CY1_NEUCR
ID CY1_NEUCR Reviewed; 332 AA.
AC P07142; Q7SCQ1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cytochrome c1, heme protein, mitochondrial;
DE EC=7.1.1.8 {ECO:0000269|PubMed:1847681, ECO:0000269|PubMed:3015618};
DE AltName: Full=Complex III subunit 4;
DE AltName: Full=Complex III subunit IV {ECO:0000303|PubMed:6302289};
DE AltName: Full=Cytochrome b-c1 complex subunit 4;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase complex cytochrome c1 subunit;
DE Short=Cytochrome c-1;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 31 kDa protein;
DE Flags: Precursor;
GN Name=cyt-1; ORFNames=NCU09816;
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 [MRNA].
RX PubMed=3030747; DOI=10.1111/j.1432-1033.1987.tb11000.x;
RA Roemisch J., Tropschug M., Sebald W., Weiss H.;
RT "The primary structure of cytochrome c1 from Neurospora crassa.";
RL Eur. J. Biochem. 164:111-115(1987).
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 PROTEIN SEQUENCE OF N-TERMINUS.
RA Tsugita A., Gregor J., Kubota J., Van der Broek R.;
RL (In) King T.E., Ovii Y., Chance B., Okonuki K. (eds.);
RL Cytochrome oxidase, pp.67-77, Elsevier, New York (1979).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=226365; DOI=10.1111/j.1432-1033.1979.tb13240.x;
RA Weiss H., Kolb H.J.;
RT "Isolation of mitochondrial succinate: ubiquinone reductase, cytochrome c
RT reductase and cytochrome c oxidase from Neurospora crassa using nonionic
RT detergent.";
RL Eur. J. Biochem. 99:139-149(1979).
RN [5]
RP SUBUNIT.
RX PubMed=6273583; DOI=10.1016/0022-2836(81)90301-6;
RA Leonard K., Wingfield P., Arad T., Weiss H.;
RT "Three-dimensional structure of ubiquinol:cytochrome c reductase from
RT Neurospora mitochondria determined by electron microscopy of membrane
RT crystals.";
RL J. Mol. Biol. 149:259-274(1981).
RN [6]
RP SUBUNIT.
RX PubMed=18251112; DOI=10.1007/bf00744526;
RA Mendel-Hartvig I., Nelson B.D.;
RT "Comparative study of the peptide composition of Complex III (quinol-
RT cytochrome c reductase).";
RL J. Bioenerg. Biomembr. 15:289-299(1983).
RN [7]
RP SUBUNIT.
RX PubMed=6302289; DOI=10.1016/s0022-2836(83)80258-7;
RA Karlsson B., Hovmoeller S., Weiss H., Leonard K.;
RT "Structural studies of cytochrome reductase. Subunit topography determined
RT by electron microscopy of membrane crystals of a subcomplex.";
RL J. Mol. Biol. 165:287-302(1983).
RN [8]
RP FUNCTION OF COMPLEX III.
RX PubMed=3015618; DOI=10.1111/j.1432-1033.1986.tb09799.x;
RA Linke P., Bechmann G., Gothe A., Weiss H.;
RT "Dimeric ubiquinol:cytochrome c reductase of Neurospora mitochondria
RT contains one cooperative ubiquinone-reduction centre.";
RL Eur. J. Biochem. 158:615-621(1986).
RN [9]
RP FUNCTION OF COMPLEX III.
RX PubMed=1847681; DOI=10.1111/j.1432-1033.1991.tb15722.x;
RA Bechmann G., Weiss H.;
RT "Regulation of the proton/electron stoichiometry of mitochondrial
RT ubiquinol:cytochrome c reductase by the membrane potential.";
RL Eur. J. Biochem. 195:431-438(1991).
RN [10]
RP COMPOSITION OF THE RESPIRATORY COMPLEX III, 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 [11]
RP FUNCTION OF COMPLEX III, AND SUBUNIT.
RX PubMed=19239619; DOI=10.1111/j.1365-2958.2009.06643.x;
RA Duarte M., Videira A.;
RT "Effects of mitochondrial complex III disruption in the respiratory chain
RT of Neurospora crassa.";
RL Mol. Microbiol. 72:246-258(2009).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c (PubMed:3015618) (Probable). Cytochrome c1 is a
CC catalytic core subunit containing a c-type heme. It transfers electrons
CC from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to
CC cytochrome c (By similarity). {ECO:0000250|UniProtKB:P07143,
CC ECO:0000269|PubMed:3015618, ECO:0000305|PubMed:1847681,
CC ECO:0000305|PubMed:19239619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1847681,
CC ECO:0000269|PubMed:3015618};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:P07143};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:P07143};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (cob), cytochrome c1 (cyt-1) and Rieske protein
CC (fes-1), 2 core protein subunits pep and ucr-1, and 5 low-molecular
CC weight protein subunits qcr6, qcr7, qcr8, qcr9 and probably
CC NCU16844/qcr10 (PubMed:226365, PubMed:6273583, PubMed:18251112,
CC PubMed:6302289). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase
CC (complex IV, CIV), resulting in different assemblies (supercomplexes
CC SCI(1)III(2), SCIII(2)IV(1) and SCIII(2)IV(2) as well as higher order
CC I(x)III(y)IV(z) megacomplexes) (PubMed:17873079, PubMed:19239619).
CC {ECO:0000269|PubMed:17873079, ECO:0000269|PubMed:18251112,
CC ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:226365,
CC ECO:0000269|PubMed:6273583, ECO:0000269|PubMed:6302289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:226365}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA34520.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X05235; CAA28860.1; -; mRNA.
DR EMBL; CM002236; EAA34520.1; ALT_FRAME; Genomic_DNA.
DR PIR; A27187; A27187.
DR RefSeq; XP_963756.1; XM_958663.3.
DR AlphaFoldDB; P07142; -.
DR SMR; P07142; -.
DR STRING; 5141.EFNCRP00000009558; -.
DR PRIDE; P07142; -.
DR EnsemblFungi; EAA34520; EAA34520; NCU09816.
DR GeneID; 3879905; -.
DR KEGG; ncr:NCU09816; -.
DR HOGENOM; CLU_040334_1_1_1; -.
DR InParanoid; P07142; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR PANTHER; PTHR10266; PTHR10266; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF81496; SSF81496; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..70
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 71..332
FT /note="Cytochrome c1, heme protein, mitochondrial"
FT /id="PRO_0000006556"
FT TOPO_DOM 71..277
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT TRANSMEM 278..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..332
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT DOMAIN 97..250
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 139..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 113
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 114
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 234
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P07143"
SQ SEQUENCE 332 AA; 36456 MW; 3AAFCCE896E8D4DB CRC64;
MLARTCLRST RTFASAKNGA FKFAKRSAST QSSGAAAESP LRLNIAAAAA TAVAAGSIAW
YYHLYGFASA MTPAEEGLHA TKYPWVHEQW LKTFDHQALR RGFQVYREVC ASCHSLSRVP
YRALVGTILT VDEAKALAEE NEYDTEPNDQ GEIEKRPGKL SDYLPDPYKN DEAARFANNG
ALPPDLSLIV KARHGGCDYI FSLLTGYPDE PPAGASVGAG LNFNPYFPGT GIAMARVLYD
GLVDYEDGTP ASTSQMAKDV VEFLNWAAEP EMDDRKRMGM KVLVVTSVLF ALSVYVKRYK
WAWLKSRKIV YDPPKSPPPA TNLALPQQRA KS
