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Protein

Cytochrome c1, heme protein, mitochondrial

Gene

CYT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heme-containing component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011Heme (covalent)
Binding sitei104 – 1041Heme (covalent)
Metal bindingi105 – 1051Iron (heme axial ligand)
Metal bindingi225 – 2251Iron (heme axial ligand)

GO - Molecular functioni

GO - Biological processi

  • mitochondrial electron transport, ubiquinol to cytochrome c Source: SGD
  • oxidative phosphorylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33605-MONOMER.
YEAST:MONOMER3O-103.

Protein family/group databases

TCDBi3.D.3.3.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c1, heme protein, mitochondrial
Alternative name(s):
Complex III subunit 4
Complex III subunit IV
Cytochrome b-c1 complex subunit 4
Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit
Short name:
Cytochrome c-1
Gene namesi
Name:CYT1
Synonyms:CTC1
Ordered Locus Names:YOR065W
ORF Names:YOR29-16
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR065W.
SGDiS000005591. CYT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei273 – 28715Helical; Note=Anchors to the membraneSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: Reactome
  • mitochondrial inner membrane Source: SGD
  • mitochondrial intermembrane space Source: Reactome
  • mitochondrial respiratory chain Source: SGD
  • mitochondrial respiratory chain complex III Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi272 – 2721K → A: Loss of RIP1 from the bc1 complex.
Mutagenesisi288 – 2881K → L: Loss of CYT1 and COB from the bc1 complex; when associated with L-289 and L-296. 1 Publication
Mutagenesisi289 – 2891K → L: Loss of CYT1 and COB from the bc1 complex; when associated with L-288 and L-296. 1 Publication
Mutagenesisi296 – 2961K → L: Loss of CYT1 and COB from the bc1 complex; when associated with L-288 and L-289. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161MitochondrionAdd
BLAST
Chaini62 – 309248Cytochrome c1, heme protein, mitochondrialPRO_0000006566Add
BLAST

Post-translational modificationi

Binds 1 heme group per subunit.

Proteomic databases

MaxQBiP07143.
PeptideAtlasiP07143.

Interactioni

Subunit structurei

Fungal cytochrome b-c1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins. Cytochrome b-c1 complex is a homodimer.

Protein-protein interaction databases

BioGridi34464. 181 interactions.
DIPiDIP-4166N.
IntActiP07143. 14 interactions.
MINTiMINT-569228.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 674Combined sources
Helixi87 – 9913Combined sources
Helixi101 – 1033Combined sources
Helixi112 – 1154Combined sources
Turni116 – 1183Combined sources
Helixi122 – 1298Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi158 – 1614Combined sources
Helixi162 – 1676Combined sources
Turni168 – 1714Combined sources
Turni180 – 1823Combined sources
Beta strandi183 – 1864Combined sources
Helixi187 – 19610Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi221 – 2255Combined sources
Helixi244 – 25916Combined sources
Helixi263 – 29634Combined sources
Beta strandi299 – 3024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30D62-306[»]
1KB9X-ray2.30D62-307[»]
1KYOX-ray2.97D/O62-309[»]
1P84X-ray2.50D62-307[»]
2IBZX-ray2.30D62-309[»]
3CX5X-ray1.90D/O62-309[»]
3CXHX-ray2.50D/O62-309[»]
4PD4X-ray3.04D62-309[»]
ProteinModelPortaliP07143.
SMRiP07143. Positions 62-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07143.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 241154Cytochrome cPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cytochrome c family.Curated
Contains 1 cytochrome c domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000012445.
HOGENOMiHOG000003867.
InParanoidiP07143.
KOiK00413.
OMAiKRPGKLA.
OrthoDBiEOG7M0P2N.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002326. Cyt_c1.
IPR021157. Cyt_c1_TM_anchor_C.
[Graphical view]
PANTHERiPTHR10266. PTHR10266. 1 hit.
PfamiPF02167. Cytochrom_C1. 1 hit.
[Graphical view]
PRINTSiPR00603. CYTOCHROMEC1.
SUPFAMiSSF46626. SSF46626. 1 hit.
SSF81496. SSF81496. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07143-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSNLSKRWA QRTLSKSFYS TATGAASKSG KLTQKLVTAG VAAAGITAST
60 70 80 90 100
LLYADSLTAE AMTAAEHGLH APAYAWSHNG PFETFDHASI RRGYQVYREV
110 120 130 140 150
CAACHSLDRV AWRTLVGVSH TNEEVRNMAE EFEYDDEPDE QGNPKKRPGK
160 170 180 190 200
LSDYIPGPYP NEQAARAANQ GALPPDLSLI VKARHGGCDY IFSLLTGYPD
210 220 230 240 250
EPPAGVALPP GSNYNPYFPG GSIAMARVLF DDMVEYEDGT PATTSQMAKD
260 270 280 290 300
VTTFLNWCAE PEHDERKRLG LKTVIILSSL YLLSIWVKKF KWAGIKTRKF

VFNPPKPRK
Length:309
Mass (Da):34,055
Last modified:April 1, 1988 - v1
Checksum:i6CB7A0813AA06AF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00791 Genomic DNA. Translation: CAA25375.1.
Z74973 Genomic DNA. Translation: CAA99258.1.
Z70678 Genomic DNA. Translation: CAA94550.1.
BK006948 Genomic DNA. Translation: DAA10844.1.
PIRiA22737. CCBY1H.
RefSeqiNP_014708.1. NM_001183484.1.

Genome annotation databases

EnsemblFungiiYOR065W; YOR065W; YOR065W.
GeneIDi854231.
KEGGisce:YOR065W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00791 Genomic DNA. Translation: CAA25375.1.
Z74973 Genomic DNA. Translation: CAA99258.1.
Z70678 Genomic DNA. Translation: CAA94550.1.
BK006948 Genomic DNA. Translation: DAA10844.1.
PIRiA22737. CCBY1H.
RefSeqiNP_014708.1. NM_001183484.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30D62-306[»]
1KB9X-ray2.30D62-307[»]
1KYOX-ray2.97D/O62-309[»]
1P84X-ray2.50D62-307[»]
2IBZX-ray2.30D62-309[»]
3CX5X-ray1.90D/O62-309[»]
3CXHX-ray2.50D/O62-309[»]
4PD4X-ray3.04D62-309[»]
ProteinModelPortaliP07143.
SMRiP07143. Positions 62-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34464. 181 interactions.
DIPiDIP-4166N.
IntActiP07143. 14 interactions.
MINTiMINT-569228.

Protein family/group databases

TCDBi3.D.3.3.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

Proteomic databases

MaxQBiP07143.
PeptideAtlasiP07143.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR065W; YOR065W; YOR065W.
GeneIDi854231.
KEGGisce:YOR065W.

Organism-specific databases

EuPathDBiFungiDB:YOR065W.
SGDiS000005591. CYT1.

Phylogenomic databases

GeneTreeiENSGT00390000012445.
HOGENOMiHOG000003867.
InParanoidiP07143.
KOiK00413.
OMAiKRPGKLA.
OrthoDBiEOG7M0P2N.

Enzyme and pathway databases

BioCyciYEAST:G3O-33605-MONOMER.
YEAST:MONOMER3O-103.

Miscellaneous databases

EvolutionaryTraceiP07143.
NextBioi976115.
PROiP07143.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002326. Cyt_c1.
IPR021157. Cyt_c1_TM_anchor_C.
[Graphical view]
PANTHERiPTHR10266. PTHR10266. 1 hit.
PfamiPF02167. Cytochrom_C1. 1 hit.
[Graphical view]
PRINTSiPR00603. CYTOCHROMEC1.
SUPFAMiSSF46626. SSF46626. 1 hit.
SSF81496. SSF81496. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of the nuclear gene for the yeast cytochrome c1 precursor reveals an unusually complex amino-terminal presequence."
    Sadler I., Suda K., Schatz G., Kaudewitz F., Haid A.
    EMBO J. 3:2137-2143(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the presence of two tRNAs and 24 new open reading frames."
    Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.
    Yeast 13:379-390(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment."
    Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.
    Structure 8:669-684(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  7. "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), MUTAGENESIS OF LYS-288; LYS-289 AND LYS-296.

Entry informationi

Entry nameiCY1_YEAST
AccessioniPrimary (citable) accession number: P07143
Secondary accession number(s): D6W2C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 11, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 39900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.