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UniProtKB/Swiss-Prot entry P00044


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYC1_YEAST
Primary accession number P00044
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 110)
Name and origin of the protein
Protein name Cytochrome c iso-1
Synonyms None
Gene name
Name: CYC1
OrderedLocusNames: YJR048W
ORFNames: J1653
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(79)90091-6; PubMed=222467 [NCBI, ExPASy, EBI, Israel, Japan]
Smith M., Leung D.W., Gillam S., Astell C.R., Montgomery D.L., Hall B.D.;
"Sequence of the gene for iso-1-cytochrome c in Saccharomyces cerevisiae.";
Cell 16:753-761(1979).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6273415 [NCBI, ExPASy, EBI, Israel, Japan]
Boss J.M., Gillam S., Ziotmer R.S., Smith M.;
"Sequence of the yeast iso-1-cytochrome c mRNA.";
J. Biol. Chem. 256:12958-12961(1981).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(90)90297-5; PubMed=2158927 [NCBI, ExPASy, EBI, Israel, Japan]
Melnick L., Sherman F.;
"Nucleotide sequence of the COR region: a cluster of six genes in the yeast Saccharomyces cerevisiae.";
Gene 87:157-166(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7975898 [NCBI, ExPASy, EBI, Israel, Japan]
Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
"Revised nucleotide sequence of the COR region of yeast Saccharomyces cerevisiae chromosome X.";
Yeast 10:811-818(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[6]
PROTEIN SEQUENCE OF 2-109.
STRAIN=Oviformis;
PubMed=5771953 [NCBI, ExPASy, EBI, Israel, Japan]
Narita K., Titani K.;
"The complete amino acid sequence in baker's yeast cytochrome c.";
J. Biochem. 65:259-267(1969).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
DOI=10.1016/0022-2836(86)90439-0; PubMed=3009831 [NCBI, ExPASy, EBI, Israel, Japan]
McNeil J.B., Smith M.;
"Transcription initiation of the Saccharomyces cerevisiae iso-1-cytochrome c gene. Multiple, independent T-A-T-A sequences.";
J. Mol. Biol. 187:363-378(1986).
[8]
SYNTHESIS.
PubMed=4348687 [NCBI, ExPASy, EBI, Israel, Japan]
Moroder L., Marchiori F., Borin G., Scoffone E.;
"Studies on cytochrome c. 8. Synthesis of the protected hexadecapeptide (sequence 93-108) of Baker's yeast iso-1-cytochrome c.";
Biopolymers 12:729-750(1973).
[9]
METHYLATION.
PubMed=2822698 [NCBI, ExPASy, EBI, Israel, Japan]
Park K.S., Frost B., Tuck M., Ho L.L., Kim S., Paik W.K.;
"Enzymatic methylation of in vitro synthesized apocytochrome c enhances its transport into mitochondria.";
J. Biol. Chem. 262:14702-14708(1987).
[10]
METHYLATION AT LYS-78, AND MUTAGENESIS OF LYS-78.
DOI=10.1074/jbc.M001891200; PubMed=10791961 [NCBI, ExPASy, EBI, Israel, Japan]
Polevoda B., Martzen M.R., Das B., Phizicky E.M., Sherman F.;
"Cytochrome c methyltransferase, Ctm1p, of yeast.";
J. Biol. Chem. 275:20508-20513(2000).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1016/0022-2836(88)90315-4; PubMed=2832611 [NCBI, ExPASy, EBI, Israel, Japan]
Louie G.V., Hutcheon W.L., Brayer G.D.;
"Yeast iso-1-cytochrome c. A 2.8-A resolution three-dimensional structure determination.";
J. Mol. Biol. 199:295-314(1988).
[13]
X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS).
DOI=10.1016/0022-2836(90)90197-T; PubMed=2166169 [NCBI, ExPASy, EBI, Israel, Japan]
Louie G.V., Brayer G.D.;
"High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c.";
J. Mol. Biol. 214:527-555(1990).
[14]
X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
DOI=10.1073/pnas.052704699; PubMed=11880631 [NCBI, ExPASy, EBI, Israel, Japan]
Lange C., Hunte C.;
"Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.";
Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
[15]
STRUCTURE BY NMR.
DOI=10.1021/bi961110e; PubMed=8901521 [NCBI, ExPASy, EBI, Israel, Japan]
Baistrocchi P., Banci L., Bertini I., Turano P., Bren K.L., Gray H.B.;
"Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c.";
Biochemistry 35:13788-13796(1996).
[16]
STRUCTURE BY NMR.
DOI=10.1021/bi963025c; PubMed=9220987 [NCBI, ExPASy, EBI, Israel, Japan]
Banci L., Bertini I., Bren K.L., Gray H.B., Sompornpisut P., Turano P.;
"Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c.";
Biochemistry 36:8992-9001(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M37696; AAB59344.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01298; CAA24605.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L26347; AAA62856.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L36344; AAA88751.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49548; CAA89576.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03472; CAA27189.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00037; CCBY.
RefSeq NP_012582.1; -.
3D structure databases
PDB
1CHH; X-ray; 1.97 A; A=1-109.[ExPASy / RCSB / EBI]
1CHI; X-ray; 2.00 A; A=1-109.[ExPASy / RCSB / EBI]
1CHJ; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1CIE; X-ray; 1.80 A; A=1-109.[ExPASy / RCSB / EBI]
1CIF; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1CIG; X-ray; 1.80 A; A=1-109.[ExPASy / RCSB / EBI]
1CIH; X-ray; 1.80 A; A=1-109.[ExPASy / RCSB / EBI]
1CRG; X-ray; 2.00 A; A=1-109.[ExPASy / RCSB / EBI]
1CRH; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1CRI; X-ray; 2.00 A; A=1-109.[ExPASy / RCSB / EBI]
1CRJ; X-ray; 2.05 A; A=1-109.[ExPASy / RCSB / EBI]
1CSU; X-ray; 1.81 A; A=1-109.[ExPASy / RCSB / EBI]
1CSV; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1CSW; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1CSX; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1CTY; X-ray; 2.20 A; A=1-109.[ExPASy / RCSB / EBI]
1CTZ; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1FHB; NMR; -; A=1-109.[ExPASy / RCSB / EBI]
1IRV; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1IRW; X-ray; 2.00 A; A=1-109.[ExPASy / RCSB / EBI]
1KYO; X-ray; 2.97 A; W=1-109.[ExPASy / RCSB / EBI]
1LMS; NMR; -; A=1-109.[ExPASy / RCSB / EBI]
1NMI; NMR; -; A=1-109.[ExPASy / RCSB / EBI]
1RAP; X-ray; 2.25 A; A=1-109.[ExPASy / RCSB / EBI]
1RAQ; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
1S6V; X-ray; 1.88 A; B/D=3-109.[ExPASy / RCSB / EBI]
1U74; X-ray; 2.40 A; B/D=1-109.[ExPASy / RCSB / EBI]
1YCC; X-ray; 1.23 A; A=1-109.[ExPASy / RCSB / EBI]
1YFC; NMR; -; A=1-109.[ExPASy / RCSB / EBI]
1YIC; NMR; -; A=1-109.[ExPASy / RCSB / EBI]
2B0Z; X-ray; 2.70 A; B=1-109.[ExPASy / RCSB / EBI]
2B10; X-ray; 2.80 A; B/D=1-109.[ExPASy / RCSB / EBI]
2B11; X-ray; 2.30 A; B/D=1-109.[ExPASy / RCSB / EBI]
2B12; X-ray; 3.02 A; B=1-109.[ExPASy / RCSB / EBI]
2BCN; X-ray; 1.70 A; B=1-109.[ExPASy / RCSB / EBI]
2GB8; NMR; -; B=2-109.[ExPASy / RCSB / EBI]
2HV4; NMR; -; A=2-109.[ExPASy / RCSB / EBI]
2JQR; NMR; -; A=2-109.[ExPASy / RCSB / EBI]
2ORL; NMR; -; A=2-109.[ExPASy / RCSB / EBI]
2PCC; X-ray; 2.30 A; B/D=1-109.[ExPASy / RCSB / EBI]
2YCC; X-ray; 1.90 A; A=1-109.[ExPASy / RCSB / EBI]
3CX5; X-ray; 1.90 A; W=2-109.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CHH; -.
1CHI; -.
1CHJ; -.
1CIE; -.
1CIF; -.
1CIG; -.
1CIH; -.
1CRG; -.
1CRH; -.
1CRI; -.
1CRJ; -.
1CSU; -.
1CSV; -.
1CSW; -.
1CSX; -.
1CTY; -.
1CTZ; -.
1FHB; -.
1IRV; -.
1IRW; -.
1KYO; -.
1LMS; -.
1NMI; -.
1RAP; -.
1RAQ; -.
1S6V; -.
1U74; -.
1YCC; -.
1YFC; -.
1YIC; -.
2B0Z; -.
2B10; -.
2B11; -.
2B12; -.
2BCN; -.
2GB8; -.
2HV4; -.
2JQR; -.
2ORL; -.
2PCC; -.
2YCC; -.
3CX5; -.
ModBase P00044.
Protein-protein interaction databases
DIP DIP:4265N; -.
IntAct P00044; -.
Organism-specific databases
CYGD YJR048w; -.
SGD S000003809; CYC1.
Yeast-GFP YJR048W.
Gene expression databases
ArrayExpress P00044; -.
GermOnline YJR048W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from direct assay from SGD).
GO:0009055; Molecular function: electron carrier activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006123; Biological process: mitochondrial electron transport, cytochrome c to oxygen (inferred from direct assay from SGD).
GO:0006122; Biological process: mitochondrial electron transport, ubiquinol to cytochrome c (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR009056; Cyt_c_monohaem.
IPR003088; Cyt_CI.
IPR002327; Cyt_CIAB.
Graphical view of domain structure.
Gene3D G3DSA:1.10.760.10; Cytochrome_c_R; 1.
PANTHER PTHR11961; Cyt_CIAB; 1.
Pfam PF00034; Cytochrom_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00604; CYTCHRMECIAB.
ProDom PD000375; Cyt_CIAB; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS51007; CYTC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00044.
ProtoNet P00044.
Proteomic databases
PeptideAtlas P00044; -.
Genome annotation databases
Ensembl YJR048W; Saccharomyces cerevisiae. [Contig view]
GeneID 853507; -.
GenomeReviews Y13136_GR; YJR048W.
KEGG sce:YJR048W; -.
NMPDR fig|4932.3.peg.3556; -.
Phylogenomic databases
HOGENOM P00044; -.
Other
BindingDB P00044; -.
LinkHub P00044; -.
NextBio 974162; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Methylation; Mitochondrion; Respiratory chain; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   109  108     Cytochrome c iso-1. PRO_0000108337
METAL   24    24        Iron (heme axial ligand). 
METAL   86    86        Iron (heme axial ligand). 
BINDING   20    20        Heme (covalent). 
BINDING   23    23        Heme (covalent). 
MOD_RES   78    78        N6,N6,N6-trimethyllysine; by CTM1. 
MUTAGEN   78    78        K->R: Loss of methylation by CTM1. 
HELIX   9    19  11      
TURN   20    23  4      
HELIX   56    61  6      
HELIX   67    75  9      
HELIX   77    80  4      
HELIX   94   107  14      
Sequence information
Length: 109 AA [This is the length of the unprocessed precursor] Molecular weight: 12182 Da [This is the MW of the unprocessed precursor] CRC64: 1F8B6CB3B60C0BE8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTEFKAGSAK KGATLFKTRC LQCHTVEKGG PHKVGPNLHG IFGRHSGQAE GYSYTDANIK 

        70         80         90        100 
KNVLWDENNM SEYLTNPKKY IPGTKMAFGG LKKEKDRNDL ITYLKKACE 

P00044 in FASTA format

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View entry in raw text format (no links)
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