DEDD_RAT
ID DEDD_RAT Reviewed; 318 AA.
AC Q9Z2K0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Death effector domain-containing protein;
DE AltName: Full=Death effector domain-containing testicular molecule;
GN Name=Dedd; Synonyms=Deft;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=9832420; DOI=10.1210/endo.139.12.6335;
RA Leo C.P., Hsu S.Y., McGee E.A., Salanova M., Hsueh A.J.W.;
RT "DEFT, a novel death effector domain-containing molecule predominantly
RT expressed in testicular germ cells.";
RL Endocrinology 139:4839-4848(1998).
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. Inhibits DNA
CC transcription in vitro (By similarity). {ECO:0000250}.
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: Widely expressed with highest levels in testis.
CC Within the testis, highly expressed in germ cells but not expressed in
CC Sertoli cells. {ECO:0000269|PubMed:9832420}.
CC -!- DEVELOPMENTAL STAGE: First detected in 20-day-old animals. Reaches a
CC peak at 30 days. {ECO:0000269|PubMed:9832420}.
CC -!- PTM: Exists predominantly in a mono- or diubiquitinated form.
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DR EMBL; AF053362; AAC80287.1; -; mRNA.
DR RefSeq; NP_113988.1; NM_031800.1.
DR RefSeq; XP_006250331.1; XM_006250269.3.
DR RefSeq; XP_006250334.1; XM_006250272.3.
DR RefSeq; XP_006250336.1; XM_006250274.3.
DR RefSeq; XP_017454431.1; XM_017598942.1.
DR RefSeq; XP_017454432.1; XM_017598943.1.
DR RefSeq; XP_017454433.1; XM_017598944.1.
DR RefSeq; XP_017454434.1; XM_017598945.1.
DR RefSeq; XP_017454435.1; XM_017598946.1.
DR AlphaFoldDB; Q9Z2K0; -.
DR SMR; Q9Z2K0; -.
DR STRING; 10116.ENSRNOP00000005147; -.
DR PaxDb; Q9Z2K0; -.
DR PRIDE; Q9Z2K0; -.
DR Ensembl; ENSRNOT00000005147; ENSRNOP00000005147; ENSRNOG00000003779.
DR GeneID; 83631; -.
DR KEGG; rno:83631; -.
DR UCSC; RGD:620050; rat.
DR CTD; 9191; -.
DR RGD; 620050; Dedd.
DR eggNOG; ENOG502QRWB; Eukaryota.
DR GeneTree; ENSGT00390000008714; -.
DR HOGENOM; CLU_053869_0_0_1; -.
DR InParanoid; Q9Z2K0; -.
DR OMA; KTXIRLR; -.
DR OrthoDB; 653785at2759; -.
DR PhylomeDB; Q9Z2K0; -.
DR TreeFam; TF331807; -.
DR PRO; PR:Q9Z2K0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003779; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q9Z2K0; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; NAS:RGD.
DR GO; GO:0046697; P:decidualization; ISO:RGD.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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_0000191276"
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"
SQ SEQUENCE 318 AA; 36847 MW; B8751791F66A03DE CRC64;
MAGLKRRASQ VWPEERVEQE 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
