DEDD_MOUSE
ID DEDD_MOUSE Reviewed; 318 AA.
AC Q9Z1L3; Q7TQH8; Q9R227;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Death effector domain-containing protein;
DE AltName: Full=DEDPro1;
GN Name=Dedd;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9774341; DOI=10.1093/emboj/17.20.5974;
RA Stegh A.H., Schickling O., Ehret A., Scaffidi C., Peterhaensel C.,
RA Hofmann T.G., Grummt I., Krammer P.H., Peter M.E.;
RT "DEDD, a novel death effector domain-containing protein, targeted to the
RT nucleolus.";
RL EMBO J. 17:5974-5986(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Thome M., Tschopp J.;
RT "DEDPRO1, a novel DED-containing protein.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Colon, and Mammary gland;
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: A scaffold protein that directs CASP3 to certain substrates
CC and facilitates their ordered degradation during apoptosis. May also
CC play a role in mediating CASP3 cleavage of KRT18. Regulates degradation
CC of intermediate filaments during apoptosis. May play a role in the
CC general transcription machinery in the nucleus and might be an
CC important regulator of the activity of GTF3C3 (By similarity). Inhibits
CC DNA transcription in vitro. {ECO:0000250, ECO:0000269|PubMed:9774341}.
CC -!- SUBUNIT: Interacts with CASP8, CASP10, KRT8, KRT18, CASP3 and FADD.
CC Homodimerizes and heterodimerizes with DEDD2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Note=Translocated to the nucleus during CD95-mediated
CC apoptosis where it is localized in the nucleoli. Following apoptosis
CC induction, the mono and/or diubiquitination form increases and forms
CC filamentous structures that colocalize with KRT8 and KRT18 intermediate
CC filament network in simple epithelial cells (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9774341}.
CC -!- PTM: Exists predominantly in a mono- or diubiquitinated form.
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DR EMBL; AJ011386; CAA09604.1; -; mRNA.
DR EMBL; AF100342; AAD16415.1; -; mRNA.
DR EMBL; BC023668; AAH23668.1; -; mRNA.
DR EMBL; BC054445; AAH54445.1; -; mRNA.
DR CCDS; CCDS15490.1; -.
DR RefSeq; NP_001122081.1; NM_001128609.1.
DR RefSeq; NP_035745.3; NM_011615.3.
DR RefSeq; XP_006496801.1; XM_006496738.3.
DR RefSeq; XP_006496802.1; XM_006496739.3.
DR RefSeq; XP_006496803.1; XM_006496740.3.
DR RefSeq; XP_006496804.1; XM_006496741.3.
DR RefSeq; XP_011237084.1; XM_011238782.2.
DR AlphaFoldDB; Q9Z1L3; -.
DR BioGRID; 204257; 1.
DR IntAct; Q9Z1L3; 1.
DR STRING; 10090.ENSMUSP00000106931; -.
DR iPTMnet; Q9Z1L3; -.
DR PhosphoSitePlus; Q9Z1L3; -.
DR MaxQB; Q9Z1L3; -.
DR PaxDb; Q9Z1L3; -.
DR PRIDE; Q9Z1L3; -.
DR ProteomicsDB; 279331; -.
DR Antibodypedia; 34292; 236 antibodies from 33 providers.
DR DNASU; 21945; -.
DR Ensembl; ENSMUST00000064950; ENSMUSP00000068419; ENSMUSG00000013973.
DR Ensembl; ENSMUST00000097467; ENSMUSP00000095075; ENSMUSG00000013973.
DR Ensembl; ENSMUST00000111299; ENSMUSP00000106930; ENSMUSG00000013973.
DR Ensembl; ENSMUST00000111300; ENSMUSP00000106931; ENSMUSG00000013973.
DR GeneID; 21945; -.
DR KEGG; mmu:21945; -.
DR UCSC; uc007dnx.2; mouse.
DR CTD; 9191; -.
DR MGI; MGI:1333874; Dedd.
DR VEuPathDB; HostDB:ENSMUSG00000013973; -.
DR eggNOG; ENOG502QRWB; Eukaryota.
DR GeneTree; ENSGT00390000008714; -.
DR HOGENOM; CLU_053869_0_0_1; -.
DR InParanoid; Q9Z1L3; -.
DR OMA; KTXIRLR; -.
DR OrthoDB; 653785at2759; -.
DR PhylomeDB; Q9Z1L3; -.
DR TreeFam; TF331807; -.
DR BioGRID-ORCS; 21945; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Dedd; mouse.
DR PRO; PR:Q9Z1L3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9Z1L3; protein.
DR Bgee; ENSMUSG00000013973; Expressed in primary oocyte and 248 other tissues.
DR ExpressionAtlas; Q9Z1L3; baseline and differential.
DR Genevisible; Q9Z1L3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046697; P:decidualization; IMP:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; IDA:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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; Cytoplasm; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..318
FT /note="Death effector domain-containing protein"
FT /id="PRO_0000191275"
FT DOMAIN 25..103
FT /note="DED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT REGION 128..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 237
FT /note="K -> N (in Ref. 2; AAD16415)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="A -> V (in Ref. 3; AAH54445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36805 MW; C9A31DFC4C0E57CA CRC64;
MAGLKRRASQ VWPEERGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV DVIDDHERGL
IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY VTLKKRRAVC PDLVDKYLEE
TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP VVCCPTSGSQ MCSKRPARGR TTLGSQRKRR
KSVTPDPKEK QTCDIRLRVR AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD
LGSIICDIKF SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED
YELGRQKLLR NLMLQALP
