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P00004

- CYC_HORSE

UniProt

P00004 - CYC_HORSE

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Protein

Cytochrome c

Gene

CYCS

Organism
Equus caballus (Horse)
Status
Reviewed - 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)1 PublicationPROSITE-ProRule annotation
Metal bindingi81 – 811Iron (heme axial ligand)

GO - Molecular functioni

  1. electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity Source: UniProtKB
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. apoptotic DNA fragmentation Source: UniProtKB
  2. oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP00004.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c
Gene namesi
Name:CYCS
Synonyms:CYC
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
ProteomesiUP000002281: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: UniProtKB-KW
  3. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 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 residuei98 – 981PhosphotyrosineBy 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

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 – 1411
Turni15 – 184
Beta strandi21 – 244
Beta strandi28 – 303
Turni34 – 374
Beta strandi39 – 424
Beta strandi44 – 474
Helixi51 – 544
Helixi62 – 709
Helixi72 – 754
Beta strandi76 – 783
Beta strandi86 – 883
Helixi89 – 10214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
2PCBX-ray2.80B2-105[»]
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[»]
DisProtiDP00006.
ProteinModelPortaliP00004.
SMRiP00004. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00004.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome c family.Curated

Phylogenomic databases

eggNOGiCOG3474.
HOGENOMiHOG000009762.
HOVERGENiHBG003023.
InParanoidiP00004.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[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

PIRi A00005. CCHO.
UniGenei Eca.1571.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AKK NMR - A 2-105 [» ]
1CRC X-ray 2.08 A/B 2-105 [» ]
1FI7 NMR - A 2-105 [» ]
1FI9 NMR - A 2-105 [» ]
1GIW NMR - A 2-105 [» ]
1HRC X-ray 1.90 A 2-105 [» ]
1I5T NMR - A 2-105 [» ]
1LC1 NMR - A 2-105 [» ]
1LC2 NMR - A 2-105 [» ]
1M60 NMR - A 2-105 [» ]
1OCD NMR - A 2-105 [» ]
1U75 X-ray 2.55 B 2-105 [» ]
1WEJ X-ray 1.80 F 2-105 [» ]
2FRC NMR - A 2-105 [» ]
2GIW NMR - A 2-105 [» ]
2PCB X-ray 2.80 B 2-105 [» ]
3NBS X-ray 2.20 A/B/C/D 2-105 [» ]
3NBT X-ray 2.10 A/B/C/D/E/F 2-105 [» ]
3O1Y X-ray 1.75 A/B/C 2-105 [» ]
3O20 X-ray 1.90 A/B/C 2-105 [» ]
3WC8 X-ray 1.80 A 2-105 [» ]
3WUI X-ray 1.80 A 2-105 [» ]
DisProti DP00006.
ProteinModelPortali P00004.
SMRi P00004. Positions 2-105.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36774N.
IntActi P00004. 2 interactions.
STRINGi 9796.ENSECAP00000012031.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3474.
HOGENOMi HOG000009762.
HOVERGENi HBG003023.
InParanoidi P00004.

Enzyme and pathway databases

SABIO-RK P00004.

Miscellaneous databases

EvolutionaryTracei P00004.
PMAP-CutDB P00004.

Family and domain databases

Gene3Di 1.10.760.10. 1 hit.
InterProi IPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view ]
PANTHERi PTHR11961. PTHR11961. 1 hit.
Pfami PF00034. Cytochrom_C. 1 hit.
[Graphical view ]
PRINTSi PR00604. CYTCHRMECIAB.
SUPFAMi SSF46626. SSF46626. 1 hit.
PROSITEi PS51007. CYTC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 120 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

External Data

Dasty 3