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Reviewed, UniProtKB/Swiss-Prot P00029 (CYC_ASTRU)

Last modified July 22, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytochrome c
OrganismAsterias rubens (Common European starfish)
Taxonomic identifier7604 [NCBI]
Taxonomic lineageEukaryotaMetazoaEchinodermataEleutherozoaAsterozoaAsteroideaForcipulataceaForcipulatidaAsteriidaeAsterias

Protein attributes

Sequence length104 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Subcellular location

Mitochondrion matrix.

Post-translational modification

Binds 1 heme group per subunit.

Sequence similarities

Belongs to the cytochrome c family.

Ontologies

Keywords

   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMitochondrion
   LigandHeme
Iron
Metal-binding
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Initiator methionine11Removed
Chain2 – 104103Cytochrome c

Sites

Metal binding191Iron (heme axial ligand)
Metal binding811Iron (heme axial ligand)
Binding site151Heme (covalent)
Binding site181Heme (covalent)

Sequences

Sequence LengthMass (Da)Tools
P00029-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A0984E9258A7F154

FASTA10411,661
        10         20         30         40         50         60 
MGQVEKGKKI FVQRCAQCHT VEKAGKHKTG PNLNGILGRK TGQAAGFSYT DANRNKGITW 

        70         80         90        100 
KNETLFEYLE NPKKYIPGTK MVFAGLKKQK ERQDLIAYLE AATK 

« Hide

References

[1]"The amino acid sequence of cytochrome c from Asterias rubens L. (common starfish)."
Lyddiatt A., Boulter D.
FEBS Lett. 67:331-334(1976) [PubMed: 183984] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-104.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

PIRCCSF. A00026.

3D structure databases

HSSPHSSP built from PDB template 2PCB based on UniProtKB P00004.
SMRP00029. Positions 2-103.
ModBaseSearch...

Family and domain databases

InterProIPR009056. Cyt_c_monohaem.
IPR003088. Cyt_CI.
IPR002327. Cyt_CIAB.
[Graphical view]
Gene3DG3DSA:1.10.760.10. Cytochrome_c_R. 1 hit.
PANTHERPTHR11961. Cyt_CIAB. 1 hit.
PfamPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSPR00604. CYTCHRMECIAB.
ProDomPD000375. Cyt_CIAB. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameCYC_ASTRU
AccessionPrimary (citable) accession number: P00029
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2008
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents