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IPR000488

Description

IPR000488 is a Death domain.

<p>The death domain (DD) is a homotypic protein interaction module composed of a bundle of six α-helices. DD is related in sequence and structure to the death effector domain (DED, see [interpro:IPR001875]) and the caspase recruitment domain (CARD, see [interpro:IPR001315]), which work in similar pathways and show similar interaction properties [[cite:PUB00015013]]. DD bind each other forming oligomers. Mammals have numerous and diverse DD-containing proteins [[cite:PUB00005444]]. Within these proteins, the DD domains can be found in combination with other domains, including: CARDs, DEDs, ankyrin repeats ([interpro:IPR002110]), caspase-like folds, kinase domains, leucine zippers, leucine-rich repeats (LRR) ([interpro:IPR001611]), TIR domains ([interpro:IPR000157]), and ZU5 domains ([interpro:IPR000906]) [[cite:PUB00015057]].</p> <p>Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB, which typically involves interactions with TNF (tumour necrosis factor) cytokine receptors [[cite:PUB00015011], [cite:PUB00015012]]. In humans, eight of the over 30 known TNF receptors contain DD in their cytoplasmic tails; several of these TNF receptors use caspase activation as a signalling mechanism. The DD mediates self-association of these receptors, thus giving the signal to downstream events that lead to apoptosis. Other DD-containing proteins, such as ankyrin, MyD88 and pelle, are probably not directly involved in cell death signalling. DD-containing proteins also have links to innate immunity, communicating with Toll family receptors through bipartite adapter proteins such as MyD88 [[cite:PUB00015014]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function Protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Biological process Signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

Associated Lotus transcripts 2

Transcript Name Description Predicted domains Domain count
Retrovirus-related Pol polyprotein from transposon TNT 1-94; TAIR: AT4G05360.1 Zinc knuckle (CCHC-type) family protein; Swiss-Prot: sp|P04146|COPIA_DROME Copia protein; TrEMBL-Plants: tr|Q84VH6|Q84VH6_SOYBN Gag-pol polyprotein; Found in the gene: LotjaGi5g1v0100800_LC 17
Gag-pol polyprotein; TAIR: AT3G45850.1 P-loop containing nucleoside triphosphate hydrolases superfamily protein; Swiss-Prot: sp|Q9ULM0|PKHH1_HUMAN Pleckstrin homology domain-containing family H member 1; TrEMBL-Plants: tr|A0A072V619|A0A072V619_MEDTR Uncharacterized protein; Found in the gene: LotjaGi5g1v0125600_LC 4

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
mobidb-lite MobiDBLite 1 50.00