ID   CYC_NEUCR               Reviewed;         108 AA.
AC   P00048; Q7RV53;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Cytochrome c;
GN   Name=cyc-1; Synonyms=cyt-12; ORFNames=B1K11.020, NCU01808;
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 [GENOMIC DNA / MRNA], AND VARIANT ASP-11.
RC   STRAIN=74A;
RX   PubMed=2820723; DOI=10.1002/j.1460-2075.1987.tb02480.x;
RA   Stuart R.A., Neupert W., Tropschug M.;
RT   "Deficiency in mRNA splicing in a cytochrome c mutant of Neurospora crassa:
RT   importance of carboxy terminus for import of apocytochrome c into
RT   mitochondria.";
RL   EMBO J. 6:2131-2137(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-11.
RX   PubMed=7882427; DOI=10.1007/bf00310497;
RA   Bottorff D.A., Parmaksizoglu S., Lemire E.G., Coffin J.W., Bertrand H.,
RA   Nargang F.E.;
RT   "Mutations in the structural gene for cytochrome c result in deficiency of
RT   both cytochromes aa3 and c in Neurospora crassa.";
RL   Curr. Genet. 26:329-335(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
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   PROTEIN SEQUENCE OF 2-108.
RX   PubMed=5950080; DOI=10.1016/s0021-9258(18)96512-9;
RA   Heller J., Smith E.L.;
RT   "Neurospora crassa cytochrome c. II. Chymotryptic peptides, tryptic
RT   peptides, cyanogen bromide peptides, and the complete amino acid
RT   sequence.";
RL   J. Biol. Chem. 241:3165-3180(1966).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-44.
RX   PubMed=4363050; DOI=10.1016/0006-291x(74)90844-4;
RA   Lederer F., Simon A.M.;
RT   "Neurospora crassa and Humicola lanuginosa cytochromes c: more homology in
RT   the heme region.";
RL   Biochem. Biophys. Res. Commun. 56:317-323(1974).
RN   [7]
RP   METHYLATION AT LYS-77.
RX   PubMed=4304194; DOI=10.1016/s0021-9258(18)91855-7;
RA   Delange R.J., Glazer A.N., Smith E.L.;
RT   "Presence and location of an unusual amino acid, epsilon-N-trimethyllysine,
RT   in cytochrome c of wheat germ and Neurospora.";
RL   J. Biol. Chem. 244:1385-1388(1969).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
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DR   EMBL; X05506; CAA29050.1; -; mRNA.
DR   EMBL; L19358; AAA92156.1; -; Genomic_DNA.
DR   EMBL; X05507; CAA29051.1; -; Genomic_DNA.
DR   EMBL; AL669998; CAD21169.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA27250.2; -; Genomic_DNA.
DR   PIR; S48221; CCNC.
DR   RefSeq; XP_956486.2; XM_951393.3.
DR   AlphaFoldDB; P00048; -.
DR   SMR; P00048; -.
DR   STRING; 367110.P00048; -.
DR   PaxDb; 5141-EFNCRP00000001740; -.
DR   EnsemblFungi; EAA27250; EAA27250; NCU01808.
DR   GeneID; 3872635; -.
DR   KEGG; ncr:NCU01808; -.
DR   VEuPathDB; FungiDB:NCU01808; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00048; -.
DR   OrthoDB; 4150at2759; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
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   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF12; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Methylation; Mitochondrion; Reference proteome; Respiratory chain;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4363050,
FT                   ECO:0000269|PubMed:5950080"
FT   CHAIN           2..108
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108328"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         22
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         23
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   BINDING         85
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   MOD_RES         77
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:4304194"
FT   VARIANT         11
FT                   /note="G -> D (in cyt-12-12/cyc-1-1; characterized by slow
FT                   growth and a deficiency of
FT                   spectrophotometrically-detectable cytochromes aa3 and c)"
FT                   /evidence="ECO:0000269|PubMed:2820723,
FT                   ECO:0000269|PubMed:7882427"
FT   CONFLICT        21
FT                   /note="Q -> E (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24..31
FT                   /note="TLEEGGGN -> GEGGNLTQ (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   108 AA;  11813 MW;  8150D1A1B92A6E85 CRC64;
     MGFSAGDSKK GANLFKTRCA QCHTLEEGGG NKIGPALHGL FGRKTGSVDG YAYTDANKQK
     GITWDENTLF EYLENPKKYI PGTKMAFGGL KKDKDRNDII TFMKEATA
//