DFFB_MOUSE
ID DFFB_MOUSE Reviewed; 344 AA.
AC O54788;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=DNA fragmentation factor subunit beta;
DE EC=3.-.-.-;
DE AltName: Full=Caspase-activated deoxyribonuclease;
DE Short=CAD;
DE Short=Caspase-activated DNase;
DE AltName: Full=DNA fragmentation factor 40 kDa subunit;
DE Short=DFF-40;
GN Name=Dffb; Synonyms=Cad;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9422506; DOI=10.1038/34112;
RA Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S.;
RT "A caspase-activated DNase that degrades DNA during apoptosis, and its
RT inhibitor ICAD.";
RL Nature 391:43-50(1998).
RN [2]
RP CHARACTERIZATION.
RX PubMed=9422513; DOI=10.1038/34214;
RA Sakahira H., Enari M., Nagata S.;
RT "Cleavage of CAD inhibitor in CAD activation and DNA degradation during
RT apoptosis.";
RL Nature 391:96-99(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Nuclease that induces DNA fragmentation and chromatin
CC condensation during apoptosis. Degrades naked DNA and induces apoptotic
CC morphology.
CC -!- ACTIVITY REGULATION: Inhibited by DFFA (DFF45).
CC -!- SUBUNIT: Heterodimer of DFFA and DFFB (By similarity). Interacts with
CC H1-1 (By similarity). {ECO:0000250|UniProtKB:O76075}.
CC -!- INTERACTION:
CC O54788; O54786: Dffa; NbExp=7; IntAct=EBI-7365197, EBI-1634519;
CC O54788; Q9D1C8: Vps28; NbExp=6; IntAct=EBI-7365197, EBI-309205;
CC O54788; O00273: DFFA; Xeno; NbExp=8; IntAct=EBI-7365197, EBI-727171;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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DR EMBL; AB009377; BAA24977.1; -; mRNA.
DR CCDS; CCDS19004.1; -.
DR RefSeq; NP_031885.3; NM_007859.4.
DR PDB; 1C9F; NMR; -; A=1-87.
DR PDB; 1F2R; NMR; -; C=1-87.
DR PDB; 1V0D; X-ray; 2.60 A; A=1-329.
DR PDBsum; 1C9F; -.
DR PDBsum; 1F2R; -.
DR PDBsum; 1V0D; -.
DR AlphaFoldDB; O54788; -.
DR BMRB; O54788; -.
DR SMR; O54788; -.
DR BioGRID; 199222; 3.
DR IntAct; O54788; 4.
DR MINT; O54788; -.
DR STRING; 10090.ENSMUSP00000030893; -.
DR PhosphoSitePlus; O54788; -.
DR MaxQB; O54788; -.
DR PaxDb; O54788; -.
DR PRIDE; O54788; -.
DR ProteomicsDB; 279642; -.
DR Antibodypedia; 3813; 540 antibodies from 37 providers.
DR DNASU; 13368; -.
DR Ensembl; ENSMUST00000030893; ENSMUSP00000030893; ENSMUSG00000029027.
DR GeneID; 13368; -.
DR KEGG; mmu:13368; -.
DR UCSC; uc008wav.2; mouse.
DR CTD; 1677; -.
DR MGI; MGI:1196287; Dffb.
DR VEuPathDB; HostDB:ENSMUSG00000029027; -.
DR eggNOG; ENOG502R0RF; Eukaryota.
DR GeneTree; ENSGT00390000014490; -.
DR HOGENOM; CLU_049235_1_1_1; -.
DR InParanoid; O54788; -.
DR OMA; AQYHGSY; -.
DR OrthoDB; 1254881at2759; -.
DR PhylomeDB; O54788; -.
DR TreeFam; TF102022; -.
DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation.
DR BioGRID-ORCS; 13368; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dffb; mouse.
DR EvolutionaryTrace; O54788; -.
DR PRO; PR:O54788; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O54788; protein.
DR Bgee; ENSMUSG00000029027; Expressed in granulocyte and 233 other tissues.
DR ExpressionAtlas; O54788; baseline and differential.
DR Genevisible; O54788; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004536; F:deoxyribonuclease activity; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004518; F:nuclease activity; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISO:MGI.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; ISO:MGI.
DR GO; GO:0006308; P:DNA catabolic process; ISO:MGI.
DR GO; GO:1902511; P:negative regulation of apoptotic DNA fragmentation; ISO:MGI.
DR InterPro; IPR003508; CIDE-N_dom.
DR InterPro; IPR039729; DFF40.
DR InterPro; IPR015311; DFF40_C.
DR InterPro; IPR044925; His-Me_finger_sf.
DR PANTHER; PTHR13067; PTHR13067; 1.
DR Pfam; PF02017; CIDE-N; 1.
DR Pfam; PF09230; DFF40; 1.
DR SMART; SM00266; CAD; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Hydrolase; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..344
FT /note="DNA fragmentation factor subunit beta"
FT /id="PRO_0000144714"
FT DOMAIN 7..83
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:1C9F"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1F2R"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1C9F"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1C9F"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1C9F"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1C9F"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1F2R"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1C9F"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 142..147
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 155..175
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:1V0D"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1V0D"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1V0D"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1V0D"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1V0D"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1V0D"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:1V0D"
SQ SEQUENCE 344 AA; 39449 MW; E854B413EA139DE1 CRC64;
MCAVLRQPKC VKLRALHSAC KFGVAARSCQ ELLRKGCVRF QLPMPGSRLC LYEDGTEVTD
DCFPGLPNDA ELLLLTAGET WHGYVSDITR FLSVFNEPHA GVIQAARQLL SDEQAPLRQK
LLADLLHHVS QNITAETREQ DPSWFEGLES RFRNKSGYLR YSCESRIRGY LREVSAYTSM
VDEAAQEEYL RVLGSMCQKL KSVQYNGSYF DRGAEASSRL CTPEGWFSCQ GPFDLESCLS
KHSINPYGNR ESRILFSTWN LDHIIEKKRT VVPTLAEAIQ DGREVNWEYF YSLLFTAENL
KLVHIACHKK TTHKLECDRS RIYRPQTGSR RKQPARKKRP ARKR
