Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
11714 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
Cytochrome c, testis-specific 
Protein Synonyms/Alias
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
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.
Temporarily unavailable 
Abstract of related literatures
1. Mammalian testis contains two forms of cytochrome c, one identical to the form found in somatic tissues and a second that is expressed in a stage-specific manner during spermatogenic differentiation. We have isolated both rat and mouse cDNA clones and the rat gene encoding the testis-specific cytochrome c and determined their DNA sequences. The testicular variant displays a number of notable differences with its somatic counterpart. 1) In contrast to the multipseudogene family derived from mammalian somatic cytochrome c genes, the testis gene is single-copy in genomic DNA with no detectable pseudogenes. 2) The rat testis gene is approximately 7 kilobases (kb) long with three introns totaling nearly 6.5 kb whereas the two introns dividing the 2.1-kb somatic gene occupy only 0.9 kb. Introns differ in position as well as size. 3) The testicular variant has a longer 5'-untranslated leader (230 versus 70 base pairs for the somatic gene) with an upstream open reading frame of 129 base pairs beginning with an AUG in a favorable translational context. 4) A single polyadenylation site in the testicular mRNA (approximately 900 nucleotides) contrasts with the three functionally equivalent sites observed in rat somatic messages. 5) Finally, rat and mouse testis cytochromes c differ at 4 amino acid residues as opposed to the complete sequence identity found in the somatic proteins suggesting a shorter unit evolutionary period for these molecules. These observations are consistent with a duplication of an ancestral cytochrome c gene leading to the emergence of novel structural features and regulatory properties likely associated with the striking tissue specificity of the testicular cytochrome c. PMID: [2834389] 

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 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] 

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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 (By similarity). 
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Subcellular Location
Mitochondrion intermembrane space.Note=Loosely associated with the inner membrane. 
Tissue Specificity
This is one of two isocytochromes C found inthe testis. The other is identical with the form found in othermouse tissues. These cytochromes are assumed to be located in thesperm. 
Gene Ontology
GO IDGO termEvidence
GO:0005758 C:mitochondrial intermembrane space IEA:UniProtKB-SubCell.
GO:0005739 C:mitochondrion IDA:MGI.
GO:0070469 C:respiratory chain IEA:UniProtKB-KW.
GO:0009055 F:electron carrier activity IEA:InterPro.
GO:0020037 F:heme binding IDA:MGI.
GO:0006915 P:apoptotic process IDA:MGI.
GO:0022900 P:electron transport chain IEA:UniProtKB-KW.
GO:0042743 P:hydrogen peroxide metabolic process IDA:MGI.
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IPR002327;    Cyt_c_1A/1B.
IPR009056;    Cyt_c_dom.
IPR003088;    Cyt_c_I.
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PF00034;    Cytochrom_C;    1.
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PS51007;    CYTC;    1.
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PR00604;    CYTCHRMECIAB.;   
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Created Date
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed.
CHAIN         2    105       Cytochrome c, testis-specific.
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).
HELIX         4     14
TURN         15     18
STRAND       39     42
HELIX        51     55
HELIX        62     70
HELIX        72     75
HELIX        89    104
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Nucleotide Sequence
Length: 620 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 105 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
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