P62894 (CYC_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytochrome c | ||||
| Gene names |
| ||||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 105 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases By similarity. |
| Subcellular location | Mitochondrion intermembrane space. Note: Loosely associated with the inner membrane. |
| Post-translational modification | Binds 1 heme group per subunit. Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. |
| Sequence similarities | Belongs to the cytochrome c family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Apoptosis Electron transport Respiratory chain Transport |
| Cellular component | Mitochondrion |
| Ligand | Heme Iron Metal-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chainInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial intermembrane space 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 iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||
Molecule processing | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | |||||||||||||||||
| Chain | 2 – 105 | 104 | Cytochrome c | PRO_0000108209 | ||||||||||||||||
Sites | ||||||||||||||||||||
| Metal binding | 19 | 1 | Iron (heme axial ligand) | |||||||||||||||||
| Metal binding | 81 | 1 | Iron (heme axial ligand) | |||||||||||||||||
| Binding site | 15 | 1 | Heme (covalent) | |||||||||||||||||
| Binding site | 18 | 1 | Heme (covalent) | |||||||||||||||||
Amino acid modifications | ||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylglycine Ref.2 | |||||||||||||||||
| Modified residue | 49 | 1 | Phosphotyrosine Ref.3 | |||||||||||||||||
| Modified residue | 98 | 1 | Phosphotyrosine Ref.4 | |||||||||||||||||
Secondary structure | ||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||
| Helix | 4 – 14 | 11 | ||||||||||||||||||
| Turn | 15 – 18 | 4 | ||||||||||||||||||
| Helix | 51 – 55 | 5 | ||||||||||||||||||
| Helix | 62 – 68 | 7 | ||||||||||||||||||
| Helix | 72 – 75 | 4 | ||||||||||||||||||
| Helix | 89 – 102 | 14 | ||||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus. |
| [2] | "The amino acid sequence of bovine heart cytochrome c." Nakashima T., Higa H., Matsubara H., Benson A.M., Yasunobu K.T. J. Biol. Chem. 241:1166-1177(1966) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2. Tissue: Heart. |
| [3] | "New prospects for an old enzyme: mammalian cytochrome c is tyrosine-phosphorylated in vivo." Lee I., Salomon A.R., Yu K., Doan J.W., Grossman L.I., Huttemann M. Biochemistry 45:9121-9128(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-49. Tissue: Heart. |
| [4] | "Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration." Yu H., Lee I., Salomon A.R., Yu K., Huttemann M. Biochim. Biophys. Acta 1777:1066-1071(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-98. Tissue: Liver. |
| [5] | "High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor." Mirkin N., Jaconcic J., Stojanoff V., Moreno A. Proteins 70:83-92(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-105, HEME-BINDING SITES. |
| + | Additional computationally mapped references. |
Web resources
| Protein Spotlight Life shuttle - Issue 76 of November 2006 |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BC105397 mRNA. Translation: AAI05398.1. | ||||||||||||||||||||||||
| IPI | IPI00906486. | ||||||||||||||||||||||||
| PIR | CCBO. A92022. | ||||||||||||||||||||||||
| RefSeq | NP_001039526.1. NM_001046061.2. XP_003582877.1. XM_003582829.1. XP_003582879.1. XM_003582831.1. XP_003586721.1. XM_003586673.1. | ||||||||||||||||||||||||
| UniGene | Bt.23981. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| ProteinModelPortal | P62894. | ||||||||||||||||||||||||
| SMR | P62894. Positions 2-105. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| DIP | DIP-58978N. | ||||||||||||||||||||||||
| IntAct | P62894. 1 interaction. | ||||||||||||||||||||||||
| STRING | 9913.ENSBTAP00000051780. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PaxDb | P62894. | ||||||||||||||||||||||||
| PRIDE | P62894. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENSBTAT00000004594; ENSBTAP00000051780; ENSBTAG00000023823. ENSBTAT00000007918; ENSBTAP00000007918; ENSBTAG00000022613. | ||||||||||||||||||||||||
| GeneID | 100847700. 100850794. 510767. | ||||||||||||||||||||||||
| KEGG | bta:100847700. bta:100850794. bta:510767. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 54205. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | COG3474. | ||||||||||||||||||||||||
| GeneTree | ENSGT00390000009405. | ||||||||||||||||||||||||
| HOGENOM | HOG000009762. | ||||||||||||||||||||||||
| HOVERGEN | HBG003023. | ||||||||||||||||||||||||
| InParanoid | P62894. | ||||||||||||||||||||||||
| KO | K08738. | ||||||||||||||||||||||||
| OMA | IAYLKQY. | ||||||||||||||||||||||||
| OrthoDB | EOG45DWQX. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | CATTLE:510767-MONOMER. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P62894. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR002327. Cyt_c_1A/1B. IPR009056. Cyt_c_dom. IPR003088. Cyt_c_I. [Graphical view] | ||||||||||||||||||||||||
| PANTHER | PTHR11961. PTHR11961. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00034. Cytochrom_C. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR00604. CYTCHRMECIAB. | ||||||||||||||||||||||||
| SUPFAM | SSF46626. Cytochrome_c. 1 hit. | ||||||||||||||||||||||||
| PROSITE | PS51007. CYTC. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | P62894. | ||||||||||||||||||||||||
| NextBio | 20869605. | ||||||||||||||||||||||||
Entry information
| Entry name | CYC_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P62894 Secondary accession number(s): P00006, Q2KJD4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |

Clusters with
