ID   COX1_NEUCR              Reviewed;         557 AA.
AC   P03945; M1RV30;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-MAY-2023, entry version 142.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
DE   AltName: Full=Cytochrome c oxidase subunit Cox1 {ECO:0000303|PubMed:31316820};
GN   Name=cox-1; Synonyms=coi, cox1; ORFNames=NCM025, NCU16016;
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], AND PROTEIN SEQUENCE OF 3-99; 234-285;
RP   346-354; 443-489 AND 494-521.
RX   PubMed=6327266; DOI=10.1002/j.1460-2075.1982.tb01327.x;
RA   Burger G., Scriven C., Machleidt W., Werner S.;
RT   "Subunit 1 of cytochrome oxidase from Neurospora crassa: nucleotide
RT   sequence of the coding gene and partial amino acid sequence of the
RT   protein.";
RL   EMBO J. 1:1385-1391(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   DOI=10.1007/BF00365676;
RA   de Jonge J.C., de Vries H.;
RT   "The structure of the gene for subunit I of cytochrome c oxidase in
RT   Neurospora crassa mitochondria.";
RL   Curr. Genet. 7:21-28(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Adiopodoume / FGSC 430;
RX   PubMed=2531370; DOI=10.1093/nar/17.22.9087;
RA   Field D.J., Sommerfield A., Saville B.J., Collins R.A.;
RT   "A group II intron in the Neurospora mitochondrial coI gene: nucleotide
RT   sequence and implications for splicing and molecular evolution.";
RL   Nucleic Acids Res. 17:9087-9099(1989).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 519-557.
RX   PubMed=2949084; DOI=10.1016/0022-2836(86)90447-x;
RA   Burger G., Werner S.;
RT   "Mitochondrial gene URFN of Neurospora crassa codes for a long polypeptide
RT   with highly repetitive structure.";
RL   J. Mol. Biol. 191:589-599(1986).
RN   [7]
RP   MYRISTOYLATION AT LYS-324.
RX   PubMed=7567996; DOI=10.1073/pnas.92.19.8680;
RA   Vassilev A.O., Plesofsky-Vig N., Brambl R.;
RT   "Cytochrome c oxidase in Neurospora crassa contains myristic acid
RT   covalently linked to subunit 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8680-8684(1995).
RN   [8]
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   [9]
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:P00401}.
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:P00401};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds 2 heme A groups non-covalently per subunit.
CC       {ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00401}.
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   -!- PTM: The amino end of the mature protein may be Ser-3.
CC       {ECO:0000305|PubMed:6327266}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X01850; CAA25976.1; -; Genomic_DNA.
DR   EMBL; M36958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X14669; CAA32799.1; -; Genomic_DNA.
DR   EMBL; KC683708; AGG16005.1; -; Genomic_DNA.
DR   EMBL; X04512; CAA28195.1; -; Genomic_DNA.
DR   PIR; A00469; ODNC1.
DR   RefSeq; YP_009126717.1; NC_026614.1.
DR   AlphaFoldDB; P03945; -.
DR   SMR; P03945; -.
DR   STRING; 367110.P03945; -.
DR   iPTMnet; P03945; -.
DR   EnsemblFungi; AGG16005; AGG16005; NCU16016.
DR   GeneID; 23681570; -.
DR   KEGG; ncr:NCU16016; -.
DR   VEuPathDB; FungiDB:NCU16016; -.
DR   InParanoid; P03945; -.
DR   OrthoDB; 5387269at2759; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001805; Mitochondrion.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   1: Evidence at protein level;
KW   Calcium; Copper; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Reference proteome;
KW   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..557
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183366"
FT   TOPO_DOM        1..20
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        21..45
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        46..59
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        60..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        94..102
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        103..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        124..147
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        148..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        177..188
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        189..220
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        221..233
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        234..268
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        269..274
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        275..300
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        301..303
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        304..332
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        333..340
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        341..363
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        364..375
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        376..405
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        406..411
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        412..436
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        437..454
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TRANSMEM        455..479
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   TOPO_DOM        480..557
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:31316820"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         67
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         246
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         250
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         295
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         296
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         373
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with COX2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with COX2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         381
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_note="high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         383
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   LIPID           324
FT                   /note="N6-myristoyl lysine"
FT                   /evidence="ECO:0000269|PubMed:7567996"
FT   CROSSLNK        246..250
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   CONFLICT        527
FT                   /note="V -> A (in Ref. 1; CAA25976 and 3; CAA28195)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   557 AA;  61522 MW;  8AC9618704E5C91D CRC64;
     MSSISIWTER WFLSTNAKDI GVLYLIFALF SGLLGTAFSV LIRMELSGPG VQYIADNQLY
     NAIITAHAIL MIFFMVMPAL IGGFGNFLLP LLVGGPDMAF PRLNNISFWL LPPSLLLLVF
     SACIEGGAGT GWTIYPPLSG VQSHSGPSVD LAIFALHLSG VSSLLGSINF ITTIVNMRTP
     GIRLHKLALF GWAVVITAVL LLLSLPVLAG AITMLLTDRN FNTSFFETAG GGDPILFQHL
     FWFFGHPEVY ILIIPGFGII STTISAYSNK SVFGYIGMVY AMMSIGILGF IVWSHHMYTV
     GLDVDTRAYF TAATLIIAVP TGIKIFSWLA TCYGGSIRLT PSMLFALGFV FMFTIGGLSG
     VVLANASLDI AFHDTYYVVA HFHYVLSMGA VFAMFSGWYH WVPKILGLNY NMVLSKAQFW
     LLFIGVNLTF FPQHFLGLQG MPRRISDYPD AFSGWNLISS FGSIVSVVAS WLFLYIVYIQ
     LVQGEYAGRY PWSIPQFYTD SLRALLNRSY PSLEWSISSP PKPHSFVSLP LQSSSFFLSF
     FRLSSYGEQK EISGRQN
//