LRDD

Protein-coding gene in the species Homo sapiens
PIDD1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2OF5

Identifiers
AliasesPIDD1, LRDD, PIDD, p53-induced death domain protein 1
External IDsOMIM: 605247; MGI: 1889507; HomoloGene: 11220; GeneCards: PIDD1; OMA:PIDD1 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for PIDD1
Genomic location for PIDD1
Band11p15.5Start799,179 bp[1]
End809,753 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for PIDD1
Genomic location for PIDD1
Band7|7 F5Start141,018,026 bp[2]
End141,023,938 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • apex of heart

  • right hemisphere of cerebellum

  • right uterine tube

  • granulocyte

  • mucosa of transverse colon

  • C1 segment

  • right lobe of thyroid gland

  • anterior pituitary

  • left lobe of thyroid gland

  • skin of leg
Top expressed in
  • epithelium of nasopharynx

  • genital tubercle

  • fetal liver hematopoietic progenitor cell

  • tail of embryo

  • epiblast

  • ventricular zone

  • embryo

  • blastocyst

  • embryo

  • thymus
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • death receptor binding
  • protein binding
  • volume-sensitive anion channel activity
  • endopeptidase activity
  • hydrolase activity
Cellular component
  • Golgi apparatus
  • nucleus
  • nucleoplasm
  • cytoplasm
  • cytosol
  • ion channel complex
Biological process
  • positive regulation of extrinsic apoptotic signaling pathway via death domain receptors
  • apoptotic process
  • positive regulation of extrinsic apoptotic signaling pathway
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
  • negative regulation of apoptotic process
  • positive regulation of apoptotic signaling pathway
  • activation of cysteine-type endopeptidase activity involved in apoptotic process
  • positive regulation of NF-kappaB transcription factor activity
  • signal transduction
  • cellular response to DNA damage stimulus
  • positive regulation of apoptotic process
  • regulation of apoptotic process
  • inorganic anion transport
  • anion transmembrane transport
  • protein autoprocessing
  • regulation of I-kappaB kinase/NF-kappaB signaling
  • extrinsic apoptotic signaling pathway via death domain receptors
  • apoptotic signaling pathway
  • extrinsic apoptotic signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

55367

57913

Ensembl

ENSG00000177595

ENSMUSG00000025507

UniProt

Q9HB75

Q9ERV7

RefSeq (mRNA)

NM_018494
NM_145886
NM_145887

NM_022654
NM_001360523
NM_001360524

RefSeq (protein)

NP_665893
NP_665894

NP_073145
NP_001347452
NP_001347453

Location (UCSC)Chr 11: 0.8 – 0.81 MbChr 7: 141.02 – 141.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Leucine-rich repeats and death domain containing, also known as LRDD or p53-induced protein with a death domain (PIDD), is a protein which in humans is encoded by the LRDD gene.[5]

Function

The protein encoded by this gene contains a leucine-rich repeat and a death domain. This protein has been shown to interact with other death domain proteins, such as Fas (TNFRSF6)-associated via death domain (FADD) and MAP-kinase activating death domain-containing protein (MADD), and thus may function as an adaptor protein in cell death-related signaling processes. The expression of the mouse counterpart of this gene has been found to be positively regulated by the tumor suppressor p53 and to induce cell apoptosis in response to DNA damage, which suggests a role for this gene as an effector of p53-dependent apoptosis. Three alternatively spliced transcript variants encoding distinct isoforms have been reported.[5] Besides its pro-apoptotic function it may also be involved in DNA repair as part of a protein complex formed together with the catalytic subunit of DNA-PK (DNA-PKcs)and caspase 2.

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000177595 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025507 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: LRDD leucine-rich repeats and death domain containing".

Further reading

  • Telliez JB, Bean KM, Lin LL (2000). "LRDD, a novel leucine rich repeat and death domain containing protein". Biochim. Biophys. Acta. 1478 (2): 280–8. doi:10.1016/S0167-4838(00)00029-7. PMID 10825539.
  • Lin Y, Ma W, Benchimol S (2000). "Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis". Nat. Genet. 26 (1): 122–7. doi:10.1038/79102. PMID 10973264. S2CID 10601123.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Tinel A, Tschopp J (2004). "The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress". Science. 304 (5672): 843–6. Bibcode:2004Sci...304..843T. doi:10.1126/science.1095432. PMID 15073321. S2CID 6583298.
  • Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Janssens S, Tinel A, Lippens S, Tschopp J (2006). "PIDD mediates NF-kappaB activation in response to DNA damage". Cell. 123 (6): 1079–92. doi:10.1016/j.cell.2005.09.036. PMID 16360037. S2CID 15953086.
  • Vakifahmetoglu H, Olsson M, Orrenius S, Zhivotovsky B (2006). "Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage". Oncogene. 25 (41): 5683–92. doi:10.1038/sj.onc.1209569. PMID 16652156.
  • Pick R, Badura S, Bösser S, Zörnig M (2006). "Upon intracellular processing, the C-terminal death domain-containing fragment of the p53-inducible PIDD/LRDD protein translocates to the nucleoli and interacts with nucleolin". Biochem. Biophys. Res. Commun. 349 (4): 1329–38. doi:10.1016/j.bbrc.2006.08.176. PMID 16982033.
  • Tinel A, Janssens S, Lippens S, et al. (2007). "Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-κB pathway". EMBO J. 26 (1): 197–208. doi:10.1038/sj.emboj.7601473. PMC 1782377. PMID 17159900.
  • Park HH, Wu H (2007). "Crystallization and preliminary X-ray crystallographic studies of the oligomeric death-domain complex between PIDD and RAIDD". Acta Crystallographica Section F. 63 (Pt 3): 229–32. doi:10.1107/S1744309107007889. PMC 2330181. PMID 17329820.
  • Bradley G, Tremblay S, Irish J, et al. (2007). "The expression of p53-induced protein with death domain (Pidd) and apoptosis in oral squamous cell carcinoma". Br. J. Cancer. 96 (9): 1425–32. doi:10.1038/sj.bjc.6603745. PMC 2360189. PMID 17437012.
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  • 2of5: Oligomeric Death Domain complex
    2of5: Oligomeric Death Domain complex


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