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P00044 (CYC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c iso-1
Gene names
Name:CYC1
Ordered Locus Names:YJR048W
ORF Names:J1653
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.

Subcellular location

Mitochondrion intermembrane space. Note: Loosely associated with the inner membrane By similarity.

Developmental stage

Iso-1 is the predominant cytochrome c in aerobically grown cells.

Induction

By oxygen.

Post-translational modification

Binds 1 heme group per subunit.

Methylation may enhance its transport into mitochondria. Methylation occurs in fungi, plants, and some protozoa, but not in animals. The precise role of methylation at Lys-79 is unknown, but it seems to preclude pro-apoptotic activity, possibly by lowering affinity for APAF1. Ref.10 Ref.11 Ref.12 Ref.20

Miscellaneous

Present with 7330 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cytochrome c family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCP1P004312EBI-5393,EBI-4389

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 109108Cytochrome c iso-1
PRO_0000108337

Sites

Metal binding241Iron (heme axial ligand)
Metal binding861Iron (heme axial ligand)
Binding site201Heme (covalent)
Binding site231Heme (covalent)

Amino acid modifications

Modified residue781N6,N6,N6-trimethyllysine; by CTM1 Ref.12
Modified residue791N6,N6,N6-trimethyllysine Ref.11 Ref.20

Experimental info

Mutagenesis781K → R: Loss of methylation by CTM1. Ref.12

Secondary structure

....................... 109
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00044 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1F8B6CB3B60C0BE8

FASTA10912,182
        10         20         30         40         50         60 
MTEFKAGSAK KGATLFKTRC LQCHTVEKGG PHKVGPNLHG IFGRHSGQAE GYSYTDANIK 

        70         80         90        100 
KNVLWDENNM SEYLTNPKKY IPGTKMAFGG LKKEKDRNDL ITYLKKACE 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the gene for iso-1-cytochrome c in Saccharomyces cerevisiae."
Smith M., Leung D.W., Gillam S., Astell C.R., Montgomery D.L., Hall B.D.
Cell 16:753-761(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of the yeast iso-1-cytochrome c mRNA."
Boss J.M., Gillam S., Ziotmer R.S., Smith M.
J. Biol. Chem. 256:12958-12961(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Nucleotide sequence of the COR region: a cluster of six genes in the yeast Saccharomyces cerevisiae."
Melnick L., Sherman F.
Gene 87:157-166(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Revised nucleotide sequence of the COR region of yeast Saccharomyces cerevisiae chromosome X."
Huang M.-E., Manus V., Chuat J.-C., Galibert F.
Yeast 10:811-818(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
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. expand/collapse author list , 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.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"The complete amino acid sequence in baker's yeast cytochrome c."
Narita K., Titani K.
J. Biochem. 65:259-267(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-109.
Strain: Oviformis.
[8]"Transcription initiation of the Saccharomyces cerevisiae iso-1-cytochrome c gene. Multiple, independent T-A-T-A sequences."
McNeil J.B., Smith M.
J. Mol. Biol. 187:363-378(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[9]"Studies on cytochrome c. 8. Synthesis of the protected hexadecapeptide (sequence 93-108) of Baker's yeast iso-1-cytochrome c."
Moroder L., Marchiori F., Borin G., Scoffone E.
Biopolymers 12:729-750(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS.
[10]"Enzymatic methylation of in vitro synthesized apocytochrome c enhances its transport into mitochondria."
Park K.S., Frost B., Tuck M., Ho L.L., Kim S., Paik W.K.
J. Biol. Chem. 262:14702-14708(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION.
[11]"Determinants of cytochrome c pro-apoptotic activity. The role of lysine 72 trimethylation."
Kluck R.M., Ellerby L.M., Ellerby H.M., Naiem S., Yaffe M.P., Margoliash E., Bredesen D., Mauk A.G., Sherman F., Newmeyer D.D.
J. Biol. Chem. 275:16127-16133(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-79.
[12]"Cytochrome c methyltransferase, Ctm1p, of yeast."
Polevoda B., Martzen M.R., Das B., Phizicky E.M., Sherman F.
J. Biol. Chem. 275:20508-20513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-78, MUTAGENESIS OF LYS-78.
[13]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Yeast iso-1-cytochrome c. A 2.8-A resolution three-dimensional structure determination."
Louie G.V., Hutcheon W.L., Brayer G.D.
J. Mol. Biol. 199:295-314(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]"High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c."
Louie G.V., Brayer G.D.
J. Mol. Biol. 214:527-555(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS).
[17]"Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c."
Lange C., Hunte C.
Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
[18]"Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c."
Baistrocchi P., Banci L., Bertini I., Turano P., Bren K.L., Gray H.B.
Biochemistry 35:13788-13796(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[19]"Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c."
Banci L., Bertini I., Bren K.L., Gray H.B., Sompornpisut P., Turano P.
Biochemistry 36:8992-9001(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[20]"Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer."
Solmaz S.R., Hunte C.
J. Biol. Chem. 283:17542-17549(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-109 IN THE BC1 COMPLEX, METHYLATION AT LYS-79.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37696 Genomic DNA. Translation: AAB59344.1.
V01298 Genomic DNA. Translation: CAA24605.1.
L26347 Genomic DNA. Translation: AAA62856.1.
L36344 Genomic DNA. Translation: AAA88751.1.
Z49548 Genomic DNA. Translation: CAA89576.1.
X03472 Genomic DNA. Translation: CAA27189.1.
BK006943 Genomic DNA. Translation: DAA08835.1.
PIRCCBY. A00037.
RefSeqNP_012582.1. NM_001181706.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHHX-ray1.97A2-107[»]
1CHIX-ray2.00A2-107[»]
1CHJX-ray1.90A2-107[»]
1CIEX-ray1.80A2-107[»]
1CIFX-ray1.90A2-107[»]
1CIGX-ray1.80A2-107[»]
1CIHX-ray1.80A2-107[»]
1CRGX-ray2.00A2-107[»]
1CRHX-ray1.90A2-109[»]
1CRIX-ray2.00A2-107[»]
1CRJX-ray2.05A2-107[»]
1CSUX-ray1.81A2-107[»]
1CSVX-ray1.90A2-107[»]
1CSWX-ray1.90A2-107[»]
1CSXX-ray1.90A2-107[»]
1CTYX-ray2.20A2-107[»]
1CTZX-ray1.90A2-107[»]
1FHBNMR-A2-107[»]
1IRVX-ray1.90A2-107[»]
1IRWX-ray2.00A2-107[»]
1KYOX-ray2.97W2-109[»]
1LMSNMR-A2-107[»]
1NMINMR-A2-107[»]
1RAPX-ray2.25A2-109[»]
1RAQX-ray1.90A2-109[»]
1S6VX-ray1.88B/D2-107[»]
1U74X-ray2.40B/D2-107[»]
1YCCX-ray1.23A2-109[»]
1YFCNMR-A2-107[»]
1YICNMR-A2-107[»]
2B0ZX-ray2.70B2-109[»]
2B10X-ray2.80B/D2-109[»]
2B11X-ray2.30B/D2-109[»]
2B12X-ray3.02B2-109[»]
2BCNX-ray1.70B2-107[»]
2GB8NMR-B2-109[»]
2HV4NMR-A2-107[»]
2JQRNMR-A2-107[»]
2JTINMR-B2-109[»]
2LIRNMR-A2-107[»]
2LITNMR-A2-107[»]
2ORLNMR-A2-107[»]
2PCCX-ray2.30B/D2-109[»]
2YCCX-ray1.90A2-107[»]
3CX5X-ray1.90W2-109[»]
3TYIX-ray1.40A/B2-107[»]
ProteinModelPortalP00044.
SMRP00044. Positions 2-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33801. 72 interactions.
DIPDIP-4265N.
IntActP00044. 5 interactions.
MINTMINT-8285287.
STRING4932.YJR048W.

Proteomic databases

MaxQBP00044.
PaxDbP00044.
PeptideAtlasP00044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR048W; YJR048W; YJR048W.
GeneID853507.
KEGGsce:YJR048W.

Organism-specific databases

SGDS000003809. CYC1.

Phylogenomic databases

eggNOGCOG3474.
GeneTreeENSGT00390000009405.
HOGENOMHOG000009762.
KOK08738.
OMACHNLKEG.
OrthoDBEOG71RXXT.

Enzyme and pathway databases

BioCycYEAST:G3O-31683-MONOMER.

Gene expression databases

GenevestigatorP00044.

Family and domain databases

Gene3D1.10.760.10. 1 hit.
InterProIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view]
PANTHERPTHR11961. PTHR11961. 1 hit.
PfamPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSPR00604. CYTCHRMECIAB.
SUPFAMSSF46626. SSF46626. 1 hit.
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00044.
NextBio974162.

Entry information

Entry nameCYC1_YEAST
AccessionPrimary (citable) accession number: P00044
Secondary accession number(s): D6VWL9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references