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   24-JAN-2024, entry version 150.
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; 367110.P07142; -.
DR   PaxDb; 5141-EFNCRP00000009558; -.
DR   EnsemblFungi; EAA34520; EAA34520; NCU09816.
DR   GeneID; 3879905; -.
DR   KEGG; ncr:NCU09816; -.
DR   HOGENOM; CLU_040334_1_1_1; -.
DR   InParanoid; P07142; -.
DR   OrthoDB; 275461at2759; -.
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; Cytochrome c-like domain; 1.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 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; CYTOCHROME C1; 1.
DR   PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF02167; Cytochrom_C1; 1.
DR   PRINTS; PR00603; CYTOCHROMEC1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF81496; Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor; 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
//