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 27-MAR-2024, entry version 234. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7MRI; X-ray; 2.46 A; A/C/E=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; 7MRI; -. DR PDBsum; 7PR2; -. DR PDBsum; 7PR3; -. DR PDBsum; 7PR4; -. DR AlphaFoldDB; P00044; -. DR BMRB; P00044; -. DR SMR; P00044; -. DR BioGRID; 33801; 141. DR DIP; DIP-4265N; -. DR IntAct; P00044; 4. DR MINT; P00044; -. DR STRING; 4932.YJR048W; -. DR MoonProt; P00044; -. DR MaxQB; P00044; -. DR PaxDb; 4932-YJR048W; -. DR PeptideAtlas; P00044; -. DR EnsemblFungi; YJR048W_mRNA; YJR048W; YJR048W. DR GeneID; 853507; -. DR KEGG; sce:YJR048W; -. DR AGR; SGD:S000003809; -. 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; WGCPASE; -. DR OrthoDB; 4150at2759; -. DR BioCyc; YEAST:G3O-31683-MONOMER; -. 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 BioGRID-ORCS; 853507; 7 hits in 10 CRISPR screens. 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; 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 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 //