ID   COX13_NEUCR             Reviewed;         136 AA.
AC   V5IRD7;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Cytochrome c oxidase subunit 13, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIa;
DE   AltName: Full=Cytochrome c oxidase subunit Cox6a {ECO:0000303|PubMed:31316820};
DE   AltName: Full=Encodes anonymous transcript-5 protein;
DE   Flags: Precursor;
GN   Name=eat-5; ORFNames=NCU01962;
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   COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX.
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   [3]
RP   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:P32799}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P32799}.
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). Cox6a/Cox13 was not present in
CC       the cryo-EM structure. It may be involved in complex IV dimer formation
CC       and might not be always expressed. This would explain its absence in
CC       the map of the isolated monomer (Probable).
CC       {ECO:0000269|PubMed:17873079, ECO:0000269|PubMed:31316820,
CC       ECO:0000305|PubMed:31316820}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:31316820}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:31316820}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.
CC       {ECO:0000305}.
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DR   EMBL; CM002236; ESA43841.1; -; Genomic_DNA.
DR   RefSeq; XP_011392913.1; XM_011394611.1.
DR   AlphaFoldDB; V5IRD7; -.
DR   SMR; V5IRD7; -.
DR   STRING; 5141.EFNCRP00000001261; -.
DR   EnsemblFungi; ESA43841; ESA43841; NCU01962.
DR   GeneID; 3880491; -.
DR   VEuPathDB; FungiDB:NCU01962; -.
DR   HOGENOM; CLU_122515_0_0_1; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0097250; P:mitochondrial respirasome assembly; IEA:EnsemblFungi.
DR   CDD; cd00925; Cyt_c_Oxidase_VIa; 1.
DR   Gene3D; 4.10.95.10; -; 1.
DR   InterPro; IPR001349; Cyt_c_oxidase_su6a.
DR   InterPro; IPR036418; Cyt_c_oxidase_su6a_sf.
DR   PANTHER; PTHR11504; PTHR11504; 1.
DR   Pfam; PF02046; COX6A; 1.
DR   SUPFAM; SSF81411; SSF81411; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..136
FT                   /note="Cytochrome c oxidase subunit 13, mitochondrial"
FT                   /id="PRO_0000448903"
FT   TOPO_DOM        30..62
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        84..136
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
SQ   SEQUENCE   136 AA;  16043 MW;  E93AE751E47DE514 CRC64;
     MFAQRQMFFA RLAANLRAPA VRQTVQRRFA STPANESGKN AFVREREAVK QHAAETTELW
     RKISLYGIPP ALALAGYNAY TLYNEHWEHW SHLPPLEERT EYPYQNIRTR NYPWGDGDKT
     LFWNESVNYH NRDKVT