P59823 · IRPL1_MOUSE
- ProteinInterleukin-1 receptor accessory protein-like 1
- GeneIl1rapl1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids695 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK (By similarity).
Plays a role in neurite outgrowth (By similarity).
During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans-synaptically binding to PTPRD (PubMed:21940441, PubMed:25908590).
Plays a role in neurite outgrowth (By similarity).
During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans-synaptically binding to PTPRD (PubMed:21940441, PubMed:25908590).
Catalytic activity
- H2O + NAD+ = ADP-D-ribose + H+ + nicotinamideThis reaction proceeds in the forward direction.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 34 | Essential for interaction with PTPRD | ||||
Sequence: W | ||||||
Active site | 490 | |||||
Sequence: E |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | dendrite | |
Cellular Component | glutamatergic synapse | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic density membrane | |
Cellular Component | postsynaptic membrane | |
Molecular Function | NAD+ nucleosidase activity | |
Molecular Function | NAD+ nucleotidase, cyclic ADP-ribose generating | |
Molecular Function | signaling receptor binding | |
Biological Process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | negative regulation of exocytosis | |
Biological Process | neuron differentiation | |
Biological Process | positive regulation of dendrite morphogenesis | |
Biological Process | positive regulation of dendritic spine morphogenesis | |
Biological Process | positive regulation of synapse assembly | |
Biological Process | presynaptic membrane assembly | |
Biological Process | regulation of neuron projection development | |
Biological Process | signal transduction | |
Biological Process | synaptic membrane adhesion |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterleukin-1 receptor accessory protein-like 1
- EC number
- Short namesIL-1-RAPL-1; IL-1RAPL-1; IL1RAPL-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP59823
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: May localize to the cell body and growth cones of dendrite-like processes.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 25-357 | Extracellular | ||||
Sequence: RGSADGCTDWSVDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLTVGENDTGLCYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKAWRPSIVFKRDTLLIKEVKEDDIGNYTCELKYGGFVVRRTTELTVTAPLTDKPPKLLYPMESKLTVQETQLGGSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSCYVENGNGRRHASVLLHKRELMYT | ||||||
Transmembrane | 358-378 | Helical | ||||
Sequence: VELAGGLGAILLLLICSVTIY | ||||||
Topological domain | 379-695 | Cytoplasmic | ||||
Sequence: KCYKIEIMLFYRNHFGAEELDGDNKDYDAYLSYTKVDPDQWNQETGEEERFALEILPDMLEKHYGYKLFIPDRDLIPTGNIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVTGEIKVILIECSELRGIMNYQEVEALKHTIKLLTVIKWHGPKCNKLNSKFWKRLQYEMPFKRIEPITHEQALDVSEQGPFGELQTVSAISMAAATSTALATAHPDLRSTFHNTYHSQMRQKHYYRSYEYDVPPTGTLPLTSIGNQHTYCNIPMTLINGQRPQTKSNREPNPDEAHTNSAILPLLPRETSISSVIW |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Abolishes Interaction with PTPRD. Abolishes synaptogenesis. | ||||
Sequence: W → A | ||||||
Mutagenesis | 37 | Decreases affinity for PTPRD. Significantly decreases synaptogenesis. | ||||
Sequence: D → A | ||||||
Mutagenesis | 75-77 | Decreases affinity for PTPRD; when associated with 88-A--A-91. Significantly decreases synaptogenesis; when associated with 88-A--A-91. | ||||
Sequence: MWY → AWA | ||||||
Mutagenesis | 88-91 | Decreases affinity for PTPRD; when associated with 75-A--A-77. Significantly decreases synaptogenesis; when associated with 88-A--A-91. | ||||
Sequence: PIAF → AIAA | ||||||
Mutagenesis | 292 | Decreases affinity for PTPRD. Significantly decreases synaptogenesis. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MKAPIPHLILLYATFTQSLKVVTK | ||||||
Chain | PRO_0000015455 | 25-695 | Interleukin-1 receptor accessory protein-like 1 | |||
Sequence: RGSADGCTDWSVDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLTVGENDTGLCYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKAWRPSIVFKRDTLLIKEVKEDDIGNYTCELKYGGFVVRRTTELTVTAPLTDKPPKLLYPMESKLTVQETQLGGSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSCYVENGNGRRHASVLLHKRELMYTVELAGGLGAILLLLICSVTIYKCYKIEIMLFYRNHFGAEELDGDNKDYDAYLSYTKVDPDQWNQETGEEERFALEILPDMLEKHYGYKLFIPDRDLIPTGNIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVTGEIKVILIECSELRGIMNYQEVEALKHTIKLLTVIKWHGPKCNKLNSKFWKRLQYEMPFKRIEPITHEQALDVSEQGPFGELQTVSAISMAAATSTALATAHPDLRSTFHNTYHSQMRQKHYYRSYEYDVPPTGTLPLTSIGNQHTYCNIPMTLINGQRPQTKSNREPNPDEAHTNSAILPLLPRETSISSVIW | ||||||
Disulfide bond | 31↔126 | |||||
Sequence: CTDWSVDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYC | ||||||
Disulfide bond | 53↔118 | |||||
Sequence: CALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYAC | ||||||
Glycosylation | 63 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 122 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 143↔185 | |||||
Sequence: CYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKEC | ||||||
Disulfide bond | 164↔216 | |||||
Sequence: CRDIEDFLLPTREPEILWYKECRTKAWRPSIVFKRDTLLIKEVKEDDIGNYTC | ||||||
Glycosylation | 213 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 264 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 267↔334 | |||||
Sequence: CRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSC | ||||||
Glycosylation | 331 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in total brain extracts, olfactory bulb, hippocampus and striatum (at protein level).
Interaction
Subunit
Homodimer (PubMed:25908590).
Interacts (calcium-independent) with NCS1/FREQ (By similarity).
Interacts (via the first immunoglobilin domain) with PTPRD (via the second immunoglobilin domain); this interaction is PTPRD-splicing-dependent and induces pre- and post-synaptic differentiation of neurons and is required for IL1RAPL1-mediated synapse formation (PubMed:21940441, PubMed:25908590).
Interacts (calcium-independent) with NCS1/FREQ (By similarity).
Interacts (via the first immunoglobilin domain) with PTPRD (via the second immunoglobilin domain); this interaction is PTPRD-splicing-dependent and induces pre- and post-synaptic differentiation of neurons and is required for IL1RAPL1-mediated synapse formation (PubMed:21940441, PubMed:25908590).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P59823 | Ptprd Q64487 | 6 | EBI-5452114, EBI-771834 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-134 | Ig-like C2-type 1 | ||||
Sequence: RGSADGCTDWSVDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLT | ||||||
Domain | 143-232 | Ig-like C2-type 2 | ||||
Sequence: CYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKAWRPSIVFKRDTLLIKEVKEDDIGNYTCELKYGGFVVRRTTELT | ||||||
Domain | 242-350 | Ig-like C2-type 3 | ||||
Sequence: PKLLYPMESKLTVQETQLGGSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSCYVENGNGRRHASVLLH | ||||||
Domain | 403-558 | TIR | ||||
Sequence: KDYDAYLSYTKVDPDQWNQETGEEERFALEILPDMLEKHYGYKLFIPDRDLIPTGNIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVTGEIKVILIECSELRGIMNYQEVEALKHTIKLLTVIKWHGPKCNKLNSKFWKRLQYEM | ||||||
Region | 548-643 | Interaction with NCS1 | ||||
Sequence: SKFWKRLQYEMPFKRIEPITHEQALDVSEQGPFGELQTVSAISMAAATSTALATAHPDLRSTFHNTYHSQMRQKHYYRSYEYDVPPTGTLPLTSIG | ||||||
Region | 657-679 | Disordered | ||||
Sequence: NGQRPQTKSNREPNPDEAHTNSA |
Domain
The TIR domain mediates NAD+ hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Sequence similarities
Belongs to the interleukin-1 receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length695
- Mass (Da)79,630
- Last updated2003-08-22 v1
- Checksum5FE34F204E5908B7
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Keywords
- Technical term