CYT-C-D (Drosophila melanogaster)
Description [+]
- Synonyms: CYT-C-D, CYTOCHROME C-1, CYTOCHROME C-DISTAL, CYTC1, DC3
- Species: Metazoa;Bilateria;Ecdysozoa;Arthropoda;Hexapoda; Drosophila melanogaster
- Short gene description: NA
- Family: other
- Process:
- Pathways:
- Criteria: manually curated
- Curator comment: The role of cytochrome c on apoptosis in Drosophila is still unclear since there is not a classical mitochondrial pathway. However, cyt.c seems to participate in apoptosis of some cell types [Pubmed Link: 12737804]
- WIKI: CYT-C-D-D_melanogaster
References [+]
- Living with death: the evolution of the mitochondrial pathway of apoptosis in animals.
- Oberst A, Bender C, Green DR
- The mitochondrial pathway of cell death, in which apoptosis proceeds following mitochondrial outer membrane permeabilization, release of cytochrome c, and APAF-1 apoptosome-mediated caspase activation, represents the major pathway of physiological apoptosis in vertebrates. However, the well-characterized apoptotic pathways of the invertebrates C. elegans and D. melanogaster indicate that this apoptotic pathway is not universally conserved among animals. This review will compare the role of the mitochondria in the apoptotic programs of mammals, nematodes, and flies, and will survey our knowledge of the apoptotic pathways of other, less familiar model organisms in an effort to explore the evolutionary origins of the mitochondrial pathway of apoptosis. Cell Death Differ. 2008 Jul;15(7):1139-46. Epub 2008 May 2.
- Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila.
- Arama E, Agapite J, Steller H
- The final stage of spermatid terminal differentiation involves the removal of their bulk cytoplasm in a process known as spermatid individualization. Here we show that apoptotic proteins play an essential role during spermatid individualization in Drosophila melanogaster. Several aspects of sperm terminal differentiation, including the activation of caspases, are reminiscent of apoptosis. Notably, caspase inhibitors prevent the removal of bulk cytoplasm in spermatids and block sperm maturation in vivo, causing male sterility. We further identified loss-of-function mutations in one of the two Drosophila cyt-c genes, cyt-c-d, which block caspase activation and subsequent spermatid terminal differentiation. Finally, a giant ubiquitin-conjugating enzyme, dBruce, is required to protect the sperm nucleus against hypercondensation and degeneration. These observations suggest that an apoptosis-like mechanism is required for spermatid differentiation in Drosophila. Dev Cell. 2003 May;4(5):687-97.
- Altered cytochrome c display precedes apoptotic cell death in Drosophila.
- Varkey J, Chen P, Jemmerson R, Abrams JM
- Drosophila affords a genetically well-defined system to study apoptosis in vivo. It offers a powerful extension to in vitro models that have implicated a requirement for cytochrome c in caspase activation and apoptosis. We found that an overt alteration in cytochrome c anticipates programmed cell death (PCD) in Drosophila tissues, occurring at a time that considerably precedes other known indicators of apoptosis. The altered configuration is manifested by display of an otherwise hidden epitope and occurs without release of the protein into the cytosol. Conditional expression of the Drosophila death activators, reaper or grim, provoked apoptogenic cytochrome c display and, surprisingly, caspase activity was necessary and sufficient to induce this alteration. In cell-free studies, cytosolic caspase activation was triggered by mitochondria from apoptotic cells but identical preparations from healthy cells were inactive. Our observations provide compelling validation of an early role for altered cytochrome c in PCD and suggest propagation of apoptotic physiology through reciprocal, feed-forward amplification involving cytochrome c and caspases. J Cell Biol. 1999 Feb 22;144(4):701-10.
Structure & Sequence [+]
Pfam domains:
(Pfam is a large collection of protein families.)
| Source | Domain Name | Start | End |
|---|---|---|---|
| PFAM A | Cytochrom_C | 6 | 105 |
Protein sequence [+]
Cyt-c-d | Drosophila melanogaster | 7227 | length:105
MGSGDAENGKKIFVQKCAQCHTYEVGGKHKVGPNLGGVVGRKCGTAAGYKYTDANIKKGV
TWTEGNLDEYLKDPKKYIPGTKMVFAGLKKAEERADLIAFLKSNK
TWTEGNLDEYLKDPKKYIPGTKMVFAGLKKAEERADLIAFLKSNK
Evolution [+]
View protein alignment and tree with Jalview:
Explore tree at phylomeDB: Click here.
Homologs list [+]
DeathBase uses Jalview, an external application that requires Java. Please, check that you have the latest version of Java
installed and that Java is enabled in your browser. When correctly installed your browser should display the following examples properly. You can download the latest version of Java at Java Download Site.
Gene Ontology [+]
| GO id | Name | Ontology type | Evidence |
|---|---|---|---|
| GO:0006024 | glycosaminoglycan biosynthetic process | biological_proccess | IEA |
| GO:0016857 | racemase and epimerase activity, acting on carbohydrates and derivatives | mollecular_function | IEA |
| GO:0003824 | catalytic activity | mollecular_function | IEA |
| GO:0016021 | integral to membrane | cell_component | IEA |
Check GO Evidence Codes here
Information from other databases [+]
- Gene info from FyBase [?] FBgn0086907
- Ensembl genome browser [?] : FBgn0086907
- Expression info from Arrayexpress [?] : FBgn0086907
- Protein expression from Protein Atlas: [?] FBgn0086907
Click on [?] for more information.
