CRADD_MOUSE
ID CRADD_MOUSE Reviewed; 199 AA.
AC O88843; Q9QUN0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Death domain-containing protein CRADD;
DE AltName: Full=Caspase and RIP adapter with death domain;
DE AltName: Full=RIP-associated protein with a death domain;
GN Name=Cradd; Synonyms=Raidd;
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].
RA Pan G.;
RT "A mouse cell death adaptor molecule that contains a death domain and a
RT CARD domain.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9806843; DOI=10.1006/geno.1998.5540;
RA Horvat S., Medrano J.F.;
RT "A 500-kb YAC and BAC contig encompassing the high-growth deletion in mouse
RT chromosome 10 and identification of the murine Raidd/Cradd gene in the
RT candidate region.";
RL Genomics 54:159-164(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and 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).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH PIDD, AND MUTAGENESIS OF GLY-128.
RX PubMed=22279524; DOI=10.1371/journal.pone.0028936;
RA Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A.,
RA Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J.,
RA Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N.,
RA Setton R.A., Dipiazza R., Sherman E.A., Eastman J.T., Francklyn C.,
RA Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.;
RT "Genetic mapping and exome sequencing identify variants associated with
RT five novel diseases.";
RL PLoS ONE 7:E28936-E28936(2012).
CC -!- FUNCTION: Adapter protein that associates with PIDD1 and the caspase
CC CASP2 to form the PIDDosome, a complex that activates CASP2 and
CC triggers apoptosis. Also recruits CASP2 to the TNFR-1 signaling complex
CC through its interaction with RIPK1 and TRADD and may play a role in the
CC tumor necrosis factor-mediated signaling pathway.
CC {ECO:0000250|UniProtKB:P78560}.
CC -!- SUBUNIT: Forms a complex named the PIDDosome with PIDD1 and CASP2
CC (PubMed:22279524). Interacts (via Death domain) with RIPK1 (via Death
CC domain); the interaction is direct. Interacts with TRADD. Interacts
CC with TNFRSF1A (By similarity). {ECO:0000250|UniProtKB:P78560,
CC ECO:0000269|PubMed:22279524}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22279524}. Nucleus
CC {ECO:0000269|PubMed:22279524}.
CC -!- DOMAIN: The Death domain mediates the interaction with PIDD1 and the
CC formation of a complex composed of 5 PIDD1 and 7 CRADD proteins which
CC in turn probably recruit 7 CASP2 to form the PIDDosome. The Death
CC domain mediates a direct interaction with the Death domain of RIPK1.
CC {ECO:0000250|UniProtKB:P78560}.
CC -!- DOMAIN: The CARD domain mediates a direct interaction with CASP2.
CC {ECO:0000250|UniProtKB:P78560}.
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DR EMBL; AF017992; AAC35882.1; -; mRNA.
DR EMBL; AJ224738; CAA12107.1; -; mRNA.
DR EMBL; AJ224740; CAA12109.1; -; mRNA.
DR EMBL; BC005608; AAH05608.1; -; mRNA.
DR CCDS; CCDS24135.1; -.
DR RefSeq; NP_001317067.1; NM_001330138.1.
DR RefSeq; NP_001317070.1; NM_001330141.1.
DR RefSeq; NP_001317104.1; NM_001330175.1.
DR RefSeq; NP_034080.1; NM_009950.3.
DR RefSeq; XP_006513243.1; XM_006513180.2.
DR RefSeq; XP_006513244.1; XM_006513181.3.
DR AlphaFoldDB; O88843; -.
DR SMR; O88843; -.
DR BioGRID; 198870; 3.
DR ComplexPortal; CPX-3963; Caspase-2 PIDDosome.
DR STRING; 10090.ENSMUSP00000050295; -.
DR PhosphoSitePlus; O88843; -.
DR EPD; O88843; -.
DR PaxDb; O88843; -.
DR PeptideAtlas; O88843; -.
DR PRIDE; O88843; -.
DR ProteomicsDB; 283953; -.
DR Antibodypedia; 3943; 544 antibodies from 38 providers.
DR DNASU; 12905; -.
DR Ensembl; ENSMUST00000053594; ENSMUSP00000050295; ENSMUSG00000045867.
DR Ensembl; ENSMUST00000217809; ENSMUSP00000151735; ENSMUSG00000045867.
DR Ensembl; ENSMUST00000220279; ENSMUSP00000152022; ENSMUSG00000045867.
DR GeneID; 12905; -.
DR KEGG; mmu:12905; -.
DR UCSC; uc007gwa.1; mouse.
DR CTD; 8738; -.
DR MGI; MGI:1336168; Cradd.
DR VEuPathDB; HostDB:ENSMUSG00000045867; -.
DR eggNOG; ENOG502R26C; Eukaryota.
DR GeneTree; ENSGT00390000014448; -.
DR HOGENOM; CLU_118159_0_0_1; -.
DR InParanoid; O88843; -.
DR OMA; RCRSDHS; -.
DR OrthoDB; 1346117at2759; -.
DR PhylomeDB; O88843; -.
DR TreeFam; TF333055; -.
DR Reactome; R-MMU-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
DR BioGRID-ORCS; 12905; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Cradd; mouse.
DR PRO; PR:O88843; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O88843; protein.
DR Bgee; ENSMUSG00000045867; Expressed in granulocyte and 169 other tissues.
DR ExpressionAtlas; O88843; baseline and differential.
DR Genevisible; O88843; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1905369; C:endopeptidase complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070513; F:death domain binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR CDD; cd08327; CARD_RAIDD; 1.
DR CDD; cd08319; Death_RAIDD; 1.
DR Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR042148; CARD_RAIDD.
DR InterPro; IPR037939; CRADD.
DR InterPro; IPR037926; CRADD_Death.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR PANTHER; PTHR15034; PTHR15034; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF00531; Death; 1.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00005; DEATH; 1.
DR SUPFAM; SSF47986; SSF47986; 2.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..199
FT /note="Death domain-containing protein CRADD"
FT /id="PRO_0000079327"
FT DOMAIN 1..92
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 116..188
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT MUTAGEN 128
FT /note="G->R: Impairs the interaction with PIDD."
FT /evidence="ECO:0000269|PubMed:22279524"
FT CONFLICT 185
FT /note="Q -> H (in Ref. 1; AAC35882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22656 MW; 6C2F987B1ED47229 CRC64;
MEARDKQVLR SLRLELGAEV LVEGLVLQYL YQEGILTENH IQEIKAQTTG LRKTMLLLDI
LPSRGPKAFD TFLDSLQEFP WVREKLEKAR EEVTAELPTG DWMAGIPSHI LSSSPSDQQI
NQLAQRLGPE WEPVVLSLGL SQTDIYRCKA NHPHNVHSQV VEAFVRWRQR FGKQATFLSL
HKGLQAVEAD PSLLQHMLE
