Q9HB29 · ILRL2_HUMAN
- ProteinInterleukin-1 receptor-like 2
- GeneIL1RL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids575 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for interleukin-36 (IL36A, IL36B and IL36G). After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways (By similarity).
The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL-23/IL-17/IL-22 pathway
The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL-23/IL-17/IL-22 pathway
Catalytic activity
- H2O + NAD+ = ADP-D-ribose + H+ + nicotinamideThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 467 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | interleukin-1 receptor activity | |
Molecular Function | interleukin-1, type I, activating receptor activity | |
Molecular Function | NAD+ nucleosidase activity | |
Molecular Function | NAD+ nucleotidase, cyclic ADP-ribose generating | |
Biological Process | cellular defense response | |
Biological Process | inflammatory response | |
Biological Process | innate immune response | |
Biological Process | positive regulation of interleukin-6 production | |
Biological Process | positive regulation of T cell differentiation | |
Biological Process | regulation of inflammatory response | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterleukin-1 receptor-like 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9HB29
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-335 | Extracellular | ||||
Sequence: DGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTVFEKHWCDTSIGGLPNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNGITVSITERAGYGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHAGVSTAYIILQLPAPDFR | ||||||
Transmembrane | 336-356 | Helical | ||||
Sequence: AYLIGGLIALVAVAVSVVYIY | ||||||
Topological domain | 357-575 | Cytoplasmic | ||||
Sequence: NIFKIDIVLWYRSAFHSTETIVDGKLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHMPPRRCRPFPPVQLLQHTPCYRTAGPELGSRRKKCTLTTG |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053378 | 237 | in dbSNP:rs13405631 | |||
Sequence: I → T | ||||||
Natural variant | VAR_025259 | 352 | in dbSNP:rs33946385 | |||
Sequence: V → I | ||||||
Natural variant | VAR_025260 | 550 | in dbSNP:rs2302612 | |||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 706 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MWSLLLCGLSIALPLSVTA | ||||||
Chain | PRO_0000015445 | 20-575 | Interleukin-1 receptor-like 2 | |||
Sequence: DGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTVFEKHWCDTSIGGLPNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNGITVSITERAGYGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHAGVSTAYIILQLPAPDFRAYLIGGLIALVAVAVSVVYIYNIFKIDIVLWYRSAFHSTETIVDGKLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHMPPRRCRPFPPVQLLQHTPCYRTAGPELGSRRKKCTLTTG | ||||||
Glycosylation | 41 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 42↔95 | |||||
Sequence: CTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQC | ||||||
Glycosylation | 59 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 127 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 146↔195 | |||||
Sequence: CHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYAC | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 234 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 249↔316 | |||||
Sequence: CNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMC | ||||||
Glycosylation | 250 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 266 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 299 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in synovial fibroblasts and articular chondrocytes. Expressed in keratinocytes and monocyte-derived dendritic cells. Expressed in monocytes and myeloid dendritic cells; at protein level.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-111 | Ig-like C2-type 1 | ||||
Sequence: DGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLT | ||||||
Domain | 126-211 | Ig-like C2-type 2 | ||||
Sequence: PNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNG | ||||||
Domain | 222-318 | Ig-like C2-type 3 | ||||
Sequence: YGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHA | ||||||
Domain | 381-536 | TIR | ||||
Sequence: KLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHM |
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 & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9HB29-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length575
- Mass (Da)65,405
- Last updated2006-02-07 v2
- Checksum7AC0FCAB43A2A6CD
Q9HB29-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9K0I8 | C9K0I8_HUMAN | IL1RL2 | 172 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056292 | 1-46 | in isoform 2 | |||
Sequence: MWSLLLCGLSIALPLSVTADGCKDIFMKNEILSASQPFAFNCTFPP → MTGLVSLSYFPLSTRSCALQSCSPVWGCGPCCSAGCPSPFHCLSQQ | ||||||
Alternative sequence | VSP_056293 | 47-163 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_056294 | 217-218 | in isoform 2 | |||
Sequence: TE → K | ||||||
Sequence conflict | 486 | in Ref. 1; AAG21368 | ||||
Sequence: I → V | ||||||
Sequence conflict | 545-556 | in Ref. 2 | ||||
Sequence: PPVQLLQHTPCY → LRSTCRSTHLCTA | ||||||
Sequence conflict | 556 | in Ref. 1; AAG21368 | ||||
Sequence: Y → C |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF284434 EMBL· GenBank· DDBJ | AAG21368.1 EMBL· GenBank· DDBJ | mRNA | ||
U49065 EMBL· GenBank· DDBJ | AAB53237.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
DQ131903 EMBL· GenBank· DDBJ | AAZ38712.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC007271 EMBL· GenBank· DDBJ | AAX81989.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC007248 EMBL· GenBank· DDBJ | AAY15046.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC107064 EMBL· GenBank· DDBJ | AAI07065.1 EMBL· GenBank· DDBJ | mRNA |