IL1R2_RAT
ID IL1R2_RAT Reviewed; 416 AA.
AC P43303; Q5BJ99;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Interleukin-1 receptor type 2;
DE Short=IL-1R-2;
DE Short=IL-1RT-2;
DE Short=IL-1RT2;
DE AltName: Full=CD121 antigen-like family member B;
DE AltName: Full=IL-1 type II receptor;
DE AltName: Full=Interleukin-1 receptor beta;
DE Short=IL-1R-beta;
DE AltName: Full=Interleukin-1 receptor type II;
DE AltName: CD_antigen=CD121b;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, membrane form;
DE Short=mIL-1R2;
DE Short=mIL-1RII;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, soluble form;
DE Short=sIL-1R2;
DE Short=sIL-1RII;
DE Flags: Precursor;
GN Name=Il1r2; Synonyms=Il-1r2, Il1rb;
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].
RX PubMed=7524717;
RA Bristulf J., Gatti S., Malinowsky D., Bjork L., Sundgren A.K., Bartfai T.;
RT "Interleukin-1 stimulates the expression of type I and type II interleukin-
RT 1 receptors in the rat insulinoma cell line Rinm5F; sequencing a rat type
RT II interleukin-1 receptor cDNA.";
RL Eur. Cytokine Netw. 5:319-330(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B
CC activities. Serves as a decoy receptor by competitive binding to IL1B
CC and preventing its binding to IL1R1. Also modulates cellular response
CC through non-signaling association with IL1RAP after binding to IL1B.
CC IL1R2 (membrane and secreted forms) preferentially binds IL1B and
CC poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with
CC high affinity; this complex formation may be the dominant mechanism for
CC neutralization of IL1B by secreted/soluble receptors (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associates with IL1RAP to form a non-signaling interleukin-1
CC receptor complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell membrane {ECO:0000250}. Secreted {ECO:0000250}.
CC -!- PTM: A soluble form (sIL1R2) can also be produced by proteolytic
CC cleavage at the cell surface (shedding) involving a metalloproteinase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; Z22812; CAA80465.1; -; mRNA.
DR EMBL; BC091564; AAH91564.1; -; mRNA.
DR PIR; S33473; S33473.
DR RefSeq; NP_446405.1; NM_053953.1.
DR RefSeq; XP_008765206.1; XM_008766984.2.
DR RefSeq; XP_017451737.1; XM_017596248.1.
DR AlphaFoldDB; P43303; -.
DR SMR; P43303; -.
DR STRING; 10116.ENSRNOP00000019415; -.
DR GlyGen; P43303; 4 sites.
DR PaxDb; P43303; -.
DR GeneID; 117022; -.
DR KEGG; rno:117022; -.
DR UCSC; RGD:621147; rat.
DR CTD; 7850; -.
DR RGD; 621147; Il1r2.
DR eggNOG; ENOG502QVTS; Eukaryota.
DR HOGENOM; CLU_051287_0_0_1; -.
DR InParanoid; P43303; -.
DR PhylomeDB; P43303; -.
DR TreeFam; TF325519; -.
DR Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR PRO; PR:P43303; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P43303; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019966; F:interleukin-1 binding; ISO:RGD.
DR GO; GO:0004908; F:interleukin-1 receptor activity; ISO:RGD.
DR GO; GO:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:RGD.
DR GO; GO:0032690; P:negative regulation of interleukin-1 alpha production; ISO:RGD.
DR GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010955; P:negative regulation of protein processing; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR004077; IL-1_rcpt_II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF18452; Ig_6; 1.
DR PRINTS; PR01539; INTRLEUKN1R2.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..416
FT /note="Interleukin-1 receptor type 2, membrane form"
FT /id="PRO_0000015441"
FT CHAIN 14..?
FT /note="Interleukin-1 receptor type 2, soluble form"
FT /id="PRO_0000415350"
FT TOPO_DOM 14..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..136
FT /note="Ig-like C2-type 1"
FT DOMAIN 146..233
FT /note="Ig-like C2-type 2"
FT DOMAIN 249..357
FT /note="Ig-like C2-type 3"
FT REGION 396..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
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 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 64..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 416 AA; 46353 MW; 50EFBA48881C5D4E CRC64;
MFILLVLVTG VSAFTTPAVV HTGRVSESPV TSEKHPVLGD DCWFRGRDFK SELRLEGEPV
VLRCPLVPHS DTSSSSRSLL TWSKSDSSQL IPGDEPRMWV KDDTLWVLPA VQQDSGTYIC
TFRNASHCEQ MSLELKVFKN TEASFPLVSY LQISALSSTG LLVCPDLKEF ISSRTDGKIQ
WYKGSILLDK GNKKFLSAGD PTRLLISNTS MGDAGYYRCV MTFTYEGKEY NITRNIELRV
KGITTEPIPV IISPLETIPA SLGSRLIVPC KVFLGTGTSS NTIVWWMANS TFISVAYPRG
RVTEGLHHQY SENDENYVEV SLIFDPVTKE DLNTDFKCVA TNPRSFQSLH TTVKEVSSTF
SWGIALAPLS LIILVVGAIW IRRRCKRQAG KTYGLTKLPT DNQDFPSSPN QIKEMK
