DFFA

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

DNA Fragmentation factor 45kDa, C terminal domain
DNA Fragmentation factor 45kDa, C terminal domain
	nmr structure of dff-c domain
Identifiers
Symbol	DFF-C
Pfam	PF09033
InterPro	IPR015121
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

DFFA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1IBX, 1IYR, 1KOY
Identifiers
Aliases	DFFA, DFF-45, DFF1, ICAD, DNA fragmentation factor subunit alpha
External IDs	OMIM: 601882 MGI: 1196227 HomoloGene: 3240 GeneCards: DFFA
Gene location (Human)
Chr.	Chromosome 1 (human)
End	10,472,529 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	149,205,104 bp
RNA expression pattern
	Top expressed in
	internal globus pallidus; ; inferior ganglion of vagus nerve; ; nipple; ; cardia; ; ventral tegmental area; ; stromal cell of endometrium; ; renal medulla; ; subthalamic nucleus; ; islet of Langerhans; ; optic nerve;
	Top expressed in
	soleus muscle; ; yolk sac; ; medulla oblongata; ; lip; ; pons; ; quadriceps femoris muscle; ; zone of skin; ; primary motor cortex; ; tibialis anterior muscle; ; esophagus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding; protein domain specific binding; protein folding chaperone activity; deoxyribonuclease inhibitor activity;
Cellular component	cytosol; lipid droplet; intracellular anatomical structure; nucleus; nucleoplasm; cytoplasm; plasma membrane;
Biological process	positive regulation of apoptotic process; negative regulation of execution phase of apoptosis; negative regulation of apoptotic DNA fragmentation; apoptotic DNA fragmentation; thymocyte apoptotic process; apoptotic process; negative regulation of deoxyribonuclease activity; chaperone-mediated protein folding;
	Sources:Amigo / QuickGO
Orthologs
	1676
	13347
	ENSG00000160049
	ENSMUSG00000028974
	O00273
	O54786
	NM_213566; NM_004401
	NM_001025296; NM_010044
	NP_004392; NP_998731; NP_998731.1
	NP_001020467; NP_034174
	Wikidata
View/Edit Human	View/Edit Mouse

DNA fragmentation factor subunit alpha (DFFA), also known as Inhibitor of caspase-activated DNase (ICAD), is a protein that in humans is encoded by the DFFA gene.^[5]^[6]^[7]

Template:PBB Summary

The C-terminal domain of DFFA (DFF-C) consists of four alpha-helices, which are folded in a helix-packing arrangement, with alpha-2 and alpha-3 packing against a long C-terminal helix (alpha-4). The main function of this domain is the inhibition of DFFB by binding to its C-terminal catalytic domain through ionic interactions, thereby inhibiting the fragmentation of DNA in the apoptotic process. In addition to blocking the DNase activity of DFFB, the C-terminal region of DFFA is also important for the DFFB-specific folding chaperone activity, as demonstrated by the ability of DFFA to refold DFFB.^[8]

Interactions

DFFA has been shown to interact with DFFB.^[9]^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000160049 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028974 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Leek JP, Carr IM, Bell SM, Markham AF, Lench NJ (Jun 1998). "Assignment of the DNA fragmentation factor gene (DFFA) to human chromosome bands 1p36.3→p36.2 by in situ hybridization". Cytogenet. Cell Genet. 79 (3–4): 212–3. doi:10.1159/000134725. PMID 9605855.
^ Liu X, Zou H, Slaughter C, Wang X (May 1997). "DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis". Cell. 89 (2): 175–84. doi:10.1016/S0092-8674(00)80197-X. PMID 9108473.
^ "Entrez Gene: DFFA DNA fragmentation factor, 45kDa, alpha polypeptide".
^ Fukushima K, Kikuchi J, Koshiba S, Kigawa T, Kuroda Y, Yokoyama S (August 2002). "Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation". J. Mol. Biol. 321 (2): 317–27. doi:10.1016/S0022-2836(02)00588-0. PMID 12144788.
^ Ewing, Rob M; Chu Peter; Elisma Fred; Li Hongyan; Taylor Paul; Climie Shane; McBroom-Cerajewski Linda; Robinson Mark D; O'Connor Liam; Li Michael; Taylor Rod; Dharsee Moyez; Ho Yuen; Heilbut Adrian; Moore Lynda; Zhang Shudong; Ornatsky Olga; Bukhman Yury V; Ethier Martin; Sheng Yinglun; Vasilescu Julian; Abu-Farha Mohamed; Lambert Jean-Philippe; Duewel Henry S; Stewart Ian I; Kuehl Bonnie; Hogue Kelly; Colwill Karen; Gladwish Katharine; Muskat Brenda; Kinach Robert; Adams Sally-Lin; Moran Michael F; Morin Gregg B; Topaloglou Thodoros; Figeys Daniel (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1). England: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. {{cite journal}}: Cite has empty unknown parameters: |laysource=, |laydate=, and |laysummary= (help)
^ McCarty, J S; Toh S Y; Li P (Oct 1999). "Study of DFF45 in its role of chaperone and inhibitor: two independent inhibitory domains of DFF40 nuclease activity". Biochem. Biophys. Res. Commun. 264 (1). UNITED STATES: 176–80. doi:10.1006/bbrc.1999.1497. ISSN 0006-291X. PMID 10527860. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysummary=, and |laysource= (help)

Interactions

References

Further reading