Tag Content
SG ID
SG00019110 
UniProt Accession
Theoretical PI
9.61  
Molecular Weight
11605 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Cycs 
Gene Synonyms/Alias
 
Protein Name
Cytochrome c, somatic 
Protein Synonyms/Alias
 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:19;24950227-24950702;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.020189936 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. Mouse contains two functional, but differentially expressed, cytochrome c genes. One of these genes is expressed in all somatic tissues so far examined. The other gene is expressed only in testis and is assumed to be spermatogenesis-specific. The nucleotide sequence of four mouse cytochrome c-like genes has been determined. One of these genes (MC1) contains an intron and encodes a polypeptide sequence identical to the published mouse somatic cytochrome c amino acid sequence. The other three genes can not properly encode a mouse cytochrome c protein and appear to be pseudogenes which have arisen via an insertion into the mouse genome of a cDNA copy of a cytochrome c mRNA molecule. PMID: [2987801] 

2. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

3. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

4. For immunochemical and evolutionary reasons we determined the primary structure of cytochrome c from two strains of laboratory mice. Thioacetylthioethane and thioacetylthioglycolic acid were used in addition to conventional reagents for sequence determinations. The sequence was found to be identical with that of the rabbit except for residues 44 and 89 and consistent with the peptide compositional data reported by Hennig (Hennig, B. (1975), Eur. J. Biochem. 55, 167-183). The rat cytochrome c cymotryptic peptides were identical with those of the mouse in amino acid composition and amino-terminal residues. Further, peptide maps of cytochromes c of the guinea pig and two strains of rat indicate that all these animals have the same cytochrome c as the laboratory mouse. It is concluded that rodent cytochromes c are evolutionarily conservative and that there is no evidence for a generation-time effect in cytochrome c evolution. PMID: [191069] 

5. The structure of cytochrome c during mouse development is investigated. For this purpose the amino acid sequence of cytochrome c of the adult mouse had to be determined. The structure of cytochrome c of adult differentiated mouse cells differs in two amino acid residues from the known amino acid sequence of rabbit cytochrome c. No indication of different forms of cytochrome c in the adult differentiated cells was obtained. The structure of cytochrome c from 11.5-day-old mouse embryos is identical with that of adult mouse tissues. Since germ cells after meiotic division are the immediate precursors of a new individual, the structure of cytochrome c from sperm-containing mice testes was investigated. By means of chromatography of the cytochrome c and of peptide maps and amino acid analyses of its tryptic peptides, it is shown that mouse testis contains two isocytochromes c in about equal amount. The structure of one of these two isocytochromes c is identical with the structure of the adult-type cytochrome c of mouse. The testis-specific cytochrome c, which is assumed to be located in the sperm cells, differs in 13 of its 104 amino acid residues from the adult-type cytochrome c. From comparison of the primary and the spatial structures of the adult-type and the sperm-type isocytochromes c with the known structures of cytochrome c of more than 65 different species it is concluded that the duplication of the cytochrome c structural gene, causing the existence of the two ontogenetic-specific isocytochromes c in mouse, has occurred early in the evolution of eucaryotes. PMID: [240690] 

6. Apoptotic protease activating factor-1 (Apaf-1) and cytochrome c are cofactors critical for inducing caspase-9 activation following stress-induced apoptosis. One consequence of caspase-9 activation is nuclear-cytoplasmic barrier disassembly, which is required for nuclear caspase-3 translocation. In the nucleus, caspase-3 triggers proteolysis of the caspase-activated DNA nuclease (CAD) inhibitor, causing CAD induction and subsequent DNA degradation. Here we demonstrate that apoptotic cells show perinuclear cytochrome c aggregation, which may be critical for nuclear redistribution of cytochrome c and Apaf-1. We thus indicate that the nuclear redistribution of these cofactors concurs with the previously reported caspase-9-induced nuclear disassembly, and may represent an early apoptotic hallmark. PMID: [12062423] 

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Function
Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members ofthe Bcl-2 family leads to altered mitochondrial membranepermeability resulting in release of cytochrome c into thecytosol. Binding of cytochrome c to Apaf-1 triggers the activationof caspase-9, which then accelerates apoptosis by activating othercaspases. 
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Subcellular Location
Mitochondrion intermembrane space.Note=Loosely associated with the inner membrane. 
Tissue Specificity
Found in embryos and in adult liver and heart. 
Gene Ontology
GO IDGO termEvidence
GO:0005758 C:mitochondrial intermembrane space IEA:UniProtKB-SubCell.
GO:0070469 C:respiratory chain IEA:UniProtKB-KW.
GO:0009055 F:electron carrier activity IEA:InterPro.
GO:0020037 F:heme binding IEA:InterPro.
GO:0006915 P:apoptotic process IEA:UniProtKB-KW.
GO:0022900 P:electron transport chain IEA:UniProtKB-KW.
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Interpro
IPR002327;    Cyt_c_1A/1B.
IPR009056;    Cyt_c_dom.
IPR003088;    Cyt_c_I.
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Pfam
PF00034;    Cytochrom_C;    1.
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SMART
PROSITE
PS51007;    CYTC;    1.
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PRINTS
PR00604;    CYTCHRMECIAB.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed.
CHAIN         2    105       Cytochrome c, somatic.
                             /FTId=PRO_0000108225.
METAL        19     19       Iron (heme axial ligand).
METAL        81     81       Iron (heme axial ligand).
BINDING      15     15       Heme (covalent).
BINDING      18     18       Heme (covalent).
MOD_RES       2      2       N-acetylglycine.
MOD_RES      49     49       Phosphotyrosine (By similarity).
MOD_RES      98     98       Phosphotyrosine (By similarity).
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Nucleotide Sequence
Length: 1436 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 105 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
Dlg4IntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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