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P81459

- CYC_THUAA

UniProt

P81459 - CYC_THUAA

Protein

Cytochrome c

Gene

cyc

Organism
Thunnus alalunga (Albacore) (Scomber alalunga)
Status
Reviewed - Annotation score: 4 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141Heme (covalent)
    Binding sitei17 – 171Heme (covalent)
    Metal bindingi18 – 181Iron (heme axial ligand)
    Metal bindingi80 – 801Iron (heme axial ligand)

    GO - Molecular functioni

    1. electron carrier activity Source: InterPro
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome c
    Gene namesi
    Name:cyc
    OrganismiThunnus alalunga (Albacore) (Scomber alalunga)
    Taxonomic identifieri8235 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPelagimorphariaScombriformesScombridaeThunnus

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 103103Cytochrome cPRO_0000108255Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylglycine

    Post-translational modificationi

    Binds 1 heme group per subunit.

    Keywords - PTMi

    Acetylation

    Structurei

    Secondary structure

    1
    103
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Turni14 – 174
    Beta strandi27 – 293
    Helixi50 – 545
    Helixi61 – 699
    Helixi71 – 744
    Helixi88 – 10114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I54X-ray1.50A/B1-103[»]
    1I55X-ray2.00A/B1-103[»]
    1LFMX-ray1.50A/B1-103[»]
    3CYTX-ray1.80I/O1-103[»]
    5CYTX-ray1.50R1-103[»]
    ProteinModelPortaliP81459.
    SMRiP81459. Positions 1-103.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81459.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome c family.Curated

    Phylogenomic databases

    HOVERGENiHBG003023.

    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.

    P81459-1 [UniParc]FASTAAdd to Basket

    « Hide

    GDVAKGKKTF VQKCAQCHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD    50
    ANKSKGIVWN NDTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS 100
    ATS 103
    Length:103
    Mass (Da):11,370
    Last modified:November 1, 1998 - v1
    Checksum:i1CBC776EF34A8677
    GO

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Life shuttle - Issue 76 of November 2006

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I54 X-ray 1.50 A/B 1-103 [» ]
    1I55 X-ray 2.00 A/B 1-103 [» ]
    1LFM X-ray 1.50 A/B 1-103 [» ]
    3CYT X-ray 1.80 I/O 1-103 [» ]
    5CYT X-ray 1.50 R 1-103 [» ]
    ProteinModelPortali P81459.
    SMRi P81459. Positions 1-103.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG003023.

    Miscellaneous databases

    EvolutionaryTracei P81459.

    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. "The structure of ferrocytochrome c at 2.45 A resolution."
      Takano T., Kallai O.B., Swanson R., Dickerson R.E.
      J. Biol. Chem. 248:5234-5255(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
      Tissue: Heart.
    2. "Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution."
      Takano T., Dickerson R.E.
      J. Mol. Biol. 153:79-94(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF REDUCED FORM.
      Tissue: Heart.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF REDUCED FORM.
      Tissue: Heart.
    4. "Tuna cytochrome c at 2.0 A resolution. I. Ferricytochrome structure analysis."
      Swanson R., Trus B.L., Mandel N., Mandel G., Kallai O.B., Dickerson R.E.
      J. Biol. Chem. 252:759-775(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED FORM.
      Tissue: Heart.
    5. "Tuna cytochrome c at 2.0 A resolution. II. Ferrocytochrome structure analysis."
      Takano T., Trus B.L., Mandel N., Mandel G., Kallai O.B., Swanson R., Dickerson R.E.
      J. Biol. Chem. 252:776-785(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF REDUCED FORM.
      Tissue: Heart.
    6. "Tuna cytochrome c at 2.0-A resolution. III. Coordinate optimization and comparison of structures."
      Mandel N., Mandel G., Trus B.L., Rosenburg J., Carlson G., Dickerson R.E.
      J. Biol. Chem. 252:4619-4636(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED AND REDUCED FORMS.
    7. "Redox conformation changes in refined tuna cytochrome c."
      Takano T., Dickerson R.E.
      Proc. Natl. Acad. Sci. U.S.A. 77:6371-6375(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF OXIDIZED AND REDUCED FORMS.
      Tissue: Heart.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ZN-SUBSTITUTED FORMS.
      Tissue: Heart.

    Entry informationi

    Entry nameiCYC_THUAA
    AccessioniPrimary (citable) accession number: P81459
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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