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P62894 (CYC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c
Gene names
Name:CYCS
Synonyms:CYC
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length105 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.

Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases By similarity.

Subcellular location

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

Post-translational modification

Binds 1 heme group per subunit.

Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration.

Sequence similarities

Belongs to the cytochrome c family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 105104Cytochrome c
PRO_0000108209

Sites

Metal binding191Iron (heme axial ligand)
Metal binding811Iron (heme axial ligand)
Binding site151Heme (covalent)
Binding site181Heme (covalent)

Amino acid modifications

Modified residue21N-acetylglycine Ref.2
Modified residue491Phosphotyrosine Ref.3
Modified residue981Phosphotyrosine Ref.4

Secondary structure

............ 105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62894 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AF0CA628EDF40483

FASTA10511,704
        10         20         30         40         50         60 
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW 

        70         80         90        100 
GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.
[2]"The amino acid sequence of bovine heart cytochrome c."
Nakashima T., Higa H., Matsubara H., Benson A.M., Yasunobu K.T.
J. Biol. Chem. 241:1166-1177(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2.
Tissue: Heart.
[3]"New prospects for an old enzyme: mammalian cytochrome c is tyrosine-phosphorylated in vivo."
Lee I., Salomon A.R., Yu K., Doan J.W., Grossman L.I., Huttemann M.
Biochemistry 45:9121-9128(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-49.
Tissue: Heart.
[4]"Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration."
Yu H., Lee I., Salomon A.R., Yu K., Huttemann M.
Biochim. Biophys. Acta 1777:1066-1071(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-98.
Tissue: Liver.
[5]"High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor."
Mirkin N., Jaconcic J., Stojanoff V., Moreno A.
Proteins 70:83-92(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-105, HEME-BINDING SITES.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105397 mRNA. Translation: AAI05398.1.
PIRCCBO. A92022.
RefSeqNP_001039526.1. NM_001046061.2.
XP_005194076.1. XM_005194019.1.
UniGeneBt.23981.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B4ZX-ray1.50A2-105[»]
2YBBelectron microscopy19.00Y2-105[»]
3J2Telectron microscopy9.50H/I/J/K/L/M/N2-105[»]
ProteinModelPortalP62894.
SMRP62894. Positions 2-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58978N.
IntActP62894. 1 interaction.
STRING9913.ENSBTAP00000051780.

Proteomic databases

PaxDbP62894.
PRIDEP62894.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000004594; ENSBTAP00000051780; ENSBTAG00000023823.
ENSBTAT00000007918; ENSBTAP00000007918; ENSBTAG00000022613.
GeneID100850794.
510767.
KEGGbta:100850794.
bta:510767.

Organism-specific databases

CTD54205.

Phylogenomic databases

eggNOGCOG3474.
GeneTreeENSGT00390000009405.
HOGENOMHOG000009762.
HOVERGENHBG003023.
InParanoidP62894.
KOK08738.
OMARDYLHNP.
OrthoDBEOG761BWX.
TreeFamTF300226.

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

EvolutionaryTraceP62894.
NextBio20869605.

Entry information

Entry nameCYC_BOVIN
AccessionPrimary (citable) accession number: P62894
Secondary accession number(s): P00006, Q2KJD4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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