DEDD2_MOUSE
ID DEDD2_MOUSE Reviewed; 330 AA.
AC Q8QZV0; Q569Y9; Q8JZV1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA-binding death effector domain-containing protein 2;
DE AltName: Full=DED-containing protein FLAME-3;
DE AltName: Full=FADD-like anti-apoptotic molecule 3;
GN Name=Dedd2; Synonyms=Flame3;
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].
RC STRAIN=C57BL/6J;
RX PubMed=11965497; DOI=10.1038/sj/cdd/4401038;
RA Zhan Y., Hegde R., Srinivasula S.M., Fernandes-Alnemri T., Alnemri E.S.;
RT "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear
RT complexes with the TFIIIC102 subunit of human transcription factor IIIC.";
RL Cell Death Differ. 9:439-447(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12527898; DOI=10.1038/sj.onc.1206099;
RA Alcivar A., Hu S., Tang J., Yang X.;
RT "DEDD and DEDD2 associate with caspase-8/10 and signal cell death.";
RL Oncogene 22:291-297(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a critical role in death receptor-induced apoptosis
CC and may target CASP8 and CASP10 to the nucleus. May regulate
CC degradation of intermediate filaments during apoptosis. May play a role
CC in the general transcription machinery in the nucleus and might be an
CC important regulator of the activity of GTF3C3.
CC -!- SUBUNIT: Interacts with CASP8, CASP10 and GTF3C3. Homodimerizes and
CC heterodimerizes with DEDD (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Nuclear,
CC accumulated in subnuclear structures resembling nucleoli.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression is high in liver, heart, kidney, and
CC testis but low in brain, spleen, lung, and skeleton muscle.
CC -!- DOMAIN: Interactions with CASP8 and CASP10 are mediated by the DED
CC domain. {ECO:0000250}.
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DR EMBL; AF457576; AAM10836.1; -; mRNA.
DR EMBL; AF543541; AAN33179.1; -; mRNA.
DR EMBL; BC092250; AAH92250.1; -; mRNA.
DR CCDS; CCDS20973.1; -.
DR RefSeq; NP_997560.3; NM_207677.3.
DR RefSeq; XP_006540385.1; XM_006540322.1.
DR AlphaFoldDB; Q8QZV0; -.
DR SMR; Q8QZV0; -.
DR STRING; 10090.ENSMUSP00000049763; -.
DR iPTMnet; Q8QZV0; -.
DR PhosphoSitePlus; Q8QZV0; -.
DR PaxDb; Q8QZV0; -.
DR PRIDE; Q8QZV0; -.
DR ProteomicsDB; 279187; -.
DR Antibodypedia; 17411; 210 antibodies from 30 providers.
DR Ensembl; ENSMUST00000058702; ENSMUSP00000049763; ENSMUSG00000054499.
DR Ensembl; ENSMUST00000205271; ENSMUSP00000146052; ENSMUSG00000054499.
DR GeneID; 67379; -.
DR KEGG; mmu:67379; -.
DR UCSC; uc009fru.1; mouse.
DR CTD; 162989; -.
DR MGI; MGI:1914629; Dedd2.
DR VEuPathDB; HostDB:ENSMUSG00000054499; -.
DR eggNOG; ENOG502QQKR; Eukaryota.
DR GeneTree; ENSGT00390000008714; -.
DR HOGENOM; CLU_053869_0_0_1; -.
DR InParanoid; Q8QZV0; -.
DR OMA; WSDYMNG; -.
DR OrthoDB; 653785at2759; -.
DR PhylomeDB; Q8QZV0; -.
DR TreeFam; TF331807; -.
DR BioGRID-ORCS; 67379; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dedd2; mouse.
DR PRO; PR:Q8QZV0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8QZV0; protein.
DR Bgee; ENSMUSG00000054499; Expressed in granulocyte and 156 other tissues.
DR Genevisible; Q8QZV0; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISA:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0030262; P:apoptotic nuclear changes; ISO:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR038856; DEDD/DEDD2.
DR PANTHER; PTHR15205; PTHR15205; 1.
DR Pfam; PF01335; DED; 1.
DR SMART; SM00031; DED; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50168; DED; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..330
FT /note="DNA-binding death effector domain-containing protein
FT 2"
FT /id="PRO_0000191278"
FT DOMAIN 25..104
FT /note="DED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT REGION 104..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..109
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 156..174
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 137..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 36786 MW; 889BC4F9E01304B0 CRC64;
MALSGSTPAP SWEEDECLDY YGMLSLHRMF EVVGGQLTEC ELELLAFLLD EAPGAPGGLA
RARSGLELLL ELERRGQCDE SNLRLLSQLL RVLARHDLLP HLARKRRRPV SPERYSYGNP
SSSSKRTEDS CRRRRQASSS SDSPQSQWDT GSPPTKRQRR SRGRPSSGAR QRRRAGLAAS
QQHQQHQELG RPSSEGKVTC DIRLRVRAEY CEHGPALEQG VASRRPQALA RQLDVFGQAT
AVLRSRDLGS VVCDIKFSEL SYLDAFWGDY LSGALLQALR GVFLTEALRE AVGREAVRLL
VSVDEADYEA GRRRLLLMEE EGGRRGTEAS
