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Database: UniProt
Entry: P18510
LinkDB: P18510
Original site: P18510 
ID   IL1RA_HUMAN             Reviewed;         177 AA.
AC   P18510; A8K4G1; Q14628; Q53SC2; Q7RTZ4; Q96GD6; Q9UPC0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-JUN-2021, entry version 223.
DE   RecName: Full=Interleukin-1 receptor antagonist protein;
DE            Short=IL-1RN;
DE            Short=IL-1ra;
DE            Short=IRAP;
DE   AltName: Full=ICIL-1RA;
DE   AltName: Full=IL1 inhibitor;
DE   AltName: INN=Anakinra;
DE   Flags: Precursor;
GN   Name=IL1RN; Synonyms=IL1F3, IL1RA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2139180; DOI=10.1038/344633a0;
RA   Carter D.B., Deibel M.R. Jr., Dunn C.J., Tomich C.S.C., Laborde A.L.,
RA   Slightom J.L., Berger A.E., Bienkowski M.J., Sun F.F., McEwan R.N.,
RA   Harris P.K.W., Yem A.W., Waszak G.A., Chosay J.G., Sieu L.C., Hardee M.M.,
RA   Zurcher-Neely H.A., Reardon I.M., Heinrikson R.L., Truesdell S.E.,
RA   Shelly J.A., Eessalu T.E., Taylor B.M., Tracey D.E.;
RT   "Purification, cloning, expression and biological characterization of an
RT   interleukin-1 receptor antagonist protein.";
RL   Nature 344:633-638(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2137201; DOI=10.1038/343341a0;
RA   Eisenberg S.P., Evans R.J., Arend W.P., Verderber E., Brewer M.T.,
RA   Hannum C.H., Thompson R.C.;
RT   "Primary structure and functional expression from complementary DNA of a
RT   human interleukin-1 receptor antagonist.";
RL   Nature 343:341-346(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=1828896; DOI=10.1073/pnas.88.12.5232;
RA   Eisenberg S.P., Brewer M.T., Verderber E., Heimdal P., Brandhuber B.J.,
RA   Thompson R.C.;
RT   "Interleukin 1 receptor antagonist is a member of the interleukin 1 gene
RT   family: evolution of a cytokine control mechanism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5232-5236(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=1385987; DOI=10.1016/1043-4666(92)90041-o;
RA   Lennard A., Gorman P., Carrier M., Griffiths S., Scotney H., Sheer D.,
RA   Solari R.;
RT   "Cloning and chromosome mapping of the human interleukin-1 receptor
RT   antagonist gene.";
RL   Cytokine 4:83-89(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
RX   PubMed=8992991;
RA   Jenkins J.K., Drong R.F., Shuck M.E., Bienkowski M.J., Slightom J.L.,
RA   Arend W.P., Smith M.F. Jr.;
RT   "Intracellular IL-1 receptor antagonist promoter: cell type-specific and
RT   inducible regulatory regions.";
RL   J. Immunol. 158:748-755(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=1827201; DOI=10.1073/pnas.88.9.3681;
RA   Haskill S., Martin G., van Le L., Morris J., Peace A., Bigler C.F.,
RA   Jaffe G.J., Hammerberg C., Sporn S.A., Fong S., Arend W.P., Ralph P.;
RT   "cDNA cloning of an intracellular form of the human interleukin 1 receptor
RT   antagonist associated with epithelium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:3681-3685(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=7629520; DOI=10.1084/jem.182.2.623;
RA   Muzio M., Polentarutti N., Sironi M., Poli G., De Gioia L., Introna M.,
RA   Mantovani A., Colotta F.;
RT   "Cloning and characterization of a new isoform of the interleukin 1
RT   receptor antagonist.";
RL   J. Exp. Med. 182:623-628(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Esophagus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   PROTEIN SEQUENCE OF 26-45, AND GLYCOSYLATION AT ASN-109.
RX   PubMed=2137200; DOI=10.1038/343336a0;
RA   Hannum C.H., Wilcox C.J., Arend W.P., Joslin F.G., Dripps D.J.,
RA   Heimdal P.L., Armes L.G., Sommer A., Eisenberg S.P., Thompson R.C.;
RT   "Interleukin-1 receptor antagonist activity of a human interleukin-1
RT   inhibitor.";
RL   Nature 343:336-340(1990).
RN   [14]
RP   PROTEIN SEQUENCE OF 26-52.
RX   PubMed=2143761;
RA   Bienkowski M.J., Eessalu T.E., Berger A.E., Truesdell S.E., Shelly J.A.,
RA   Laborde A.L., Zurcher-Neely H.A., Reardon I.M., Heinrikson R.L.,
RA   Chosay J.G., Tracey D.E.;
RT   "Purification and characterization of interleukin 1 receptor level
RT   antagonist proteins from THP-1 cells.";
RL   J. Biol. Chem. 265:14505-14511(1990).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 35-177 (ISOFORM 4).
RX   PubMed=9514884; DOI=10.1006/bbrc.1998.8217;
RA   Weissbach L., Tran K., Colquhoun S.A., Champliaud M.-F., Towle C.A.;
RT   "Detection of an interleukin-1 intracellular receptor antagonist mRNA
RT   variant.";
RL   Biochem. Biophys. Res. Commun. 244:91-95(1998).
RN   [16]
RP   RECEPTOR-BINDING.
RX   PubMed=7989776;
RA   Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
RA   Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
RT   "Elevated levels of shed type II IL-1 receptor in sepsis. Potential role
RT   for type II receptor in regulation of IL-1 responses.";
RL   J. Immunol. 153:5802-5809(1994).
RN   [17]
RP   FUNCTION.
RX   PubMed=7775431; DOI=10.1074/jbc.270.23.13757;
RA   Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.;
RT   "Molecular cloning and characterization of a second subunit of the
RT   interleukin 1 receptor complex.";
RL   J. Biol. Chem. 270:13757-13765(1995).
RN   [18]
RP   IDENTIFICATION (ISOFORM 2).
RX   PubMed=11991722; DOI=10.1006/geno.2002.6751;
RA   Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G.,
RA   Kornman K.;
RT   "A sequence-based map of the nine genes of the human interleukin-1
RT   cluster.";
RL   Genomics 79:718-725(2002).
RN   [19]
RP   INVOLVEMENT IN MVCD4.
RX   PubMed=8786086; DOI=10.1007/bf02185776;
RA   Blakemore A.I.F., Cox A., Gonzalez A.-M., Maskil J.K., Hughes M.E.,
RA   Wilson R.M., Ward J.D., Duff G.W.;
RT   "Interleukin-1 receptor antagonist allele (IL1RN*2) associated with
RT   nephropathy in diabetes mellitus.";
RL   Hum. Genet. 97:369-374(1996).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [21]
RP   INVOLVEMENT IN DIRA.
RX   PubMed=19494218; DOI=10.1056/nejmoa0807865;
RA   Aksentijevich I., Masters S.L., Ferguson P.J., Dancey P., Frenkel J.,
RA   van Royen-Kerkhoff A., Laxer R., Tedgard U., Cowen E.W., Pham T.H.,
RA   Booty M., Estes J.D., Sandler N.G., Plass N., Stone D.L., Turner M.L.,
RA   Hill S., Butman J.A., Schneider R., Babyn P., El-Shanti H.I., Pope E.,
RA   Barron K., Bing X., Laurence A., Lee C.C., Chapelle D., Clarke G.I.,
RA   Ohson K., Nicholson M., Gadina M., Yang B., Korman B.D., Gregersen P.K.,
RA   van Hagen P.M., Hak A.E., Huizing M., Rahman P., Douek D.C., Remmers E.F.,
RA   Kastner D.L., Goldbach-Mansky R.;
RT   "An autoinflammatory disease with deficiency of the interleukin-1-receptor
RT   antagonist.";
RL   N. Engl. J. Med. 360:2426-2437(2009).
RN   [22]
RP   STRUCTURE BY NMR.
RX   PubMed=1534997; DOI=10.1021/bi00138a001;
RA   Stockman B.J., Scahill T.A., Roy M., Ulrich E.L., Strakalaitis N.A.,
RA   Brunner D.P., Yem A.W., Deibel M.R. Jr.;
RT   "Secondary structure and topology of interleukin-1 receptor antagonist
RT   protein determined by heteronuclear three-dimensional NMR spectroscopy.";
RL   Biochemistry 31:5237-5244(1992).
RN   [23]
RP   STRUCTURE BY NMR.
RX   PubMed=8045306; DOI=10.1016/0014-5793(94)00643-1;
RA   Stockman B.J., Scahill T.A., Strakalaitis N.A., Brunner D.P., Yem A.W.,
RA   Deibel M.R. Jr.;
RT   "Solution structure of human interleukin-1 receptor antagonist protein.";
RL   FEBS Lett. 349:79-83(1994).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8175703;
RA   Vigers G.P.A., Caffes P., Evans R.J., Thompson R.C., Eisenberg S.P.,
RA   Brandhuber B.J.;
RT   "X-ray structure of interleukin-1 receptor antagonist at 2.0-A
RT   resolution.";
RL   J. Biol. Chem. 269:12874-12879(1994).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=7867645; DOI=10.1111/j.1432-1033.1995.tb20209.x;
RA   Schreuder H.A., Rondeau J.-M., Tardif C., Soffientini A., Sarubbi E.,
RA   Akeson A., Bowlin T.L., Yanofsky S., Barrett R.W.;
RT   "Refined crystal structure of the interleukin-1 receptor antagonist.
RT   Presence of a disulfide link and a cis-proline.";
RL   Eur. J. Biochem. 227:838-847(1995).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 32-177 IN COMPLEX WITH IL1R.
RX   PubMed=9062194; DOI=10.1038/386194a0;
RA   Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E.,
RA   Akeson A., Bowlin T., Yanofsky S., Barrett R.W.;
RT   "A new cytokine-receptor binding mode revealed by the crystal structure of
RT   the IL-1 receptor with an antagonist.";
RL   Nature 386:194-200(1997).
RN   [27]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-124.
RX   PubMed=18987736; DOI=10.1038/nature07485;
RA   Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA   Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA   Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA   Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA   Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA   Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA   Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA   Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA   DiPersio J.F., Wilson R.K.;
RT   "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT   genome.";
RL   Nature 456:66-72(2008).
CC   -!- FUNCTION: Inhibits the activity of interleukin-1 by binding to receptor
CC       IL1R1 and preventing its association with the coreceptor IL1RAP for
CC       signaling. Has no interleukin-1 like activity. Binds functional
CC       interleukin-1 receptor IL1R1 with greater affinity than decoy receptor
CC       IL1R2; however, the physiological relevance of the latter association
CC       is unsure. {ECO:0000269|PubMed:7775431}.
CC   -!- INTERACTION:
CC       P18510; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1026330, EBI-750109;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P18510-1; Sequence=Displayed;
CC       Name=2; Synonyms=icIL-1ra;
CC         IsoId=P18510-2; Sequence=VSP_002649;
CC       Name=3; Synonyms=icIL-1ra type II;
CC         IsoId=P18510-3; Sequence=VSP_002650;
CC       Name=4;
CC         IsoId=P18510-4; Sequence=VSP_002651;
CC   -!- TISSUE SPECIFICITY: The intracellular form of IL1RN is predominantly
CC       expressed in epithelial cells.
CC   -!- DISEASE: Microvascular complications of diabetes 4 (MVCD4)
CC       [MIM:612628]: Pathological conditions that develop in numerous tissues
CC       and organs as a consequence of diabetes mellitus. They include diabetic
CC       retinopathy, diabetic nephropathy leading to end-stage renal disease,
CC       and diabetic neuropathy. Diabetic retinopathy remains the major cause
CC       of new-onset blindness among diabetic adults. It is characterized by
CC       vascular permeability and increased tissue ischemia and angiogenesis.
CC       {ECO:0000269|PubMed:8786086}. Note=Disease susceptibility is associated
CC       with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Interleukin 1 receptor antagonist deficiency (DIRA)
CC       [MIM:612852]: A rare autoinflammatory disease of skin and bone
CC       resulting in sterile multifocal osteomyelitis, periostitis, and
CC       pustulosis from birth. The term autoinflammatory disease describes a
CC       group of disorders characterized by attacks of seemingly unprovoked
CC       inflammation without significant levels of autoantibodies and
CC       autoreactive T-cells. {ECO:0000269|PubMed:19494218}. Note=The disease
CC       is caused by variants affecting the gene represented in this entry.
CC   -!- PHARMACEUTICAL: Available under the name Kineret (Amgen). Used for the
CC       reduction in signs and symptoms and slowing the progression of
CC       structural damage in moderately to severely active rheumatoid
CC       arthritis.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
CC       URL="https://en.wikipedia.org/wiki/Interleukin_1";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/il1rn/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL1RN";
CC   -!- WEB RESOURCE: Name=Kineret professional medical information;
CC       URL="https://www.rxlist.com/kineret-drug.htm";
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DR   EMBL; X53296; CAA37386.1; -; mRNA.
DR   EMBL; X52015; CAA36262.1; -; mRNA.
DR   EMBL; M63099; AAB41943.1; -; Genomic_DNA.
DR   EMBL; X64532; CAA45832.1; -; Genomic_DNA.
DR   EMBL; U65590; AAB92270.1; -; Genomic_DNA.
DR   EMBL; U65590; AAB92268.1; -; Genomic_DNA.
DR   EMBL; U65590; AAB92269.1; -; Genomic_DNA.
DR   EMBL; M55646; AAA59138.1; -; mRNA.
DR   EMBL; X84348; CAA59087.1; -; mRNA.
DR   EMBL; AY196903; AAN87150.1; -; Genomic_DNA.
DR   EMBL; AK290898; BAF83587.1; -; mRNA.
DR   EMBL; AK290926; BAF83615.1; -; mRNA.
DR   EMBL; AC024704; AAX93278.1; -; Genomic_DNA.
DR   EMBL; CH471217; EAW73625.1; -; Genomic_DNA.
DR   EMBL; BC009745; AAH09745.1; -; mRNA.
DR   EMBL; AF043143; AAC39672.1; -; mRNA.
DR   EMBL; BN000002; CAD29879.1; -; Genomic_DNA.
DR   CCDS; CCDS2113.1; -. [P18510-2]
DR   CCDS; CCDS2114.1; -. [P18510-3]
DR   CCDS; CCDS2115.1; -. [P18510-4]
DR   CCDS; CCDS46396.1; -. [P18510-1]
DR   PIR; A40956; A30368.
DR   PIR; I37893; A39386.
DR   RefSeq; NP_000568.1; NM_000577.4. [P18510-2]
DR   RefSeq; NP_001305843.1; NM_001318914.1. [P18510-4]
DR   RefSeq; NP_776213.1; NM_173841.2. [P18510-3]
DR   RefSeq; NP_776214.1; NM_173842.2. [P18510-1]
DR   RefSeq; NP_776215.1; NM_173843.2. [P18510-4]
DR   RefSeq; XP_005263718.1; XM_005263661.4.
DR   RefSeq; XP_011509423.1; XM_011511121.1. [P18510-4]
DR   PDB; 1ILR; X-ray; 2.10 A; 1/2=26-177.
DR   PDB; 1ILT; X-ray; 2.00 A; A/B=26-177.
DR   PDB; 1IRA; X-ray; 2.70 A; X=26-177.
DR   PDB; 1IRP; NMR; -; A=26-177.
DR   PDB; 1ITN; Model; -; A=31-177.
DR   PDB; 2IRT; X-ray; 3.20 A; A/B=26-177.
DR   PDBsum; 1ILR; -.
DR   PDBsum; 1ILT; -.
DR   PDBsum; 1IRA; -.
DR   PDBsum; 1IRP; -.
DR   PDBsum; 1ITN; -.
DR   PDBsum; 2IRT; -.
DR   SMR; P18510; -.
DR   BioGRID; 109772; 15.
DR   IntAct; P18510; 8.
DR   STRING; 9606.ENSP00000259206; -.
DR   BindingDB; P18510; -.
DR   ChEMBL; CHEMBL4523191; -.
DR   DrugBank; DB06372; Rilonacept.
DR   DrugCentral; P18510; -.
DR   Allergome; 11858; Hom s Anakinra.
DR   GlyConnect; 1947; 2 N-Linked glycans (1 site).
DR   GlyGen; P18510; 1 site.
DR   iPTMnet; P18510; -.
DR   PhosphoSitePlus; P18510; -.
DR   BioMuta; IL1RN; -.
DR   DMDM; 124312; -.
DR   jPOST; P18510; -.
DR   MassIVE; P18510; -.
DR   MaxQB; P18510; -.
DR   PaxDb; P18510; -.
DR   PeptideAtlas; P18510; -.
DR   PRIDE; P18510; -.
DR   ProteomicsDB; 53572; -. [P18510-1]
DR   ProteomicsDB; 53573; -. [P18510-2]
DR   ProteomicsDB; 53574; -. [P18510-3]
DR   ProteomicsDB; 53575; -. [P18510-4]
DR   Antibodypedia; 806; 867 antibodies.
DR   CPTC; P18510; 1 antibody.
DR   DNASU; 3557; -.
DR   Ensembl; ENST00000259206; ENSP00000259206; ENSG00000136689. [P18510-3]
DR   Ensembl; ENST00000354115; ENSP00000329072; ENSG00000136689. [P18510-2]
DR   Ensembl; ENST00000361779; ENSP00000354816; ENSG00000136689. [P18510-4]
DR   Ensembl; ENST00000409052; ENSP00000387210; ENSG00000136689. [P18510-4]
DR   Ensembl; ENST00000409930; ENSP00000387173; ENSG00000136689. [P18510-1]
DR   GeneID; 3557; -.
DR   KEGG; hsa:3557; -.
DR   UCSC; uc002tiy.3; human. [P18510-1]
DR   CTD; 3557; -.
DR   DisGeNET; 3557; -.
DR   GeneCards; IL1RN; -.
DR   HGNC; HGNC:6000; IL1RN.
DR   HPA; ENSG00000136689; Tissue enhanced (esophagus, lymphoid tissue, tongue).
DR   MalaCards; IL1RN; -.
DR   MIM; 147679; gene.
DR   MIM; 612628; phenotype.
DR   MIM; 612852; phenotype.
DR   neXtProt; NX_P18510; -.
DR   OpenTargets; ENSG00000136689; -.
DR   Orphanet; 210115; Sterile multifocal osteomyelitis with periostitis and pustulosis.
DR   PharmGKB; PA29816; -.
DR   VEuPathDB; HostDB:ENSG00000136689.18; -.
DR   eggNOG; ENOG502S5F0; Eukaryota.
DR   GeneTree; ENSGT00950000182943; -.
DR   HOGENOM; CLU_095373_2_0_1; -.
DR   InParanoid; P18510; -.
DR   OMA; WYLCTAL; -.
DR   OrthoDB; 1410755at2759; -.
DR   PhylomeDB; P18510; -.
DR   TreeFam; TF300203; -.
DR   PathwayCommons; P18510; -.
DR   Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR   Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR   SIGNOR; P18510; -.
DR   BioGRID-ORCS; 3557; 4 hits in 994 CRISPR screens.
DR   ChiTaRS; IL1RN; human.
DR   EvolutionaryTrace; P18510; -.
DR   GeneWiki; Interleukin_1_receptor_antagonist; -.
DR   GenomeRNAi; 3557; -.
DR   Pharos; P18510; Tchem.
DR   PRO; PR:P18510; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P18510; protein.
DR   Bgee; ENSG00000136689; Expressed in lower esophagus mucosa and 183 other tissues.
DR   ExpressionAtlas; P18510; baseline and differential.
DR   Genevisible; P18510; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005125; F:cytokine activity; IEA:InterPro.
DR   GO; GO:0005152; F:interleukin-1 receptor antagonist activity; IDA:BHF-UCL.
DR   GO; GO:0005149; F:interleukin-1 receptor binding; IDA:BHF-UCL.
DR   GO; GO:0045352; F:interleukin-1 type I receptor antagonist activity; IDA:BHF-UCL.
DR   GO; GO:0045353; F:interleukin-1 type II receptor antagonist activity; IDA:BHF-UCL.
DR   GO; GO:0005150; F:interleukin-1, type I receptor binding; IPI:BHF-UCL.
DR   GO; GO:0005151; F:interleukin-1, type II receptor binding; IPI:BHF-UCL.
DR   GO; GO:0006953; P:acute-phase response; IDA:BHF-UCL.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IBA:GO_Central.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
DR   InterPro; IPR020877; IL-1_CS.
DR   InterPro; IPR000975; IL-1_fam.
DR   InterPro; IPR003297; IL-1RA/IL-36.
DR   InterPro; IPR008996; IL1/FGF.
DR   InterPro; IPR039348; IL1RA.
DR   PANTHER; PTHR10078; PTHR10078; 1.
DR   PANTHER; PTHR10078:SF28; PTHR10078:SF28; 1.
DR   Pfam; PF00340; IL1; 1.
DR   PRINTS; PR00264; INTERLEUKIN1.
DR   PRINTS; PR01360; INTRLEUKIN1X.
DR   SUPFAM; SSF50353; SSF50353; 1.
DR   PROSITE; PS00253; INTERLEUKIN_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Pharmaceutical; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:2137200,
FT                   ECO:0000269|PubMed:2143761"
FT   CHAIN           26..177
FT                   /note="Interleukin-1 receptor antagonist protein"
FT                   /id="PRO_0000015328"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:2137200"
FT   DISULFID        91..141
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9514884"
FT                   /id="VSP_002651"
FT   VAR_SEQ         1..21
FT                   /note="MEICRGLRSHLITLLLFLFHS -> MAL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:1827201"
FT                   /id="VSP_002649"
FT   VAR_SEQ         1..21
FT                   /note="MEICRGLRSHLITLLLFLFHS -> MALADLYEEGGGGGGEGEDNADSK
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:7629520"
FT                   /id="VSP_002650"
FT   VARIANT         124
FT                   /note="A -> T (in dbSNP:rs45507693)"
FT                   /evidence="ECO:0000269|PubMed:18987736"
FT                   /id="VAR_049573"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:1IRP"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   HELIX           62..67
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   HELIX           118..123
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          133..141
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          145..151
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          162..168
FT                   /evidence="ECO:0007829|PDB:1ILR"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:1ILR"
SQ   SEQUENCE   177 AA;  20055 MW;  D1690776A7394057 CRC64;
     MEICRGLRSH LITLLLFLFH SETICRPSGR KSSKMQAFRI WDVNQKTFYL RNNQLVAGYL
     QGPNVNLEEK IDVVPIEPHA LFLGIHGGKM CLSCVKSGDE TRLQLEAVNI TDLSENRKQD
     KRFAFIRSDS GPTTSFESAA CPGWFLCTAM EADQPVSLTN MPDEGVMVTK FYFQEDE
//
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