Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome c

Gene

cyc

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

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
Complete GO annotation...

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPelagiariaScombriformesScombridaeThunnus

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
Complete GO annotation...

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 – 1311Combined sources
Turni14 – 174Combined sources
Beta strandi27 – 293Combined sources
Helixi50 – 545Combined sources
Helixi61 – 699Combined sources
Helixi71 – 744Combined sources
Helixi88 – 10114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
[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

        10         20         30         40         50
GDVAKGKKTF VQKCAQCHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD
60 70 80 90 100
ANKSKGIVWN NDTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS

ATS
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:
PDBei
RCSB PDBi
PDBji
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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003023.

Miscellaneous databases

EvolutionaryTraceiP81459.

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. "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(1972) [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(1980) [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(1976) [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(1976) [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(1976) [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(1979) [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: January 7, 2015
This is version 91 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

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 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.