Interleukin-1 receptor type 2

Details

Name
Interleukin-1 receptor type 2
Synonyms
  • CD121 antigen-like family member B
  • CDw121b
  • IL-1 type II receptor
  • IL-1R-2
  • IL-1R-beta
  • IL1RB
  • Interleukin-1 receptor beta
  • Interleukin-1 receptor type II
Gene Name
IL1R2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0051971|Interleukin-1 receptor type 2
MLRLYVLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWAS
VSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS
IELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDN
EKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKKEETIPVII
SPLKTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSE
NNENYIEVPLIFDPVTREDLHMDFKCVVHNTLSFQTLRTTVKEASSTFSWGIVLAPLSLA
FLVLGGIWMHRRCKHRTGKADGLTVLWPHHQDFQSYPK
Number of residues
398
Molecular Weight
45420.685
Theoretical pI
Not Available
GO Classification
Functions
interleukin-1 binding / interleukin-1 receptor activity / interleukin-1, Type II, blocking receptor activity
Processes
cytokine-mediated signaling pathway / immune response / interleukin-1-mediated signaling pathway / negative regulation of cytokine production involved in inflammatory response / negative regulation of interleukin-1 alpha secretion / negative regulation of interleukin-1-mediated signaling pathway / negative regulation of protein processing
Components
cytoplasm / extracellular region / integral component of membrane / plasma membrane
General 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.
Specific Function
Interleukin-1 binding
Pfam Domain Function
Transmembrane Regions
344-369
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0051972|Interleukin-1 receptor type 2 (IL1R2)
ATGTTGCGCTTGTACGTGTTGGTAATGGGAGTTTCTGCCTTCACCCTTCAGCCTGCGGCA
CACACAGGGGCTGCCAGAAGCTGCCGGTTTCGTGGGAGGCATTACAAGCGGGAGTTCAGG
CTGGAAGGGGAGCCTGTAGCCCTGAGGTGCCCCCAGGTGCCCTACTGGTTGTGGGCCTCT
GTCAGCCCCCGCATCAACCTGACATGGCATAAAAATGACTCTGCTAGGACGGTCCCAGGA
GAAGAAGAGACACGGATGTGGGCCCAGGACGGTGCTCTGTGGCTTCTGCCAGCCTTGCAG
GAGGACTCTGGCACCTACGTCTGCACTACTAGAAATGCTTCTTACTGTGACAAAATGTCC
ATTGAGCTCAGAGTTTTTGAGAATACAGATGCTTTCCTGCCGTTCATCTCATACCCGCAA
ATTTTAACCTTGTCAACCTCTGGGGTATTAGTATGCCCTGACCTGAGTGAATTCACCCGT
GACAAAACTGACGTGAAGATTCAATGGTACAAGGATTCTCTTCTTTTGGATAAAGACAAT
GAGAAATTTCTAAGTGTGAGGGGGACCACTCACTTACTCGTACACGATGTGGCCCTGGAA
GATGCTGGCTATTACCGCTGTGTCCTGACATTTGCCCATGAAGGCCAGCAATACAACATC
ACTAGGAGTATTGAGCTACGCATCAAGAAAAAAAAAGAAGAGACCATTCCTGTGATCATT
TCCCCCCTCAAGACCATATCAGCTTCTCTGGGGTCAAGACTGACAATCCCGTGTAAGGTG
TTTCTGGGAACCGGCACACCCTTAACCACCATGCTGTGGTGGACGGCCAATGACACCCAC
ATAGAGAGCGCCTACCCGGGAGGCCGCGTGACCGAGGGGCCACGCCAGGAATATTCAGAA
AATAATGAGAACTACATTGAAGTGCCATTGATTTTTGATCCTGTCACAAGAGAGGATTTG
CACATGGATTTTAAATGTGTTGTCCATAATACCCTGAGTTTTCAGACACTACGCACCACA
GTCAAGGAAGCCTCCTCCACGTTCTCCTGGGGCATTGTGCTGGCCCCACTTTCACTGGCC
TTCTTGGTTTTGGGGGGAATATGGATGCACAGACGGTGCAAACACAGAACTGGAAAAGCA
GATGGTCTGACTGTGCTATGGCCTCATCATCAAGACTTTCAATCCTATCCCAAGTGA
Chromosome Location
2
Locus
2q11.2
External Identifiers
ResourceLink
UniProtKB IDP27930
UniProtKB Entry NameIL1R2_HUMAN
HGNC IDHGNC:5994
General References
  1. McMahan CJ, Slack JL, Mosley B, Cosman D, Lupton SD, Brunton LL, Grubin CE, Wignall JM, Jenkins NA, Brannan CI, et al.: A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types. EMBO J. 1991 Oct;10(10):2821-32. [Article]
  2. Liu C, Hart RP, Liu XJ, Clevenger W, Maki RA, De Souza EB: Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA. J Biol Chem. 1996 Aug 23;271(34):20965-72. [Article]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, 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 EA, 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 SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Giri JG, Wells J, Dower SK, McCall CE, Guzman RN, Slack J, Bird TA, Shanebeck K, Grabstein KH, Sims JE, et al.: Elevated levels of shed type II IL-1 receptor in sepsis. Potential role for type II receptor in regulation of IL-1 responses. J Immunol. 1994 Dec 15;153(12):5802-9. [Article]
  6. Symons JA, Young PR, Duff GW: 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. Proc Natl Acad Sci U S A. 1995 Feb 28;92(5):1714-8. [Article]
  7. Orlando S, Sironi M, Bianchi G, Drummond AH, Boraschi D, Yabes D, Mantovani A: Role of metalloproteases in the release of the IL-1 type II decoy receptor. J Biol Chem. 1997 Dec 12;272(50):31764-9. [Article]
  8. Lang D, Knop J, Wesche H, Raffetseder U, Kurrle R, Boraschi D, Martin MU: The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: a novel mechanism of regulation of IL-1 responsiveness. J Immunol. 1998 Dec 15;161(12):6871-7. [Article]
  9. Neumann D, Kollewe C, Martin MU, Boraschi D: The membrane form of the type II IL-1 receptor accounts for inhibitory function. J Immunol. 2000 Sep 15;165(6):3350-7. [Article]
  10. Smith DE, Hanna R, Della Friend, Moore H, Chen H, Farese AM, MacVittie TJ, Virca GD, Sims JE: The soluble form of IL-1 receptor accessory protein enhances the ability of soluble type II IL-1 receptor to inhibit IL-1 action. Immunity. 2003 Jan;18(1):87-96. [Article]
  11. Wang D, Zhang S, Li L, Liu X, Mei K, Wang X: Structural insights into the assembly and activation of IL-1beta with its receptors. Nat Immunol. 2010 Oct;11(10):905-11. doi: 10.1038/ni.1925. Epub 2010 Aug 29. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails