ILRL2_RAT
ID ILRL2_RAT Reviewed; 561 AA.
AC Q62929;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Interleukin-1 receptor-like 2;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=IL-36 receptor;
DE AltName: Full=Interleukin-1 receptor-related protein 2;
DE Short=IL-1Rrp2;
DE Short=IL1R-rp2;
DE Flags: Precursor;
GN Name=Il1rl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8898719; DOI=10.1016/s0165-5728(96)00047-1;
RA Lovenberg T.W., Crowe P.D., Liu C., Chalmers D.T., Liu X.-J., Liaw C.,
RA Clevenger W., Oltersdorf T., De Souza E.B., Maki R.A.;
RT "Cloning of a cDNA encoding a novel interleukin-1 receptor related protein
RT (IL1R-rp2).";
RL J. Neuroimmunol. 70:113-122(1996).
CC -!- FUNCTION: Receptor for interleukin-36 (IL36A, IL36B and IL36G). After
CC binding to interleukin-36 associates with the coreceptor IL1RAP to form
CC the interleukin-36 receptor complex which mediates interleukin-36-
CC dependent activation of NF-kappa-B, MAPK and other pathways. The IL-36
CC signaling system is thought to be present in epithelial barriers and to
CC take part in local inflammatory response; it is similar to the IL-1
CC system. Seems to be involved in skin inflammatory response by induction
CC of the IL-23/IL-17/IL-22 pathway. Receptor for the interleukin IL36G.
CC Binding to the agonist leads to the activation of NF-kappa-B (By
CC similarity). {ECO:0000250|UniProtKB:Q9ERS7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBUNIT: Interacts with IL1RAP; the association is enhanced by IL36B
CC indicative for an functional signaling complex and inhibited by IL36RN
CC (By similarity). {ECO:0000250|UniProtKB:Q9ERS7}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Predominant expression in the lung and epididymis,
CC with lower expression in cerebral cortex and testis. Expression in the
CC brain is non-neuronal and associated with the cerebral vasculature. Not
CC detected in any cell line tested.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; U49066; AAB53238.1; -; mRNA.
DR RefSeq; NP_598259.1; NM_133575.1.
DR AlphaFoldDB; Q62929; -.
DR SMR; Q62929; -.
DR STRING; 10116.ENSRNOP00000019880; -.
DR GlyGen; Q62929; 11 sites.
DR PaxDb; Q62929; -.
DR GeneID; 171106; -.
DR KEGG; rno:171106; -.
DR UCSC; RGD:621782; rat.
DR CTD; 8808; -.
DR RGD; 621782; Il1rl2.
DR eggNOG; ENOG502QWEU; Eukaryota.
DR InParanoid; Q62929; -.
DR OrthoDB; 1109920at2759; -.
DR PhylomeDB; Q62929; -.
DR Reactome; R-RNO-9007892; Interleukin-38 signaling.
DR Reactome; R-RNO-9014826; Interleukin-36 pathway.
DR PRO; PR:Q62929; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW NAD; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..561
FT /note="Interleukin-1 receptor-like 2"
FT /id="PRO_0000015447"
FT TOPO_DOM 22..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..215
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..321
FT /note="Ig-like C2-type 3"
FT DOMAIN 384..539
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 149..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 252..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 561 AA; 64142 MW; 4021C297917F0199 CRC64;
MGMPPLLFCW VSFVLPLFVA AGNCTDVYMH HEMISEGQPF PFNCTYPPVT NGAVNLTWHR
TPSKSPISIN RHVRIHQDQS WILFLPLALE DSGIYQCVIK DAHSCYRIAI NLTVFRKHWC
DSSNEESSIN SSDEYQQWLP IGKSGSLTCH LYFPESCVLD SIKWYKGCEE IKVSKKFCPT
GTKLLVNNID VEDSGSYACS ARLTHLGRIF TVRNYIAVNT KEVGSGGRIP NITYPKNNSI
EVQLGSTLIV DCNITDTKEN TNLRCWRVNN TLVDDYYNDF KRIQEGIETN LSLRNHILYT
VNITFLEVKM EDYGHPFTCH AAVSAAYIIL KRPAPDFRAY LIGGLMAFLL LAVSILYIYN
TFKVDIVLWY RSTFHTAQAP DDEKLYDAYV LYPKYPRESQ GHDVDTLVLK ILPEVLEKQC
GYKLFIFGRD EFPGQAVASV IDENIKLCRR LMVLVAPETS SFSFLKNLTE EQIAVYNALV
QDGMKVILIE LERVKDYSTM PESIQYIRQK HGAIQWDGDF TEQAQCAKTK FWKKVRYHMP
PRRYPASPPV QLLGHTPRIP G
