ID   DFFB_RAT                Reviewed;         349 AA.
AC   Q99N34;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 125.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=11425895; DOI=10.1523/jneurosci.21-13-04678.2001;
RA   Cao G., Pei W., Lan J., Stetler R.A., Luo Y., Nagayama T., Graham S.H.,
RA   Yin X.M., Simon R.P., Chen J.;
RT   "Caspase-activated DNase/DNA fragmentation factor 40 mediates apoptotic DNA
RT   fragmentation in transient cerebral ischemia and in neuronal cultures.";
RL   J. Neurosci. 21:4678-4690(2001).
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       Q99N34; Q63369: Nfkb1; NbExp=2; IntAct=EBI-8498730, EBI-8498561;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR   EMBL; AF136598; AAK16646.1; -; mRNA.
DR   RefSeq; NP_445814.1; NM_053362.1.
DR   AlphaFoldDB; Q99N34; -.
DR   SMR; Q99N34; -.
DR   BioGRID; 249919; 1.
DR   IntAct; Q99N34; 1.
DR   MINT; Q99N34; -.
DR   STRING; 10116.ENSRNOP00000034722; -.
DR   iPTMnet; Q99N34; -.
DR   PhosphoSitePlus; Q99N34; -.
DR   PaxDb; Q99N34; -.
DR   PRIDE; Q99N34; -.
DR   GeneID; 84359; -.
DR   KEGG; rno:84359; -.
DR   UCSC; RGD:620335; rat.
DR   CTD; 1677; -.
DR   RGD; 620335; Dffb.
DR   eggNOG; ENOG502R0RF; Eukaryota.
DR   HOGENOM; CLU_049235_1_1_1; -.
DR   InParanoid; Q99N34; -.
DR   OrthoDB; 1254881at2759; -.
DR   PhylomeDB; Q99N34; -.
DR   TreeFam; TF102022; -.
DR   Reactome; R-RNO-140342; Apoptosis induced DNA fragmentation.
DR   PRO; PR:Q99N34; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q99N34; RN.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0004536; F:deoxyribonuclease activity; IDA:RGD.
DR   GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0004518; F:nuclease activity; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0030263; P:apoptotic chromosome condensation; ISO:RGD.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IDA:RGD.
DR   GO; GO:0007420; P:brain development; IEP:RGD.
DR   GO; GO:0006308; P:DNA catabolic process; ISO:RGD.
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   Apoptosis; Cytoplasm; Hydrolase; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..349
FT                   /note="DNA fragmentation factor subunit beta"
FT                   /id="PRO_0000144715"
FT   DOMAIN          7..83
FT                   /note="CIDE-N"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT   REGION          319..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..349
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  40097 MW;  F125972A110FE398 CRC64;
     MCAVLPQPKC VKLRALHSSC KFGVAARSCQ ELLRKGCIRF QLPVPGSRLC MYEDGTEVTD
     DCFPSLPNDS ELLLLTAGET WHGYVSDITR LLSVFNEPHA GVIQAARQLL SDEQAPLRQK
     LLADLLHHVS QNITAETREQ DPSWFEGLES RFRNKSGYLR YSCESRIRGY LREVSAYISM
     VDAAAREEYL RVLSSMCHKL KSVQYNGSYF DRGAEASSRL CTPEGWFSCQ GPFDLESCLS
     KHSINPYGNR ESRILFSTWN LDHIIEKKRT VVPTLAEAIQ DGREVNWEYF YSLLFTAENL
     KLVHIACHKK TTHKLQCDRS RIYRPQTGSR RKQPPRKQPP RKRPPRKRQ