I36RA_HUMAN
ID I36RA_HUMAN Reviewed; 155 AA.
AC Q9UBH0; A8K2I4; Q56AT9; Q7RTZ6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Interleukin-36 receptor antagonist protein;
DE Short=IL-36Ra {ECO:0000303|PubMed:21965679};
DE AltName: Full=FIL1 delta;
DE AltName: Full=IL-1-related protein 3;
DE Short=IL-1RP3;
DE AltName: Full=Interleukin-1 HY1;
DE Short=IL-1HY1;
DE AltName: Full=Interleukin-1 delta;
DE Short=IL-1 delta;
DE AltName: Full=Interleukin-1 family member 5;
DE Short=IL-1F5;
DE AltName: Full=Interleukin-1 receptor antagonist homolog 1;
DE Short=IL-1ra homolog 1;
DE AltName: Full=Interleukin-1-like protein 1;
DE Short=IL-1L1;
GN Name=IL36RN {ECO:0000312|HGNC:HGNC:15561};
GN Synonyms=FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3; ORFNames=UNQ1896/PRO4342;
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].
RC TISSUE=Placenta;
RX PubMed=10625660; DOI=10.1074/jbc.275.2.1169;
RA Smith D.E., Renshaw B.R., Ketchem R.R., Kubin M., Garka K.E., Sims J.E.;
RT "Four new members expand the IL-1 superfamily.";
RL J. Biol. Chem. 275:1169-1175(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal skin;
RX PubMed=10512743; DOI=10.1006/bbrc.1999.1440;
RA Mulero J.J., Pace A.M., Nelken S.T., Loeb D.B., Correa T.R., Drmanac R.,
RA Ford J.E.;
RT "IL1HY1: a novel interleukin-1 receptor antagonist gene.";
RL Biochem. Biophys. Res. Commun. 263:702-706(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=11093146;
RX DOI=10.1002/1521-4141(200011)30:11<3299::aid-immu3299>3.0.co;2-s;
RA Barton J.L., Herbst R., Bosisio D., Higgins L., Nicklin M.J.H.;
RT "A tissue specific IL-1 receptor antagonist homolog from the IL-1 cluster
RT lacks IL-1, IL-1ra, IL-18 and IL-18 antagonist activities.";
RL Eur. J. Immunol. 30:3299-3308(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11466363; DOI=10.4049/jimmunol.167.3.1440;
RA Debets R., Timans J.C., Homey B., Zurawski S., Sana T.R., Lo S., Wagner J.,
RA Edwards G., Clifford T., Menon S., Bazan J.F., Kastelein R.A.;
RT "Two novel IL-1 family members, IL-1 delta and IL-1 epsilon, function as an
RT antagonist and agonist of NF-kappa B activation through the orphan IL-1
RT receptor-related protein 2.";
RL J. Immunol. 167:1440-1446(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10860666; DOI=10.1006/geno.2000.6184;
RA Busfield S.J., Comrack C.A., Yu G., Chickering T.W., Smutko J.S., Zhou H.,
RA Leiby K.R., Holmgren L.M., Gearing D.P., Pan Y.;
RT "Identification and gene organization of three novel members of the IL-1
RT family on human chromosome 2.";
RL Genomics 66:213-216(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-47.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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].
RC TISSUE=Placenta;
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 FUNCTION, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=21965679; DOI=10.1074/jbc.m111.267922;
RA Towne J.E., Renshaw B.R., Douangpanya J., Lipsky B.P., Shen M., Gabel C.A.,
RA Sims J.E.;
RT "Interleukin-36 (IL-36) ligands require processing for full agonist (IL-
RT 36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra) activity.";
RL J. Biol. Chem. 286:42594-42602(2011).
RN [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=23147407; DOI=10.1002/eji.201242711;
RA Gresnigt M.S., Roesler B., Jacobs C.W., Becker K.L., Joosten L.A.,
RA van der Meer J.W., Netea M.G., Dinarello C.A., van de Veerdonk F.L.;
RT "The IL-36 receptor pathway regulates Aspergillus fumigatus-induced Th1 and
RT Th17 responses.";
RL Eur. J. Immunol. 43:416-426(2013).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [16]
RP VARIANTS PSORS14 TRP-48 AND LEU-113.
RX PubMed=21839423; DOI=10.1016/j.ajhg.2011.07.022;
RA Onoufriadis A., Simpson M.A., Pink A.E., Di Meglio P., Smith C.H.,
RA Pullabhatla V., Knight J., Spain S.L., Nestle F.O., Burden A.D., Capon F.,
RA Trembath R.C., Barker J.N.;
RT "Mutations in IL36RN/IL1F5 are associated with the severe episodic
RT inflammatory skin disease known as generalized pustular psoriasis.";
RL Am. J. Hum. Genet. 89:432-437(2011).
RN [17]
RP VARIANT PSORS14 PRO-27, AND CHARACTERIZATION OF VARIANT PSORS14 PRO-27.
RX PubMed=21848462; DOI=10.1056/nejmoa1013068;
RA Marrakchi S., Guigue P., Renshaw B.R., Puel A., Pei X.Y., Fraitag S.,
RA Zribi J., Bal E., Cluzeau C., Chrabieh M., Towne J.E., Douangpanya J.,
RA Pons C., Mansour S., Serre V., Makni H., Mahfoudh N., Fakhfakh F.,
RA Bodemer C., Feingold J., Hadj-Rabia S., Favre M., Genin E., Sahbatou M.,
RA Munnich A., Casanova J.L., Sims J.E., Turki H., Bachelez H., Smahi A.;
RT "Interleukin-36-receptor antagonist deficiency and generalized pustular
RT psoriasis.";
RL N. Engl. J. Med. 365:620-628(2011).
RN [18]
RP VARIANT PSORS14 ARG-123, AND CHARACTERIZATION OF VARIANT PSORS14 ARG-123.
RX PubMed=22903787; DOI=10.1002/humu.22203;
RA Farooq M., Nakai H., Fujimoto A., Fujikawa H., Matsuyama A., Kariya N.,
RA Aizawa A., Fujiwara H., Ito M., Shimomura Y.;
RT "Mutation analysis of the IL36RN gene in 14 Japanese patients with
RT generalized pustular psoriasis.";
RL Hum. Mutat. 34:176-183(2013).
CC -!- FUNCTION: Inhibits the activity of interleukin-36 (IL36A,IL36B and
CC IL36G) by binding to receptor IL1RL2 and preventing its association
CC with the coreceptor IL1RAP for signaling. Part of the IL-36 signaling
CC system that is thought to be present in epithelial barriers and to take
CC part in local inflammatory response; similar to the IL-1 system with
CC which it shares the coreceptor. Proposed to play a role in skin
CC inflammation. May be involved in the innate immune response to fungal
CC pathogens, such as Aspergillus fumigatus. May activate an anti-
CC inflammatory signaling pathway by recruiting SIGIRR.
CC {ECO:0000269|PubMed:11466363, ECO:0000269|PubMed:21965679,
CC ECO:0000269|PubMed:23147407}.
CC -!- SUBUNIT: Interacts with cargo receptor TMED10; the interaction mediates
CC the translocation from the cytoplasm into the ERGIC (endoplasmic
CC reticulum-Golgi intermediate compartment) and thereby secretion.
CC {ECO:0000269|PubMed:32272059}.
CC -!- INTERACTION:
CC Q9UBH0; O95994: AGR2; NbExp=3; IntAct=EBI-465156, EBI-712648;
CC Q9UBH0; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-465156, EBI-2371151;
CC Q9UBH0; O95628-2: CNOT4; NbExp=5; IntAct=EBI-465156, EBI-12019444;
CC Q9UBH0; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-465156, EBI-11982645;
CC Q9UBH0; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-465156, EBI-742054;
CC Q9UBH0; P84074: HPCA; NbExp=3; IntAct=EBI-465156, EBI-12197079;
CC Q9UBH0; Q0VD86: INCA1; NbExp=3; IntAct=EBI-465156, EBI-6509505;
CC Q9UBH0; Q9NWZ3: IRAK4; NbExp=3; IntAct=EBI-465156, EBI-448378;
CC Q9UBH0; Q04864: REL; NbExp=3; IntAct=EBI-465156, EBI-307352;
CC Q9UBH0; Q04864-2: REL; NbExp=3; IntAct=EBI-465156, EBI-10829018;
CC Q9UBH0; O14492-2: SH2B2; NbExp=3; IntAct=EBI-465156, EBI-19952306;
CC Q9UBH0; Q9BWW4: SSBP3; NbExp=8; IntAct=EBI-465156, EBI-2902395;
CC Q9UBH0; Q9BWG4: SSBP4; NbExp=4; IntAct=EBI-465156, EBI-744719;
CC Q9UBH0; Q8N7F7: UBL4B; NbExp=3; IntAct=EBI-465156, EBI-10267507;
CC Q9UBH0; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-465156, EBI-2818641;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted
CC {ECO:0000269|PubMed:32272059}. Note=The secretion is dependent on
CC protein unfolding and facilitated by the cargo receptor TMED10; it
CC results in protein translocation from the cytoplasm into the ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) followed by
CC vesicle entry and secretion. {ECO:0000269|PubMed:32272059}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skin keratinocytes but
CC not in fibroblasts, endothelial cells or melanocytes. Detected also in
CC the spleen, brain leukocyte and macrophage cell types. Increased in
CC lesional psoriasis skin. {ECO:0000269|PubMed:11466363}.
CC -!- INDUCTION: By phorbol ester (PMA) and bacterial lipopolysaccharides
CC (LPS) treatment in macrophage cell line. By Aspergillus fumigatus
CC conidia in peripheral blood mnonocytes. {ECO:0000269|PubMed:23147407}.
CC -!- DISEASE: Psoriasis 14, pustular (PSORS14) [MIM:614204]: A life-
CC threatening disease defined by repeated flares of sudden onset
CC consisting of diffuse erythematous skin eruption characterized by rapid
CC coverage with pustules, high-grade fever, asthenia, marked
CC leukocytosis, and elevated serum levels of C-reactive protein.
CC {ECO:0000269|PubMed:21839423, ECO:0000269|PubMed:21848462,
CC ECO:0000269|PubMed:22903787}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
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/il1f5/";
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DR EMBL; AF201830; AAF25210.1; -; mRNA.
DR EMBL; AF186094; AAF02757.1; -; mRNA.
DR EMBL; AJ242737; CAB59822.1; -; mRNA.
DR EMBL; AJ242738; CAB59823.1; -; mRNA.
DR EMBL; AJ271338; CAB67704.1; -; Genomic_DNA.
DR EMBL; AF216693; AAF76981.1; -; Genomic_DNA.
DR EMBL; AF230377; AAF91274.1; -; mRNA.
DR EMBL; BN000002; CAD29877.1; -; Genomic_DNA.
DR EMBL; AY359117; AAQ89475.1; -; mRNA.
DR EMBL; AK290249; BAF82938.1; -; mRNA.
DR EMBL; AY972853; AAX59031.1; -; Genomic_DNA.
DR EMBL; AC016724; AAY14990.1; -; Genomic_DNA.
DR EMBL; CH471217; EAW73617.1; -; Genomic_DNA.
DR EMBL; BC024747; AAH24747.1; -; mRNA.
DR CCDS; CCDS2111.1; -.
DR PIR; JC7104; JC7104.
DR RefSeq; NP_036407.1; NM_012275.2.
DR RefSeq; NP_775262.1; NM_173170.1.
DR PDB; 4P0J; X-ray; 2.30 A; A/B=2-135, A/B=147-155.
DR PDB; 4P0K; X-ray; 1.70 A; A=2-49, A=55-135, A=147-155.
DR PDB; 4P0L; X-ray; 1.55 A; A=2-49, A=55-135, A=147-155.
DR PDBsum; 4P0J; -.
DR PDBsum; 4P0K; -.
DR PDBsum; 4P0L; -.
DR AlphaFoldDB; Q9UBH0; -.
DR SMR; Q9UBH0; -.
DR BioGRID; 117728; 54.
DR IntAct; Q9UBH0; 26.
DR MINT; Q9UBH0; -.
DR STRING; 9606.ENSP00000376896; -.
DR iPTMnet; Q9UBH0; -.
DR PhosphoSitePlus; Q9UBH0; -.
DR BioMuta; IL36RN; -.
DR DMDM; 25008600; -.
DR MassIVE; Q9UBH0; -.
DR PaxDb; Q9UBH0; -.
DR PeptideAtlas; Q9UBH0; -.
DR PRIDE; Q9UBH0; -.
DR ProteomicsDB; 83968; -.
DR Antibodypedia; 35211; 289 antibodies from 32 providers.
DR DNASU; 26525; -.
DR Ensembl; ENST00000346807.7; ENSP00000259212.3; ENSG00000136695.15.
DR Ensembl; ENST00000393200.7; ENSP00000376896.2; ENSG00000136695.15.
DR GeneID; 26525; -.
DR KEGG; hsa:26525; -.
DR MANE-Select; ENST00000393200.7; ENSP00000376896.2; NM_012275.3; NP_036407.1.
DR UCSC; uc002tis.4; human.
DR CTD; 26525; -.
DR DisGeNET; 26525; -.
DR GeneCards; IL36RN; -.
DR HGNC; HGNC:15561; IL36RN.
DR HPA; ENSG00000136695; Group enriched (esophagus, lymphoid tissue, skin).
DR MalaCards; IL36RN; -.
DR MIM; 605507; gene.
DR MIM; 614204; phenotype.
DR neXtProt; NX_Q9UBH0; -.
DR OpenTargets; ENSG00000136695; -.
DR Orphanet; 163931; Acrodermatitis continua of Hallopeau.
DR Orphanet; 404546; DITRA.
DR Orphanet; 247353; Generalized pustular psoriasis.
DR Orphanet; 163927; Pustulosis palmaris et plantaris.
DR PharmGKB; PA38388; -.
DR VEuPathDB; HostDB:ENSG00000136695; -.
DR eggNOG; ENOG502SRSC; Eukaryota.
DR GeneTree; ENSGT00950000182943; -.
DR HOGENOM; CLU_095373_2_1_1; -.
DR InParanoid; Q9UBH0; -.
DR OMA; NRWLDAR; -.
DR OrthoDB; 1410755at2759; -.
DR PhylomeDB; Q9UBH0; -.
DR TreeFam; TF300203; -.
DR PathwayCommons; Q9UBH0; -.
DR Reactome; R-HSA-9014826; Interleukin-36 pathway.
DR SignaLink; Q9UBH0; -.
DR BioGRID-ORCS; 26525; 13 hits in 1064 CRISPR screens.
DR ChiTaRS; IL36RN; human.
DR GeneWiki; IL1F5; -.
DR GenomeRNAi; 26525; -.
DR Pharos; Q9UBH0; Tbio.
DR PRO; PR:Q9UBH0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UBH0; protein.
DR Bgee; ENSG00000136695; Expressed in amniotic fluid and 85 other tissues.
DR ExpressionAtlas; Q9UBH0; baseline and differential.
DR Genevisible; Q9UBH0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005152; F:interleukin-1 receptor antagonist activity; TAS:ProtInc.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IEA:InterPro.
DR GO; GO:0019732; P:antifungal humoral response; IMP:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IMP:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR InterPro; IPR020877; IL-1_CS.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR003297; IL-1RA/IL-36.
DR InterPro; IPR027171; IL-36RA.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR10078; PTHR10078; 1.
DR PANTHER; PTHR10078:SF32; PTHR10078:SF32; 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; Cytokine; Cytoplasm; Disease variant; Disulfide bond;
KW Immunity; Innate immunity; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:21965679"
FT CHAIN 2..155
FT /note="Interleukin-36 receptor antagonist protein"
FT /id="PRO_0000153642"
FT DISULFID 8..154
FT /evidence="ECO:0000250"
FT VARIANT 27
FT /note="L -> P (in PSORS14; expression of the protein is
FT severely impaired compared to wild-type; the mutant protein
FT is substantially less able to inhibit IL1RL2 signaling than
FT wild-type; dbSNP:rs387906914)"
FT /evidence="ECO:0000269|PubMed:21848462"
FT /id="VAR_066646"
FT VARIANT 47
FT /note="N -> S (in dbSNP:rs28938777)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_023239"
FT VARIANT 48
FT /note="R -> W (in PSORS14; dbSNP:rs151325121)"
FT /evidence="ECO:0000269|PubMed:21839423"
FT /id="VAR_066647"
FT VARIANT 113
FT /note="S -> L (in PSORS14; dbSNP:rs144478519)"
FT /evidence="ECO:0000269|PubMed:21839423"
FT /id="VAR_066648"
FT VARIANT 123
FT /note="T -> R (in PSORS14; shows impaired expression of the
FT mutant protein which fails to antagonize the IL-36
FT signaling pathway; dbSNP:rs397514629)"
FT /evidence="ECO:0000269|PubMed:22903787"
FT /id="VAR_068972"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4P0L"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4P0J"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:4P0L"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4P0L"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:4P0L"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4P0L"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4P0L"
SQ SEQUENCE 155 AA; 16962 MW; B96DB5EFA2612E25 CRC64;
MVLSGALCFR MKDSALKVLY LHNNQLLAGG LHAGKVIKGE EISVVPNRWL DASLSPVILG
VQGGSQCLSC GVGQEPTLTL EPVNIMELYL GAKESKSFTF YRRDMGLTSS FESAAYPGWF
LCTVPEADQP VRLTQLPENG GWNAPITDFY FQQCD
