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Interleukin-1 receptor type 2 (IL-1R-2) (IL-1RT-2) (IL-1RT2) (CD121 antigen-like family member B) (IL-1 type II receptor) (Interleukin-1 receptor beta) (IL-1R-beta) (Interleukin-1 receptor type II) (CD antigen CD121b) [Cleaved into: Interleukin-1 receptor type 2, membrane form (mIL-1R2) (mIL-1RII); Interleukin-1 receptor type 2, soluble form (sIL-1R2) (sIL-1RII)]

 IL1R2_MOUSE             Reviewed;         410 AA.
P27931;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Interleukin-1 receptor type 2;
Short=IL-1R-2;
Short=IL-1RT-2;
Short=IL-1RT2;
AltName: Full=CD121 antigen-like family member B;
AltName: Full=IL-1 type II receptor;
AltName: Full=Interleukin-1 receptor beta;
Short=IL-1R-beta;
AltName: Full=Interleukin-1 receptor type II;
AltName: CD_antigen=CD121b;
Contains:
RecName: Full=Interleukin-1 receptor type 2, membrane form;
Short=mIL-1R2;
Short=mIL-1RII;
Contains:
RecName: Full=Interleukin-1 receptor type 2, soluble form;
Short=sIL-1R2;
Short=sIL-1RII;
Flags: Precursor;
Name=Il1r2; Synonyms=Il-1r2, Il1rb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1833184;
McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D.,
Brunton L.L., Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I.,
Copeland N.G., Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D.,
Dower S.K., Spriggs M.K., Sims J.E.;
"A novel IL-1 receptor, cloned from B cells by mammalian expression,
is expressed in many cell types.";
EMBO J. 10:2821-2832(1991).
[2]
FUNCTION AS DECOY RECEPTOR.
PubMed=8332913; DOI=10.1126/science.8332913;
Colotta F., Re F., Muzio M., Bertini R., Polentarutti N., Sironi M.,
Giri J.G., Dower S.K., Sims J.E., Mantovani A.;
"Interleukin-1 type II receptor: a decoy target for IL-1 that is
regulated by IL-4.";
Science 261:472-475(1993).
[3]
FUNCTION.
PubMed=9662436; DOI=10.1016/S0014-5793(98)00467-0;
Malinowsky D., Lundkvist J., Laye S., Bartfai T.;
"Interleukin-1 receptor accessory protein interacts with the type II
interleukin-1 receptor.";
FEBS Lett. 429:299-302(1998).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-208.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[5]
TISSUE SPECIFICITY.
PubMed=15986350; DOI=10.1002/art.21108;
Smeets R.L., Joosten L.A., Arntz O.J., Bennink M.B., Takahashi N.,
Carlsen H., Martin M.U., van den Berg W.B., van de Loo F.A.;
"Soluble interleukin-1 receptor accessory protein ameliorates
collagen-induced arthritis by a different mode of action from that of
interleukin-1 receptor antagonist.";
Arthritis Rheum. 52:2202-2211(2005).
-!- FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces
IL1B activities. Serves as a decoy receptor by competetive binding
to IL1B and preventing its binding to IL1R1. Also modulates
cellular response through non-signaling association with IL1RAP
after binding to IL1B. IL1R2 (membrane and secreted forms)
preferentially binds IL1B and poorly IL1A and IL1RN. The secreted
IL1R2 recruits secreted IL1RAP with high affinity; this complex
formation may be the dominant mechanism for neutralization of IL1B
by secreted/soluble receptors (By similarity). {ECO:0000250,
ECO:0000269|PubMed:8332913, ECO:0000269|PubMed:9662436}.
-!- SUBUNIT: Associates with IL1RAP to form a non-signaling
interleukin-1 receptor complex. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell membrane {ECO:0000250}. Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Strongly expressed in B-cells, with levels 21
times higher than IL1R1. In T-cells expressed 5 times more
compared with IL1R1. {ECO:0000269|PubMed:15986350}.
-!- PTM: A soluble form (sIL1R2) can also be produced by proteolytic
cleavage at the cell surface (shedding) involving a
metalloproteinase. {ECO:0000250}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X59769; CAA42440.1; -; mRNA.
CCDS; CCDS14909.1; -.
RefSeq; NP_034685.1; NM_010555.4.
RefSeq; XP_011236739.1; XM_011238437.2.
RefSeq; XP_011236740.1; XM_011238438.2.
RefSeq; XP_011236741.1; XM_011238439.2.
RefSeq; XP_011236742.1; XM_011238440.2.
UniGene; Mm.1349; -.
ProteinModelPortal; P27931; -.
SMR; P27931; -.
BioGrid; 200626; 1.
IntAct; P27931; 1.
MINT; P27931; -.
STRING; 10090.ENSMUSP00000027243; -.
iPTMnet; P27931; -.
PhosphoSitePlus; P27931; -.
PaxDb; P27931; -.
PeptideAtlas; P27931; -.
PRIDE; P27931; -.
Ensembl; ENSMUST00000027243; ENSMUSP00000027243; ENSMUSG00000026073.
GeneID; 16178; -.
KEGG; mmu:16178; -.
UCSC; uc007atu.2; mouse.
CTD; 7850; -.
MGI; MGI:96546; Il1r2.
eggNOG; ENOG410IJCQ; Eukaryota.
eggNOG; ENOG410YQDP; LUCA.
GeneTree; ENSGT00760000119071; -.
HOGENOM; HOG000113036; -.
HOVERGEN; HBG052104; -.
InParanoid; P27931; -.
KO; K04387; -.
OMA; RQEYSEN; -.
OrthoDB; EOG091G077L; -.
PhylomeDB; P27931; -.
TreeFam; TF325519; -.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
ChiTaRS; Il1r2; mouse.
PRO; PR:P27931; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026073; Expressed in 96 organ(s), highest expression level in decidua.
CleanEx; MM_IL1R2; -.
ExpressionAtlas; P27931; baseline and differential.
Genevisible; P27931; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0019966; F:interleukin-1 binding; IPI:MGI.
GO; GO:0004908; F:interleukin-1 receptor activity; IPI:MGI.
GO; GO:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:MGI.
GO; GO:0050712; P:negative regulation of interleukin-1 alpha secretion; IMP:MGI.
GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IPI:MGI.
GO; GO:0010955; P:negative regulation of protein processing; IMP:MGI.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR004077; IL-1_rcpt_II-typ.
InterPro; IPR013151; Immunoglobulin.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF00047; ig; 1.
PRINTS; PR01539; INTRLEUKN1R2.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 13 {ECO:0000255}.
CHAIN 14 410 Interleukin-1 receptor type 2, membrane
form.
/FTId=PRO_0000015440.
CHAIN 14 ? Interleukin-1 receptor type 2, soluble
form.
/FTId=PRO_0000415349.
TOPO_DOM 14 355 Extracellular. {ECO:0000255}.
TRANSMEM 356 381 Helical. {ECO:0000255}.
TOPO_DOM 382 410 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 136 Ig-like C2-type 1.
DOMAIN 146 237 Ig-like C2-type 2.
DOMAIN 249 357 Ig-like C2-type 3.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 128 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 64 120 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 164 219 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 270 338 {ECO:0000255|PROSITE-ProRule:PRU00114}.
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


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