CYC1_YEAST
ID CYC1_YEAST Reviewed; 109 AA.
AC P00044; D6VWL9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Cytochrome c isoform 1;
DE Short=Iso-1-cytochrome c;
DE AltName: Full=Cytochrome c aerobic isoform;
GN Name=CYC1; OrderedLocusNames=YJR048W; ORFNames=J1653;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=222467; DOI=10.1016/0092-8674(79)90091-6;
RA Smith M., Leung D.W., Gillam S., Astell C.R., Montgomery D.L., Hall B.D.;
RT "Sequence of the gene for iso-1-cytochrome c in Saccharomyces cerevisiae.";
RL Cell 16:753-761(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6273415; DOI=10.1016/s0021-9258(18)42989-4;
RA Boss J.M., Gillam S., Ziotmer R.S., Smith M.;
RT "Sequence of the yeast iso-1-cytochrome c mRNA.";
RL J. Biol. Chem. 256:12958-12961(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2158927; DOI=10.1016/0378-1119(90)90297-5;
RA Melnick L., Sherman F.;
RT "Nucleotide sequence of the COR region: a cluster of six genes in the yeast
RT Saccharomyces cerevisiae.";
RL Gene 87:157-166(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975898; DOI=10.1002/yea.320100611;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Revised nucleotide sequence of the COR region of yeast Saccharomyces
RT cerevisiae chromosome X.";
RL Yeast 10:811-818(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP PROTEIN SEQUENCE OF 2-109.
RC STRAIN=Oviformis;
RX PubMed=5771953;
RA Narita K., Titani K.;
RT "The complete amino acid sequence in baker's yeast cytochrome c.";
RL J. Biochem. 65:259-267(1969).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=3009831; DOI=10.1016/0022-2836(86)90439-0;
RA McNeil J.B., Smith M.;
RT "Transcription initiation of the Saccharomyces cerevisiae iso-1-cytochrome
RT c gene. Multiple, independent T-A-T-A sequences.";
RL J. Mol. Biol. 187:363-378(1986).
RN [9]
RP PROTEIN SEQUENCE OF 2-5, AND SUBCELLULAR LOCATION.
RX PubMed=9866716; DOI=10.1006/abio.1998.2863;
RA Martin H., Eckerskorn C., Gaertner F., Rassow J., Lottspeich F.,
RA Pfanner N.;
RT "The yeast mitochondrial intermembrane space: purification and analysis of
RT two distinct fractions.";
RL Anal. Biochem. 265:123-128(1998).
RN [10]
RP SYNTHESIS.
RX PubMed=4348687; DOI=10.1002/bip.1973.360120405;
RA Moroder L., Marchiori F., Borin G., Scoffone E.;
RT "Studies on cytochrome c. 8. Synthesis of the protected hexadecapeptide
RT (sequence 93-108) of Baker's yeast iso-1-cytochrome c.";
RL Biopolymers 12:729-750(1973).
RN [11]
RP METHYLATION.
RX PubMed=2822698; DOI=10.1016/s0021-9258(18)47852-0;
RA Park K.S., Frost B., Tuck M., Ho L.L., Kim S., Paik W.K.;
RT "Enzymatic methylation of in vitro synthesized apocytochrome c enhances its
RT transport into mitochondria.";
RL J. Biol. Chem. 262:14702-14708(1987).
RN [12]
RP FUNCTION.
RX PubMed=7851399; DOI=10.1111/j.1432-1033.1995.tb20388.x;
RA Geier B.M., Schagger H., Ortwein C., Link T.A., Hagen W.R., Brandt U.,
RA Von Jagow G.;
RT "Kinetic properties and ligand binding of the eleven-subunit cytochrome-c
RT oxidase from Saccharomyces cerevisiae isolated with a novel large-scale
RT purification method.";
RL Eur. J. Biochem. 227:296-302(1995).
RN [13]
RP FUNCTION.
RX PubMed=7814361; DOI=10.1074/jbc.270.1.110;
RA Allen L.A., Zhao X.J., Caughey W., Poyton R.O.;
RT "Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear
RT reaction center and alter the kinetics of interaction with the isoforms of
RT yeast cytochrome c.";
RL J. Biol. Chem. 270:110-118(1995).
RN [14]
RP INDUCTION.
RX PubMed=9169434; DOI=10.1074/jbc.272.23.14705;
RA Burke P.V., Raitt D.C., Allen L.A., Kellogg E.A., Poyton R.O.;
RT "Effects of oxygen concentration on the expression of cytochrome c and
RT cytochrome c oxidase genes in yeast.";
RL J. Biol. Chem. 272:14705-14712(1997).
RN [15]
RP METHYLATION AT LYS-79.
RX PubMed=10821864; DOI=10.1074/jbc.275.21.16127;
RA Kluck R.M., Ellerby L.M., Ellerby H.M., Naiem S., Yaffe M.P.,
RA Margoliash E., Bredesen D., Mauk A.G., Sherman F., Newmeyer D.D.;
RT "Determinants of cytochrome c pro-apoptotic activity. The role of lysine 72
RT trimethylation.";
RL J. Biol. Chem. 275:16127-16133(2000).
RN [16]
RP METHYLATION AT LYS-78, AND MUTAGENESIS OF LYS-78.
RX PubMed=10791961; DOI=10.1074/jbc.m001891200;
RA Polevoda B., Martzen M.R., Das B., Phizicky E.M., Sherman F.;
RT "Cytochrome c methyltransferase, Ctm1p, of yeast.";
RL J. Biol. Chem. 275:20508-20513(2000).
RN [17]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=2832611; DOI=10.1016/0022-2836(88)90315-4;
RA Louie G.V., Hutcheon W.L., Brayer G.D.;
RT "Yeast iso-1-cytochrome c. A 2.8-A resolution three-dimensional structure
RT determination.";
RL J. Mol. Biol. 199:295-314(1988).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS).
RX PubMed=2166169; DOI=10.1016/0022-2836(90)90197-t;
RA Louie G.V., Brayer G.D.;
RT "High-resolution refinement of yeast iso-1-cytochrome c and comparisons
RT with other eukaryotic cytochromes c.";
RL J. Mol. Biol. 214:527-555(1990).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) IN COMPLEX WITH HEME, AND
RP METHYLATION AT LYS-78.
RX PubMed=11880631; DOI=10.1073/pnas.052704699;
RA Lange C., Hunte C.;
RT "Crystal structure of the yeast cytochrome bc1 complex with its bound
RT substrate cytochrome c.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
RN [23]
RP STRUCTURE BY NMR.
RX PubMed=8901521; DOI=10.1021/bi961110e;
RA Baistrocchi P., Banci L., Bertini I., Turano P., Bren K.L., Gray H.B.;
RT "Three-dimensional solution structure of Saccharomyces cerevisiae reduced
RT iso-1-cytochrome c.";
RL Biochemistry 35:13788-13796(1996).
RN [24]
RP STRUCTURE BY NMR.
RX PubMed=9220987; DOI=10.1021/bi963025c;
RA Banci L., Bertini I., Bren K.L., Gray H.B., Sompornpisut P., Turano P.;
RT "Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome
RT c.";
RL Biochemistry 36:8992-9001(1997).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-109 IN THE BC1 COMPLEX, AND
RP METHYLATION AT LYS-79.
RX PubMed=18390544; DOI=10.1074/jbc.m710126200;
RA Solmaz S.R., Hunte C.;
RT "Structure of complex III with bound cytochrome c in reduced state and
RT definition of a minimal core interface for electron transfer.";
RL J. Biol. Chem. 283:17542-17549(2008).
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 ubiquinol-cytochrome c oxidoreductase.
CC Cytochrome c then transfers this electron to the dinuclear copper A
CC center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final
CC protein carrier in the mitochondrial electron-transport chain. Isoform
CC 1 (CYC1) is the predominant cytochrome c during aerobic/normoxic
CC growth. {ECO:0000269|PubMed:7814361, ECO:0000269|PubMed:7851399,
CC ECO:0000269|PubMed:9169434}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:18390544};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:18390544};
CC -!- INTERACTION:
CC P00044; P00431: CCP1; NbExp=4; IntAct=EBI-5393, EBI-4389;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:9866716}.
CC -!- INDUCTION: By oxygen at the level of transcription. Expression drops
CC rapidly when the oxygen concentration falls below 0.5 uM O(2).
CC {ECO:0000269|PubMed:9169434}.
CC -!- PTM: Methylation may enhance its transport into mitochondria.
CC Methylation occurs in fungi, plants, and some protozoa, but not in
CC animals. The precise role of methylation at Lys-79 is unknown, but it
CC seems to preclude pro-apoptotic activity, possibly by lowering affinity
CC for APAF1. {ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:10821864,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:2822698}.
CC -!- MISCELLANEOUS: Present with 7330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; M37696; AAB59344.1; -; Genomic_DNA.
DR EMBL; V01298; CAA24605.1; -; Genomic_DNA.
DR EMBL; L26347; AAA62856.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88751.1; -; Genomic_DNA.
DR EMBL; Z49548; CAA89576.1; -; Genomic_DNA.
DR EMBL; X03472; CAA27189.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08835.1; -; Genomic_DNA.
DR PIR; A00037; CCBY.
DR RefSeq; NP_012582.1; NM_001181706.1.
DR PDB; 1CHH; X-ray; 1.97 A; A=2-107.
DR PDB; 1CHI; X-ray; 2.00 A; A=2-107.
DR PDB; 1CHJ; X-ray; 1.90 A; A=2-107.
DR PDB; 1CIE; X-ray; 1.80 A; A=2-107.
DR PDB; 1CIF; X-ray; 1.90 A; A=2-107.
DR PDB; 1CIG; X-ray; 1.80 A; A=2-107.
DR PDB; 1CIH; X-ray; 1.80 A; A=2-107.
DR PDB; 1CRG; X-ray; 2.00 A; A=2-107.
DR PDB; 1CRH; X-ray; 1.90 A; A=2-109.
DR PDB; 1CRI; X-ray; 2.00 A; A=2-107.
DR PDB; 1CRJ; X-ray; 2.05 A; A=2-107.
DR PDB; 1CSU; X-ray; 1.81 A; A=2-107.
DR PDB; 1CSV; X-ray; 1.90 A; A=2-107.
DR PDB; 1CSW; X-ray; 1.90 A; A=2-107.
DR PDB; 1CSX; X-ray; 1.90 A; A=2-107.
DR PDB; 1CTY; X-ray; 2.20 A; A=2-107.
DR PDB; 1CTZ; X-ray; 1.90 A; A=2-107.
DR PDB; 1FHB; NMR; -; A=2-107.
DR PDB; 1IRV; X-ray; 1.90 A; A=2-107.
DR PDB; 1IRW; X-ray; 2.00 A; A=2-107.
DR PDB; 1KYO; X-ray; 2.97 A; W=2-109.
DR PDB; 1LMS; NMR; -; A=2-107.
DR PDB; 1NMI; NMR; -; A=2-107.
DR PDB; 1RAP; X-ray; 2.25 A; A=2-109.
DR PDB; 1RAQ; X-ray; 1.90 A; A=2-109.
DR PDB; 1S6V; X-ray; 1.88 A; B/D=2-107.
DR PDB; 1U74; X-ray; 2.40 A; B/D=2-107.
DR PDB; 1YCC; X-ray; 1.23 A; A=2-109.
DR PDB; 1YFC; NMR; -; A=2-107.
DR PDB; 1YIC; NMR; -; A=2-107.
DR PDB; 2B0Z; X-ray; 2.70 A; B=2-109.
DR PDB; 2B10; X-ray; 2.80 A; B/D=2-109.
DR PDB; 2B11; X-ray; 2.30 A; B/D=2-109.
DR PDB; 2B12; X-ray; 3.02 A; B=2-109.
DR PDB; 2BCN; X-ray; 1.70 A; B=2-107.
DR PDB; 2GB8; NMR; -; B=2-109.
DR PDB; 2HV4; NMR; -; A=2-107.
DR PDB; 2JQR; NMR; -; A=2-107.
DR PDB; 2JTI; NMR; -; B=2-109.
DR PDB; 2LIR; NMR; -; A=2-107.
DR PDB; 2LIT; NMR; -; A=2-107.
DR PDB; 2MHM; NMR; -; A=2-107.
DR PDB; 2N18; NMR; -; B=3-107, C=2-109.
DR PDB; 2ORL; NMR; -; A=2-107.
DR PDB; 2PCC; X-ray; 2.30 A; B/D=2-109.
DR PDB; 2YCC; X-ray; 1.90 A; A=2-107.
DR PDB; 3CX5; X-ray; 1.90 A; W=2-109.
DR PDB; 3TYI; X-ray; 1.40 A; A/B=2-107.
DR PDB; 4MU8; X-ray; 1.45 A; A/B=2-107.
DR PDB; 4N0K; X-ray; 1.05 A; A/B=2-107.
DR PDB; 4P4Q; X-ray; 2.01 A; B/D=7-109.
DR PDB; 4Q5P; X-ray; 1.87 A; A/B/C=4-107.
DR PDB; 4QAO; X-ray; 2.10 A; A/B/C=4-107.
DR PDB; 4YE1; X-ray; 1.39 A; A/B=2-109.
DR PDB; 5CIB; X-ray; 3.01 A; B/D=2-109.
DR PDB; 5CIC; X-ray; 2.10 A; B/D=2-109.
DR PDB; 5CID; X-ray; 2.76 A; B/D=2-109.
DR PDB; 5CIE; X-ray; 2.60 A; B/D=2-109.
DR PDB; 5CIF; X-ray; 2.01 A; B/D=7-109.
DR PDB; 5CIG; X-ray; 2.06 A; B/D=2-109.
DR PDB; 5CIH; X-ray; 2.60 A; B/D=7-109.
DR PDB; 5KKE; X-ray; 1.70 A; A=2-107.
DR PDB; 5KLU; X-ray; 1.99 A; A/B=4-107.
DR PDB; 5KPF; X-ray; 1.70 A; A/B=3-109.
DR PDB; 5LFT; X-ray; 1.25 A; A=3-109.
DR PDB; 5LYC; X-ray; 1.80 A; A/B=3-109.
DR PDB; 5NCV; X-ray; 1.50 A; A/B=3-109.
DR PDB; 5T7H; X-ray; 2.00 A; A/B/C/D=1-107.
DR PDB; 5T8W; X-ray; 1.60 A; A/B=2-109.
DR PDB; 6EGY; X-ray; 2.70 A; A/B=2-109.
DR PDB; 6EGZ; X-ray; 2.17 A; A/B=2-109.
DR PDB; 6GD6; X-ray; 1.20 A; A=3-109.
DR PDB; 6GD7; X-ray; 1.55 A; A=3-109.
DR PDB; 6GD8; X-ray; 2.50 A; A/B/C/D=3-109.
DR PDB; 6GD9; X-ray; 2.65 A; A=3-109.
DR PDB; 6GDA; X-ray; 2.80 A; A=3-109.
DR PDB; 6P41; X-ray; 2.90 A; B/D=7-109.
DR PDB; 6P42; X-ray; 2.90 A; B/D=7-109.
DR PDB; 6P43; X-ray; 1.91 A; B=2-109.
DR PDB; 6RGI; X-ray; 2.64 A; A=3-109.
DR PDB; 6RSI; X-ray; 2.48 A; A=3-109.
DR PDB; 6RSJ; X-ray; 2.27 A; A=3-109.
DR PDB; 6RSK; X-ray; 2.31 A; A/B=3-109.
DR PDB; 6RSL; X-ray; 1.99 A; A/B=3-109.
DR PDB; 6S8Y; X-ray; 2.09 A; A=3-109.
DR PDB; 6SUY; X-ray; 1.75 A; A/B=2-109.
DR PDB; 6Y0J; X-ray; 2.70 A; A/B/C/D=3-109.
DR PDB; 7BBT; X-ray; 3.02 A; A/B/C/D=3-109.
DR PDB; 7PR2; X-ray; 1.73 A; A/B=3-109.
DR PDB; 7PR3; X-ray; 2.37 A; A/B/C/D=3-109.
DR PDB; 7PR4; X-ray; 1.32 A; A=3-109.
DR PDBsum; 1CHH; -.
DR PDBsum; 1CHI; -.
DR PDBsum; 1CHJ; -.
DR PDBsum; 1CIE; -.
DR PDBsum; 1CIF; -.
DR PDBsum; 1CIG; -.
DR PDBsum; 1CIH; -.
DR PDBsum; 1CRG; -.
DR PDBsum; 1CRH; -.
DR PDBsum; 1CRI; -.
DR PDBsum; 1CRJ; -.
DR PDBsum; 1CSU; -.
DR PDBsum; 1CSV; -.
DR PDBsum; 1CSW; -.
DR PDBsum; 1CSX; -.
DR PDBsum; 1CTY; -.
DR PDBsum; 1CTZ; -.
DR PDBsum; 1FHB; -.
DR PDBsum; 1IRV; -.
DR PDBsum; 1IRW; -.
DR PDBsum; 1KYO; -.
DR PDBsum; 1LMS; -.
DR PDBsum; 1NMI; -.
DR PDBsum; 1RAP; -.
DR PDBsum; 1RAQ; -.
DR PDBsum; 1S6V; -.
DR PDBsum; 1U74; -.
DR PDBsum; 1YCC; -.
DR PDBsum; 1YFC; -.
DR PDBsum; 1YIC; -.
DR PDBsum; 2B0Z; -.
DR PDBsum; 2B10; -.
DR PDBsum; 2B11; -.
DR PDBsum; 2B12; -.
DR PDBsum; 2BCN; -.
DR PDBsum; 2GB8; -.
DR PDBsum; 2HV4; -.
DR PDBsum; 2JQR; -.
DR PDBsum; 2JTI; -.
DR PDBsum; 2LIR; -.
DR PDBsum; 2LIT; -.
DR PDBsum; 2MHM; -.
DR PDBsum; 2N18; -.
DR PDBsum; 2ORL; -.
DR PDBsum; 2PCC; -.
DR PDBsum; 2YCC; -.
DR PDBsum; 3CX5; -.
DR PDBsum; 3TYI; -.
DR PDBsum; 4MU8; -.
DR PDBsum; 4N0K; -.
DR PDBsum; 4P4Q; -.
DR PDBsum; 4Q5P; -.
DR PDBsum; 4QAO; -.
DR PDBsum; 4YE1; -.
DR PDBsum; 5CIB; -.
DR PDBsum; 5CIC; -.
DR PDBsum; 5CID; -.
DR PDBsum; 5CIE; -.
DR PDBsum; 5CIF; -.
DR PDBsum; 5CIG; -.
DR PDBsum; 5CIH; -.
DR PDBsum; 5KKE; -.
DR PDBsum; 5KLU; -.
DR PDBsum; 5KPF; -.
DR PDBsum; 5LFT; -.
DR PDBsum; 5LYC; -.
DR PDBsum; 5NCV; -.
DR PDBsum; 5T7H; -.
DR PDBsum; 5T8W; -.
DR PDBsum; 6EGY; -.
DR PDBsum; 6EGZ; -.
DR PDBsum; 6GD6; -.
DR PDBsum; 6GD7; -.
DR PDBsum; 6GD8; -.
DR PDBsum; 6GD9; -.
DR PDBsum; 6GDA; -.
DR PDBsum; 6P41; -.
DR PDBsum; 6P42; -.
DR PDBsum; 6P43; -.
DR PDBsum; 6RGI; -.
DR PDBsum; 6RSI; -.
DR PDBsum; 6RSJ; -.
DR PDBsum; 6RSK; -.
DR PDBsum; 6RSL; -.
DR PDBsum; 6S8Y; -.
DR PDBsum; 6SUY; -.
DR PDBsum; 6Y0J; -.
DR PDBsum; 7BBT; -.
DR PDBsum; 7PR2; -.
DR PDBsum; 7PR3; -.
DR PDBsum; 7PR4; -.
DR AlphaFoldDB; P00044; -.
DR BMRB; P00044; -.
DR SMR; P00044; -.
DR BioGRID; 33801; 135.
DR DIP; DIP-4265N; -.
DR IntAct; P00044; 4.
DR MINT; P00044; -.
DR STRING; 4932.YJR048W; -.
DR MoonProt; P00044; -.
DR MaxQB; P00044; -.
DR PaxDb; P00044; -.
DR PRIDE; P00044; -.
DR EnsemblFungi; YJR048W_mRNA; YJR048W; YJR048W.
DR GeneID; 853507; -.
DR KEGG; sce:YJR048W; -.
DR SGD; S000003809; CYC1.
DR VEuPathDB; FungiDB:YJR048W; -.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00940000168884; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P00044; -.
DR OMA; AQCHTIN; -.
DR BioCyc; YEAST:G3O-31683-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SCE-5620971; Pyroptosis.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P00044; -.
DR PRO; PR:P00044; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P00044; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:SGD.
DR Gene3D; 1.10.760.10; -; 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; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Methylation; Mitochondrion; Reference proteome;
KW Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5771953,
FT ECO:0000269|PubMed:9866716"
FT CHAIN 2..109
FT /note="Cytochrome c isoform 1"
FT /id="PRO_0000108337"
FT BINDING 20
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:3CX5"
FT BINDING 23
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:3CX5"
FT BINDING 24
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:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:3CX5"
FT BINDING 86
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:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:3CX5"
FT MOD_RES 78
FT /note="N6,N6,N6-trimethyllysine; by CTM1"
FT /evidence="ECO:0000269|PubMed:10791961,
FT ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:10821864,
FT ECO:0000269|PubMed:18390544"
FT MUTAGEN 78
FT /note="K->R: Loss of methylation by CTM1."
FT /evidence="ECO:0000269|PubMed:10791961"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:4N0K"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:4N0K"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2PCC"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5LFT"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5KPF"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4N0K"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5CID"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:4N0K"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2MHM"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:4N0K"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:4N0K"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1FHB"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5KKE"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4N0K"
SQ SEQUENCE 109 AA; 12182 MW; 1F8B6CB3B60C0BE8 CRC64;
MTEFKAGSAK KGATLFKTRC LQCHTVEKGG PHKVGPNLHG IFGRHSGQAE GYSYTDANIK
KNVLWDENNM SEYLTNPKKY IPGTKMAFGG LKKEKDRNDL ITYLKKACE
