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P00004

- CYC_HORSE

UniProt

P00004 - CYC_HORSE

Protein

Cytochrome c

Gene

CYCS

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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. mitochondrial intermembrane space Source: UniProtKB-SubCell
    3. respiratory chain Source: UniProtKB-KW

    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[»]
    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

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    MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT    50
    DANKNKGITW KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK 100
    KATNE 105
    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 [» ]
    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 1, 2014
    This is version 119 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