COX2_NEUCR
ID COX2_NEUCR Reviewed; 250 AA.
AC P00411; M1R9T3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
DE AltName: Full=Cytochrome c oxidase subunit Cox2 {ECO:0000303|PubMed:31316820};
GN Name=cox-2; Synonyms=cox2, oxi1; ORFNames=NCM018, NCU16028;
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].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=6313689; DOI=10.1016/s0021-9258(17)44105-6;
RA Macino G., Morelli G.;
RT "Cytochrome oxidase subunit 2 gene in Neurospora crassa mitochondria.";
RL J. Biol. Chem. 258:13230-13235(1983).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RC STRAIN=RL3-8A;
RX PubMed=2976009; DOI=10.1093/genetics/120.4.935;
RA Almasan A., Mishra N.C.;
RT "Molecular characterization of the mitochondrial DNA of a new stopper
RT mutant ER-3 of Neurospora crassa.";
RL Genetics 120:935-945(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC STRAIN=ANT-1;
RX PubMed=6291999; DOI=10.1016/0014-5793(82)81019-3;
RA van den Boogaart P., van Dijk S., Agsteribbe E.;
RT "The mitochondrially made subunit 2 of Neurospora crassa cytochrome aa3 is
RT synthesized as a precursor protein.";
RL FEBS Lett. 147:97-100(1982).
RN [6]
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 [7]
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:P00410}.
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:P00410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC Note=Binds a dinuclear copper A center per subunit.
CC {ECO:0000250|UniProtKB:P00410};
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 2 family.
CC {ECO:0000305}.
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DR EMBL; K00825; AAA31959.2; -; Genomic_DNA.
DR EMBL; KC683708; AGG16017.1; -; Genomic_DNA.
DR EMBL; X14681; CAA32813.1; -; Genomic_DNA.
DR EMBL; J01429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A00479; OBNC2.
DR RefSeq; YP_009126729.1; NC_026614.1.
DR AlphaFoldDB; P00411; -.
DR SMR; P00411; -.
DR STRING; 367110.P00411; -.
DR EnsemblFungi; AGG16017; AGG16017; NCU16028.
DR GeneID; 23681583; -.
DR KEGG; ncr:NCU16028; -.
DR VEuPathDB; FungiDB:NCU16028; -.
DR InParanoid; P00411; -.
DR Proteomes; UP000001805; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:EnsemblFungi.
DR CDD; cd13912; CcO_II_C; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR034210; CcO_II_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 1: Evidence at protein level;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..250
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183638"
FT TOPO_DOM 1..27
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:31316820"
FT TRANSMEM 28..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:31316820"
FT TOPO_DOM 62..77
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:31316820"
FT TRANSMEM 78..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:31316820"
FT TOPO_DOM 108..250
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:31316820"
FT BINDING 185
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 220
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 220
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 222
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with COX1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 228
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 231
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT CONFLICT 50
FT /note="G -> V (in Ref. 1; AAA31959 and 4; CAA32813)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> D (in Ref. 1; AAA31959)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="G -> R (in Ref. 1; AAA31959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28555 MW; 7F8C8642EFAAB013 CRC64;
MGLLFNNLIM NFDAPSPWGI YFQDSATPQM EGLVELHDNI MYYLVVILFG VGWILLSIIR
NYISTKSPIS HKYLNHGTLI ELIWTITPAV ILILIAFPSF KLLYLMDEVS DPSMSVLAEG
HQWYWSYQYP DFLDSNDEFI EFDSYIVPES DLEEGALRML EVDNRVILPE LTHVRFIITA
GDVIHSFAVP SLGVKCDAYP GRLNQVSVFI NREGVFYGQC SEICGILHSS MPIVIESVSL
EKFLTWLEEQ
