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P27930 (IL1R2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-1 receptor type 2

Short name=IL-1R-2
Short name=IL-1RT-2
Short name=IL-1RT2
Alternative name(s):
CD121 antigen-like family member B
CDw121b
IL-1 type II receptor
Interleukin-1 receptor beta
Short name=IL-1R-beta
Interleukin-1 receptor type II
CD_antigen=CD121b

Cleaved into the following 2 chains:

  1. Interleukin-1 receptor type 2, membrane form
    Short name=mIL-1R2
    Short name=mIL-1RII
  2. Interleukin-1 receptor type 2, soluble form
    Short name=sIL-1R2
    Short name=sIL-1RII
Gene names
Name:IL1R2
Synonyms:IL1RB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.11 Ref.12 Ref.13

Subunit structure

Associates with IL1RAP to form a non-signaling interleukin-1 receptor complex. Ref.14

Subcellular location

Isoform Short: Secreted Ref.2.

Isoform Long: Cell membrane; Single-pass type I membrane protein Ref.2.

Post-translational modification

A soluble form (sIL1R2) can also be produced by proteolytic cleavage at the cell surface (shedding) involving a metalloproteinase; hovever, several sIL1R2 forms ranging from 45 and 60 kDa are reported.

Sequence similarities

Belongs to the interleukin-1 receptor family.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P27930-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P27930-2)

The sequence of this isoform differs from the canonical sequence as follows:
     297-398: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1313 Potential
Chain14 – 398385Interleukin-1 receptor type 2, membrane form
PRO_0000015439
Chain14 – ?Interleukin-1 receptor type 2, soluble formPRO_0000415348

Regions

Topological domain14 – 343330Extracellular Potential
Transmembrane344 – 36926Helical; Potential
Topological domain370 – 39829Cytoplasmic Potential
Domain18 – 124107Ig-like C2-type 1
Domain134 – 22390Ig-like C2-type 2
Domain237 – 349113Ig-like C2-type 3
Region329 – 34315Contains proteolytic cleavage site Probable

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Ref.14
Glycosylation2191N-linked (GlcNAc...) Ref.14
Glycosylation2771N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 116 Ref.14
Disulfide bond50 ↔ 108 Ref.14
Disulfide bond152 ↔ 207 Ref.14
Disulfide bond258 ↔ 326 Ref.14

Natural variations

Alternative sequence297 – 398102Missing in isoform Short.
VSP_042222
Natural variant1811E → K. Ref.4
Corresponds to variant rs28385682 [ dbSNP | Ensembl ].
VAR_019132
Natural variant2921E → K. Ref.4
Corresponds to variant rs3218976 [ dbSNP | Ensembl ].
VAR_019133

Experimental info

Sequence conflict1231L → F in AAD00242. Ref.2
Sequence conflict1711K → R in AAD00242. Ref.2
Sequence conflict1991L → Q in AAD00242. Ref.2

Secondary structure

............................................................ 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 2C2A03ADA6F3AC5B

FASTA39845,421
        10         20         30         40         50         60 
MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC PQVPYWLWAS 

        70         80         90        100        110        120 
VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ EDSGTYVCTT RNASYCDKMS 

       130        140        150        160        170        180 
IELRVFENTD AFLPFISYPQ ILTLSTSGVL VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN 

       190        200        210        220        230        240 
EKFLSVRGTT HLLVHDVALE DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII 

       250        260        270        280        290        300 
SPLKTISASL GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE 

       310        320        330        340        350        360 
NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW GIVLAPLSLA 

       370        380        390 
FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK 

« Hide

Isoform Short [UniParc].

Checksum: 581AA026BB7DACD5
Show »

FASTA29633,622

References

« Hide 'large scale' references
[1]"A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types."
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.
EMBO J. 10:2821-2832(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: B-cell.
[2]"Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA."
Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.
J. Biol. Chem. 271:20965-20972(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), IL1B-BINDING, SUBCELLULAR LOCATION (ISOFORM SHORT).
[3]"Complete nucleotide sequence and expression of the human interleukin-1 receptor type II in human gingival fibroblasts."
Chou H.-H., Takashiba T., Takigawa M., Maeda H., Asahara Y., Nishimura F., Arai H., Murayama Y.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[4]SeattleSNPs variation discovery resource
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-181 AND LYS-292.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Ovary.
[8]"Elevated levels of shed type II IL-1 receptor in sepsis. Potential role for type II receptor in regulation of IL-1 responses."
Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J., Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.
J. Immunol. 153:5802-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC PROCESSING, LIGAND-BINDING.
[9]"Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist."
Symons J.A., Young P.R., Duff G.W.
Proc. Natl. Acad. Sci. U.S.A. 92:1714-1718(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: LIGAND-BINDING.
[10]"Role of metalloproteases in the release of the IL-1 type II decoy receptor."
Orlando S., Sironi M., Bianchi G., Drummond A.H., Boraschi D., Yabes D., Mantovani A.
J. Biol. Chem. 272:31764-31769(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[11]"The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: a novel mechanism of regulation of IL-1 responsiveness."
Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D., Martin M.U.
J. Immunol. 161:6871-6877(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IL1RAP.
[12]"The membrane form of the type II IL-1 receptor accounts for inhibitory function."
Neumann D., Kollewe C., Martin M.U., Boraschi D.
J. Immunol. 165:3350-3357(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS DECOY RECEPTOR.
[13]"The soluble form of IL-1 receptor accessory protein enhances the ability of soluble type II IL-1 receptor to inhibit IL-1 action."
Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M., MacVittie T.J., Virca G.D., Sims J.E.
Immunity 18:87-96(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS DECOY RECEPTOR.
[14]"Structural insights into the assembly and activation of IL-1beta with its receptors."
Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.
Nat. Immunol. 11:905-911(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 14-343 IN COMPLEX WITH IL1RAP AND IL1B, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-112 AND ASN-219.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59770 mRNA. Translation: CAA42441.1.
U64094 mRNA. Translation: AAB05878.1.
U74649 mRNA. Translation: AAD00242.1.
AY124010 Genomic DNA. Translation: AAM64221.1.
AC007165 Genomic DNA. Translation: AAK52072.1.
CH471127 Genomic DNA. Translation: EAX01800.1.
CH471127 Genomic DNA. Translation: EAX01801.1.
CH471127 Genomic DNA. Translation: EAX01802.1.
CH471127 Genomic DNA. Translation: EAX01803.1.
BC039031 mRNA. Translation: AAH39031.1.
PIRS17428.
RefSeqNP_001248348.1. NM_001261419.1.
NP_004624.1. NM_004633.3.
UniGeneHs.25333.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4OX-ray3.30C14-343[»]
ProteinModelPortalP27930.
SMRP27930. Positions 28-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113605. 1 interaction.
IntActP27930. 3 interactions.
STRING9606.ENSP00000330959.

Chemistry

DrugBankDB00026. Anakinra.

PTM databases

PhosphoSiteP27930.

Polymorphism databases

DMDM124310.

Proteomic databases

PaxDbP27930.
PRIDEP27930.

Protocols and materials databases

DNASU7850.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332549; ENSP00000330959; ENSG00000115590. [P27930-1]
ENST00000393414; ENSP00000377066; ENSG00000115590. [P27930-1]
ENST00000441002; ENSP00000414611; ENSG00000115590. [P27930-2]
GeneID7850.
KEGGhsa:7850.
UCSCuc002tbm.3. human. [P27930-1]

Organism-specific databases

CTD7850.
GeneCardsGC02P102608.
HGNCHGNC:5994. IL1R2.
HPAHPA027597.
HPA027598.
MIM147811. gene.
neXtProtNX_P27930.
PharmGKBPA29810.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44340.
HOGENOMHOG000113036.
HOVERGENHBG052104.
InParanoidP27930.
KOK04387.
OMARQEYSEN.
OrthoDBEOG77HDDW.
PhylomeDBP27930.
TreeFamTF325519.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP27930.
BgeeP27930.
CleanExHS_IL1R2.
GenevestigatorP27930.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL-1_rcpt_fam.
IPR004074. IL-1_rcpt_I/II-typ.
IPR004077. IL-1_rcpt_II-typ.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERPTHR11890. PTHR11890. 1 hit.
PfamPF00047. ig. 1 hit.
[Graphical view]
PRINTSPR01539. INTRLEUKN1R2.
PR01536. INTRLKN1R12F.
SMARTSM00409. IG. 3 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27930.
GeneWikiInterleukin_1_receptor,_type_II.
GenomeRNAi7850.
NextBio30276.
PROP27930.
SOURCESearch...

Entry information

Entry nameIL1R2_HUMAN
AccessionPrimary (citable) accession number: P27930
Secondary accession number(s): D3DVJ5, Q6LCE6, Q9UE68
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries