PubMed:31316820};
DE   Flags: Precursor;
GN   Name=cya-4; ORFNames=B8B20.30, NCU05457;
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 [GENOMIC DNA].
RX   PubMed=2540423; DOI=10.1128/mcb.9.2.566-577.1989;
RA   Sachs M.S., Bertrand H., Metzenberg R.L., RajBhandary U.L.;
RT   "Cytochrome oxidase subunit V gene of Neurospora crassa: DNA sequences,
RT   chromosomal mapping, and evidence that the cya-4 locus specifies the
RT   structural gene for subunit V.";
RL   Mol. Cell. Biol. 9:566-577(1989).
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=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
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   [5]
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   [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:P00424}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00424}.
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:0000250|UniProtKB:P00424}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00424}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
CC       {ECO:0000305}.
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DR   EMBL; M24389; AAA31957.2; -; Genomic_DNA.
DR   EMBL; AL355933; CAB91450.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34212.1; -; Genomic_DNA.
DR   EMBL; M12117; AAA33575.1; -; Genomic_DNA.
DR   PIR; A30134; OTNCV.
DR   RefSeq; XP_963448.1; XM_958355.2.
DR   AlphaFoldDB; P06810; -.
DR   SMR; P06810; -.
DR   STRING; 367110.P06810; -.
DR   PaxDb; 5141-EFNCRP00000006586; -.
DR   EnsemblFungi; EAA34212; EAA34212; NCU05457.
DR   GeneID; 3879597; -.
DR   KEGG; ncr:NCU05457; -.
DR   VEuPathDB; FungiDB:NCU05457; -.
DR   HOGENOM; CLU_070101_2_0_1; -.
DR   InParanoid; P06810; -.
DR   OMA; YVIHLFA; -.
DR   OrthoDB; 36553at2759; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   CDD; cd00922; Cyt_c_Oxidase_IV; 1.
DR   Gene3D; 1.10.442.10; Cytochrome c oxidase subunit IV; 1.
DR   InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR   InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR   PANTHER; PTHR10707:SF10; CYTOCHROME C OXIDASE SUBUNIT 4; 1.
DR   PANTHER; PTHR10707; CYTOCHROME C OXIDASE SUBUNIT IV; 1.
DR   Pfam; PF02936; COX4; 1.
DR   SUPFAM; SSF81406; Mitochondrial cytochrome c oxidase subunit IV; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..171
FT                   /note="Cytochrome c oxidase subunit 5, mitochondrial"
FT                   /id="PRO_0000006095"
FT   TOPO_DOM        28..100
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00424"
FT   TRANSMEM        101..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..171
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00424"
FT   REGION          145..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   171 AA;  18804 MW;  5E866BE18B59440D CRC64;
     MLRTPTVSAL VRNVAVRAAK PTMAVRAAST MPISNPTLAN IEKRWEQMPM QEQAELWMAL
     RDRMKGNWAD LTLQEKKAAY YIAFGPHGPR ALPPPGEQKK VLAYTVAGVF LSFVIFATMR
     AFAKPPPATM TKEWQEATNE FLKAQKSDPL TGLTSEGYNG KGHVQSPSAS A
//