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P81459 (CYC_THUAA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
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 intermembrane space. Note: Loosely associated with the inner membrane.

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
   PTMAcetylation
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processoxidation-reduction process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial intermembrane space

Inferred from electronic annotation. Source: UniProtKB-SubCell

respiratory chain

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 103103Cytochrome c
PRO_0000108255

Sites

Metal binding181Iron (heme axial ligand)
Metal binding801Iron (heme axial ligand)
Binding site141Heme (covalent)
Binding site171Heme (covalent)

Amino acid modifications

Modified residue11N-acetylglycine

Secondary structure

.............. 103
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81459 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 1CBC776EF34A8677

FASTA10311,370
        10         20         30         40         50         60 
GDVAKGKKTF VQKCAQCHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD ANKSKGIVWN 

        70         80         90        100 
NDTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS ATS 

« Hide

References

[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]"Internal mobility of ferrocytochrome c."
Northrup S.H., Pear M.R., McCammon J.A., Karplus M., Takano T.
Nature 287:659-660(1980) [PubMed] [Europe PMC] [Abstract]
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]"Electron tunneling in protein crystals."
Tezcan F.A., Crane B.R., Winkler J.R., Gray H.B.
Proc. Natl. Acad. Sci. U.S.A. 98:5002-5006(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ZN-SUBSTITUTED FORMS.
Tissue: Heart.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP81459.
SMRP81459. Positions 1-103.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003023.

Family and domain databases

Gene3D1.10.760.10. 1 hit.
InterProIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view]
PANTHERPTHR11961. PTHR11961. 1 hit.
PfamPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSPR00604. CYTCHRMECIAB.
SUPFAMSSF46626. SSF46626. 1 hit.
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81459.

Entry information

Entry nameCYC_THUAA
AccessionPrimary (citable) accession number: P81459
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references