Reviewed,
UniProtKB/Swiss-Prot P00071 (CYC_PASSA)
Last modified
November 24, 2009.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome c |
| Organism | Pastinaca sativa (Parsnip) |
| Taxonomic identifier | 4041 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apiaceae incertae sedis › Tordylieae › Pastinaca |
Protein attributes
| Sequence length | 111 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| Post-translational modification | Binds 1 heme group per subunit. |
| Sequence similarities | Belongs to the cytochrome c family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Respiratory chain Transport |
| Cellular component | Mitochondrion |
| Ligand | Heme Iron Metal-binding |
| PTM | Acetylation Methylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 111 | 111 | Cytochrome c | PRO_0000108304 | |||||
Sites | |||||||||
| Metal binding | 26 | 1 | Iron (heme axial ligand) | ||||||
| Metal binding | 88 | 1 | Iron (heme axial ligand) | ||||||
| Binding site | 22 | 1 | Heme (covalent) | ||||||
| Binding site | 25 | 1 | Heme (covalent) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylalanine Ref.1 | ||||||
| Modified residue | 80 | 1 | N6,N6,N6-trimethyllysine Ref.1 | ||||||
| Modified residue | 94 | 1 | N6,N6,N6-trimethyllysine Ref.1 | ||||||
Sequences
References
| [1] | "The amino acid sequences of cytochrome c from four plant sources." Brown R.H., Boulter D. Biochem. J. 137:93-100(1974) [PubMed: 4362498] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | CCPZ. A00063. |
3D structure databases | |
| SMR | P00071. Positions 1-111. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002327. Cyt_c_1A/1B. IPR003088. Cyt_c_I. IPR009056. Cyt_c_monohaem. [Graphical view] |
| Gene3D | G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit. |
| PANTHER | PTHR11961. Cyt_CIAB. 1 hit. |
| Pfam | PF00034. Cytochrom_C. 1 hit. [Graphical view] |
| PRINTS | PR00604. CYTCHRMECIAB. |
| PROSITE | PS51007. CYTC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYC_PASSA | ||||||||
| Accession | Primary (citable) accession number: P00071 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


