IL1R2_MOUSE
ID IL1R2_MOUSE Reviewed; 410 AA.
AC P27931;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1833184; DOI=10.1002/j.1460-2075.1991.tb07831.x;
RA McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D., Brunton L.L.,
RA Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I., Copeland N.G.,
RA Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D., Dower S.K.,
RA Spriggs M.K., Sims J.E.;
RT "A novel IL-1 receptor, cloned from B cells by mammalian expression, is
RT expressed in many cell types.";
RL EMBO J. 10:2821-2832(1991).
RN [2]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=8332913; DOI=10.1126/science.8332913;
RA Colotta F., Re F., Muzio M., Bertini R., Polentarutti N., Sironi M.,
RA Giri J.G., Dower S.K., Sims J.E., Mantovani A.;
RT "Interleukin-1 type II receptor: a decoy target for IL-1 that is regulated
RT by IL-4.";
RL Science 261:472-475(1993).
RN [3]
RP FUNCTION.
RX PubMed=9662436; DOI=10.1016/s0014-5793(98)00467-0;
RA Malinowsky D., Lundkvist J., Laye S., Bartfai T.;
RT "Interleukin-1 receptor accessory protein interacts with the type II
RT interleukin-1 receptor.";
RL FEBS Lett. 429:299-302(1998).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-208.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15986350; DOI=10.1002/art.21108;
RA Smeets R.L., Joosten L.A., Arntz O.J., Bennink M.B., Takahashi N.,
RA Carlsen H., Martin M.U., van den Berg W.B., van de Loo F.A.;
RT "Soluble interleukin-1 receptor accessory protein ameliorates collagen-
RT induced arthritis by a different mode of action from that of interleukin-1
RT receptor antagonist.";
RL Arthritis Rheum. 52:2202-2211(2005).
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, ECO:0000269|PubMed:8332913, ECO:0000269|PubMed:9662436}.
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 -!- TISSUE SPECIFICITY: Strongly expressed in B-cells, with levels 21 times
CC higher than IL1R1. In T-cells expressed 5 times more compared with
CC IL1R1. {ECO:0000269|PubMed:15986350}.
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; X59769; CAA42440.1; -; mRNA.
DR CCDS; CCDS14909.1; -.
DR RefSeq; NP_034685.1; NM_010555.4.
DR RefSeq; XP_011236739.1; XM_011238437.2.
DR RefSeq; XP_011236740.1; XM_011238438.2.
DR RefSeq; XP_011236741.1; XM_011238439.2.
DR RefSeq; XP_011236742.1; XM_011238440.2.
DR AlphaFoldDB; P27931; -.
DR SMR; P27931; -.
DR BioGRID; 200626; 1.
DR STRING; 10090.ENSMUSP00000027243; -.
DR GlyGen; P27931; 4 sites.
DR iPTMnet; P27931; -.
DR PhosphoSitePlus; P27931; -.
DR PaxDb; P27931; -.
DR PeptideAtlas; P27931; -.
DR PRIDE; P27931; -.
DR ProteomicsDB; 267317; -.
DR ABCD; P27931; 4 sequenced antibodies.
DR Antibodypedia; 17756; 669 antibodies from 41 providers.
DR DNASU; 16178; -.
DR Ensembl; ENSMUST00000027243; ENSMUSP00000027243; ENSMUSG00000026073.
DR GeneID; 16178; -.
DR KEGG; mmu:16178; -.
DR UCSC; uc007atu.2; mouse.
DR CTD; 7850; -.
DR MGI; MGI:96546; Il1r2.
DR VEuPathDB; HostDB:ENSMUSG00000026073; -.
DR eggNOG; ENOG502QVTS; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_051287_0_0_1; -.
DR InParanoid; P27931; -.
DR OMA; CDEMSIE; -.
DR OrthoDB; 985064at2759; -.
DR PhylomeDB; P27931; -.
DR TreeFam; TF325519; -.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR BioGRID-ORCS; 16178; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Il1r2; mouse.
DR PRO; PR:P27931; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P27931; protein.
DR Bgee; ENSMUSG00000026073; Expressed in gastrula and 81 other tissues.
DR ExpressionAtlas; P27931; baseline and differential.
DR Genevisible; P27931; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; IPI:MGI.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IPI:MGI.
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; IMP:MGI.
DR GO; GO:0032690; P:negative regulation of interleukin-1 alpha production; IMP:MGI.
DR GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IPI:MGI.
DR GO; GO:0010955; P:negative regulation of protein processing; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
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 1: Evidence at protein 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..410
FT /note="Interleukin-1 receptor type 2, membrane form"
FT /id="PRO_0000015440"
FT CHAIN 14..?
FT /note="Interleukin-1 receptor type 2, soluble form"
FT /id="PRO_0000415349"
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..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..136
FT /note="Ig-like C2-type 1"
FT DOMAIN 146..237
FT /note="Ig-like C2-type 2"
FT DOMAIN 249..357
FT /note="Ig-like C2-type 3"
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:0000269|PubMed:16944957"
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 410 AA; 45645 MW; 923DFC27C70AF604 CRC64;
MFILLVLVTG VSAFTTPTVV HTGKVSESPI TSEKPTVHGD NCQFRGREFK SELRLEGEPV
VLRCPLAPHS DISSSSHSFL TWSKLDSSQL IPRDEPRMWV KGNILWILPA VQQDSGTYIC
TFRNASHCEQ MSVELKVFKN TEASLPHVSY LQISALSTTG LLVCPDLKEF ISSNADGKIQ
WYKGAILLDK GNKEFLSAGD PTRLLISNTS MDDAGYYRCV MTFTYNGQEY NITRNIELRV
KGTTTEPIPV IISPLETIPA SLGSRLIVPC KVFLGTGTSS NTIVWWLANS TFISAAYPRG
RVTEGLHHQY SENDENYVEV SLIFDPVTRE DLHTDFKCVA SNPRSSQSLH TTVKEVSSTF
SWSIALAPLS LIILVVGAIW MRRRCKRRAG KTYGLTKLRT DNQDFPSSPN
