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P00004 (CYC_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

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 By similarity.

Miscellaneous

Mules and hinnies are heterozygous, having equal amount of horse and donkey cytochromes c.

Sequence similarities

Belongs to the cytochrome c family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 105104Cytochrome c
PRO_0000108217

Sites

Metal binding191Iron (heme axial ligand) Ref.2
Metal binding811Iron (heme axial ligand)
Binding site151Heme (covalent)
Binding site181Heme (covalent)

Amino acid modifications

Modified residue21N-acetylglycine Ref.1
Modified residue491Phosphotyrosine By similarity
Modified residue981Phosphotyrosine By similarity

Secondary structure

........................ 105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00004 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 659BA128E53C3868

FASTA10511,833
        10         20         30         40         50         60 
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT DANKNKGITW 

        70         80         90        100 
KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE 

« Hide

References

[1]"Amino-acid sequence of horse heart cytochrome c."
Margoliash E., Smith E.L., Kreil G., Tuppy H.
Nature 192:1125-1127(1961) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2.
Tissue: Heart.
[2]"Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8-A resolution."
Dickerson R.E., Takano T., Eisenberg D., Kallai O.B., Samson L., Cooper A., Margoliash E.
J. Biol. Chem. 246:1511-1535(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[3]"High-resolution three-dimensional structure of horse heart cytochrome c."
Bushnell G.W., Louie G.V., Brayer G.D.
J. Mol. Biol. 214:585-595(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[4]"The low ionic strength crystal structure of horse cytochrome c at 2.1-A resolution and comparison with its high ionic strength counterpart."
Sanishvili R., Volz K.W., Westbrook E.M., Margoliash E.
Structure 3:707-716(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[5]"Proton resonance assignments of horse ferricytochrome c."
Feng Y., Roder H., Englander S.W., Wand A.J., di Stefano D.L.
Biochemistry 28:195-203(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[6]"Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution 1H NMR."
Qi P.X., Beckman R.A., Wand A.J.
Biochemistry 35:12275-12286(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[7]"Solution structure of oxidized horse heart cytochrome c."
Banci L., Bertini I., Gray H.B., Luchinat C., Reddig T., Rosato A., Turano P.
Biochemistry 36:9867-9877(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Tissue: Heart.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

PIRCCHO. A00005.
UniGeneEca.1571.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKKNMR-A2-105[»]
1CRCX-ray2.08A/B2-105[»]
1FI7NMR-A2-104[»]
1FI9NMR-A2-104[»]
1GIWNMR-A2-104[»]
1HRCX-ray1.90A2-105[»]
1I5TNMR-A2-104[»]
1LC1NMR-A2-104[»]
1LC2NMR-A2-104[»]
1M60NMR-A2-104[»]
1OCDNMR-A2-105[»]
1U75X-ray2.55B2-104[»]
1WEJX-ray1.80F2-104[»]
2FRCNMR-A2-105[»]
2GIWNMR-A2-104[»]
2PCBX-ray2.80B2-104[»]
3NBSX-ray2.20A/B/C/D2-105[»]
3NBTX-ray2.10A/B/C/D/E/F2-105[»]
3O1YX-ray1.75A/B/C2-105[»]
3O20X-ray1.90A/B/C2-105[»]
3WC8X-ray1.80A2-105[»]
DisProtDP00006.
ProteinModelPortalP00004.
SMRP00004. Positions 2-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36774N.
IntActP00004. 2 interactions.
STRING9796.ENSECAP00000012031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3474.
HOGENOMHOG000009762.
HOVERGENHBG003023.
InParanoidP00004.

Enzyme and pathway databases

SABIO-RKP00004.

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

EvolutionaryTraceP00004.
PMAP-CutDBP00004.

Entry information

Entry nameCYC_HORSE
AccessionPrimary (citable) accession number: P00004
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 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