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0IL1AP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameIL1RAP
DescriptionInterleukin-1 receptor accessory protein precursor (il-1 receptor accessory protein) (il-1racp).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005515 protein binding (IPI)
0004871 signal transducer activity (TAS)
0006954 inflammatory response (TAS)
0006461 protein complex assembly (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
In Drosophila melanogaster the Toll protein is involved in establishment of dorso-ventralpolarity in the embryo. In addition.embers of the Toll family play a keyrole in innate antibacterial and antifungal immunity in insects as well as inmammals. These proteins are type-I transmembrane receptors that share anintracellular 200 residue domain with the interleukin-1 receptor (IL-1R).heToll/IL-1R homologous region (TIR). The similarity between Toll-like receptors(LTRs) and IL-1R is not restricted to sequence homology since these proteinsalso share a similar signaling pathway. They both induce the activation of aRel type transcription factor via an adaptor protein and a protein kinase .Interestingly.yD88. cytoplasmic adaptor protein found in mammals.ontainsa TIR domain associated to a DEATH domain (see ) . Besides the mammalian and Drosophila melanogaster proteins. TIR domain is also found in a number of plant proteins implicated in host defense . As MyD88.hese proteins are cytoplasmic.Site directed mutagenesis and deletion analysis have shown that the TIR domain is essential for Toll and IL-1R activities. Sequence analysis have revealedthe presence of three highly conserved regions among the different members ofthe family: box 1 (FDAFISY).ox 2 (GYKLC-RD-PG).nd box 3 (a conserved Wsurrounded by basic residues). It has been proposed that boxes 1 and 2 areinvolved in the binding of proteins involved in signaling.hereas box 3 isprimarily involved in directing localization of receptor.erhaps throughinteractions with cytoskeletal elements .
  IPR000157:Toll-Interleukin receptor
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This subfamily includes:Cell surface receptors containing an immunoglobin domain.Killer cell inhibitory receptors.Oprin a snake venom metalloproteinase inhibitor from Didelphis marsupialis (Southern opossum) .hich belongs to MEROPS inhibitor family I43.lan I- .Oprin homologues.
  IPR003599:Immunoglobulin subtype
Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses.nflammatory reactions.nd hematopoiesis . Two types of IL-1 receptor.ach with three extracellular immunoglobulin (Ig)-like domains.imited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors . The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution.nd map to thesame chromosomal location . The receptors can both bind all three forms of IL-1 (IL-1 alpha.L-1 beta and IL-1RA).The vaccinia virus genes B15R and B18R each encode proteins with N-terminal hydrophobic sequences.ossible sites for attachment of N-linked carbohydrate and a short C-terminal hydrophobic domain . These properties are consistent with the mature proteins being either virion.ell surface or secretory glycoproteins. Protein sequence comparisons reveal that the gene products are related to each other (20% identity) and to the Ig superfamily. The highest degree of similarity is to the human and murine interleukin-1 receptors.lthough both proteins are related to a wide range of Ig superfamily members.ncluding the interleukin-6 receptor. A novel method for virus immune evasion has been proposed in which the product of one or both of these proteins may bind interleukin-1 and/or interleukin-6.reventing these cytokines reaching their natural receptors . A similar gene product from cowpox virus has also been shown to specifically bind murine IL-1 beta .The crystal structure of the soluble extracellular part of type-I IL1Rcomplexed with IL1RA has been determined to 2.7A resolution . The receptor structure is characterised by three Ig-like domains.f whichdomains 1 and 2 are tightly linked.hile domain 3 is completely separate and connected by a flexible linker.
  IPR004074:Interleukin-1 receptor, type I and type II
Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses.nflammatory reactions.nd hematopoiesis . Two types of IL-1 receptor.ach with three extracellular immunoglobulin (Ig)-like domains.imited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors . The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors.Both IL-1 receptors appear to be well conserved in evolution.nd map to thesame chromosomal location. The receptors can both bind all three forms of IL-1 (IL-1 alpha.L-1 beta and IL-1RA) . The mature type I IL-1 receptor consists of (i) a ligand binding portion comprising three Ig-likedomains; (ii) a single TM domain; and (iii) a large cytoplasmic domain of ~215 amino acids. This domain is shared by a number of other proteins.ncluding the rat FIT-1M precursor.he murine ST2L protein precursor.uman oligophrenin-4 and interleukin-18 receptor accessory protein.nd Drosophila toll-like proteins.
  IPR004075:Interleukin-1 receptor, type I/Toll precursor
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR000157:TIR 
Evalue:-42.9586067199707 
Location:407-545IPR003599:IG 
Evalue:-2.82390874094432 
Location:251-350IPR003599:IG 
Evalue:-1.65757731917779 
Location:32-132IPR013783:Ig-like_fold 
Evalue:0 
Location:145-237IPR004075:INTRLKN1R1F 
Evalue:0 
Location:362-390
SequencesProtein: IL1AP_HUMAN (570 aa)
mRNA: NM_002182
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
KO assignmentK04723
  Level 3 annotation:
    interleukin 1 receptor accessory protein
  Level 2 annotation:
    Cytokine receptors
    Cytokine-cytokine receptor interaction
    Apoptosis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 40 residues, 191714584-191714702Exon2: 31 residues, 191756612-191756699Exon3: 23 residues, 191764771-191764836Exon4: 97 residues, 191804610-191804896Exon5: 64 residues, 191809477-191809664Exon6: 57 residues, 191820757-191820923Exon7: 26 residues, 191823826-191823898Exon8: 44 residues, 191827805-191827932Exon9: 51 residues, 191829832-191829981Exon10: 52 residues, 191844730-191844880Exon11: 50 residues, 191846181-191846325Exon12: 1060 residues, 191848820-191851995Exon13: 2 residues, -Jump to IL1AP_HUMAN  
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