COX1_NEUCR
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-AUG-2022, entry version 139.
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 UniPathway; UPA00705; -.
DR Proteomes; UP000001805; Mitochondrion.
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: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:0009060; P:aerobic respiration; IBA:GO_Central.
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 GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 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; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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
