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Protein

Cytochrome c

Gene

CYCS

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151Heme (covalent)
Binding sitei18 – 181Heme (covalent)
Metal bindingi19 – 191Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication
Metal bindingi81 – 811Iron (heme axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP00004.

Protein family/group databases

MoonProtiP00004.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c
Gene namesi
Name:CYCS
Synonyms:CYC
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 105104Cytochrome cPRO_0000108217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei49 – 491PhosphotyrosineBy similarity
Modified residuei56 – 561N6-succinyllysineBy similarity
Modified residuei73 – 731N6-acetyllysine; alternateBy similarity
Modified residuei73 – 731N6-succinyllysine; alternateBy similarity
Modified residuei98 – 981PhosphotyrosineBy similarity
Modified residuei100 – 1001N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00004.
PeptideAtlasiP00004.

PTM databases

iPTMnetiP00004.

Miscellaneous databases

PMAP-CutDBP00004.

Interactioni

Protein-protein interaction databases

DIPiDIP-36774N.
IntActiP00004. 2 interactions.
STRINGi9796.ENSECAP00000012031.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Turni15 – 184Combined sources
Beta strandi21 – 244Combined sources
Beta strandi28 – 303Combined sources
Turni34 – 374Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 474Combined sources
Helixi51 – 544Combined sources
Helixi62 – 709Combined sources
Helixi72 – 754Combined sources
Beta strandi76 – 783Combined sources
Beta strandi86 – 883Combined sources
Helixi89 – 10214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKKNMR-A2-105[»]
1CRCX-ray2.08A/B2-105[»]
1FI7NMR-A2-105[»]
1FI9NMR-A2-105[»]
1GIWNMR-A2-105[»]
1HRCX-ray1.90A2-105[»]
1I5TNMR-A2-105[»]
1LC1NMR-A2-105[»]
1LC2NMR-A2-105[»]
1M60NMR-A2-105[»]
1OCDNMR-A2-105[»]
1U75X-ray2.55B2-105[»]
1WEJX-ray1.80F2-105[»]
2FRCNMR-A2-105[»]
2GIWNMR-A2-105[»]
2N3BNMR-A2-105[»]
2PCBX-ray2.80B2-105[»]
3JBTelectron microscopy3.80B/D/F/H/J/L/N1-105[»]
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[»]
3WUIX-ray1.80A2-105[»]
4NFGX-ray2.11B2-105[»]
4RSZX-ray2.19A/B/C/D/E/F2-105[»]
DisProtiDP00006.
ProteinModelPortaliP00004.
SMRiP00004. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00004.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome c family.Curated

Phylogenomic databases

eggNOGiKOG3453. Eukaryota.
COG3474. LUCA.
HOGENOMiHOG000009762.
HOVERGENiHBG003023.
InParanoidiP00004.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT
60 70 80 90 100
DANKNKGITW KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK

KATNE
Length:105
Mass (Da):11,833
Last modified:January 23, 2007 - v2
Checksum:i659BA128E53C3868
GO

Sequence databases

PIRiA00005. CCHO.
UniGeneiEca.1571.

Cross-referencesi

Web resourcesi

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Sequence databases

PIRiA00005. CCHO.
UniGeneiEca.1571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKKNMR-A2-105[»]
1CRCX-ray2.08A/B2-105[»]
1FI7NMR-A2-105[»]
1FI9NMR-A2-105[»]
1GIWNMR-A2-105[»]
1HRCX-ray1.90A2-105[»]
1I5TNMR-A2-105[»]
1LC1NMR-A2-105[»]
1LC2NMR-A2-105[»]
1M60NMR-A2-105[»]
1OCDNMR-A2-105[»]
1U75X-ray2.55B2-105[»]
1WEJX-ray1.80F2-105[»]
2FRCNMR-A2-105[»]
2GIWNMR-A2-105[»]
2N3BNMR-A2-105[»]
2PCBX-ray2.80B2-105[»]
3JBTelectron microscopy3.80B/D/F/H/J/L/N1-105[»]
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[»]
3WUIX-ray1.80A2-105[»]
4NFGX-ray2.11B2-105[»]
4RSZX-ray2.19A/B/C/D/E/F2-105[»]
DisProtiDP00006.
ProteinModelPortaliP00004.
SMRiP00004. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36774N.
IntActiP00004. 2 interactions.
STRINGi9796.ENSECAP00000012031.

Protein family/group databases

MoonProtiP00004.

PTM databases

iPTMnetiP00004.

Proteomic databases

PaxDbiP00004.
PeptideAtlasiP00004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3453. Eukaryota.
COG3474. LUCA.
HOGENOMiHOG000009762.
HOVERGENiHBG003023.
InParanoidiP00004.

Enzyme and pathway databases

SABIO-RKP00004.

Miscellaneous databases

EvolutionaryTraceiP00004.
PMAP-CutDBP00004.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. Cited for: STRUCTURE BY NMR.
    Tissue: Heart.

Entry informationi

Entry nameiCYC_HORSE
AccessioniPrimary (citable) accession number: P00004
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

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.