IL1R2_CHLAE
ID IL1R2_CHLAE Reviewed; 393 AA.
AC Q29612;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=IL1RB;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN SEQUENCE
RP OF 125-145.
RX PubMed=8702856; DOI=10.1074/jbc.271.34.20965;
RA Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.;
RT "Cloning and characterization of an alternatively processed human type II
RT interleukin-1 receptor mRNA.";
RL J. Biol. Chem. 271:20965-20972(1996).
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: Forms a non-signaling receptor complex consisting of IL1R2 and
CC IL1RAP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q29612-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q29612-2; Sequence=VSP_002663;
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; U64092; AAB05876.1; -; mRNA.
DR EMBL; U64093; AAB05877.1; -; mRNA.
DR AlphaFoldDB; Q29612; -.
DR SMR; Q29612; -.
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:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..393
FT /note="Interleukin-1 receptor type 2, membrane form"
FT /id="PRO_0000015438"
FT CHAIN 14..?
FT /note="Interleukin-1 receptor type 2, soluble form"
FT /id="PRO_0000415347"
FT TOPO_DOM 14..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..120
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..221
FT /note="Ig-like C2-type 2"
FT DOMAIN 237..342
FT /note="Ig-like C2-type 3"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 50..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 258..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 297..393
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8702856"
FT /id="VSP_002663"
SQ SEQUENCE 393 AA; 44779 MW; D4D746C5DE569AB8 CRC64;
MFRLYVLVMG VSAFTLQPAA HTGAARSCPV RGRHYKREFR LEGEPVALRC PQVPYQLWAS
VSPHINLTWH KNDSARMVPG EEETRMWAQD GALWLLPALQ EDSGTYICTT RNASYCDKVS
IELRVFENTD ASLPFISYPQ ILTLSTFGVL VCPDLREFTR DKTDGKIQWY KDFLPLDKDN
EKFLSVRGTT HLLVHDVALE DAGYYRCVLT FAHEGQQYNI TRNIELRIKK KKEETIPVII
SPLKTISASL GSRLTIPCKV FLGTGTPLTT MLWWTANDTH VESAYPGGRV TEGPRQEYSE
NNENYIEVPL IFDPVTRKDL NMVFKCFVRN TMGFQTLRTT VKEPPPTFSW GIVLAPLALA
FLVLGGIWMH RRCKHRTGKA DGLTVLRPHH QDF
