P18510 (IL1RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-1 receptor antagonist protein
Short name=IL-1RN
Short name=IL-1ra
Short name=IRAP

Alternative name(s):
ICIL-1RA
IL1 inhibitor
INN=Anakinra

Gene names

Name:	IL1RN
Synonyms:	IL1F3, IL1RA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity. Binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unsure.
Subcellular location	Isoform 1: Secreted. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm.
Tissue specificity	The intracellular form of IL1RN is predominantly expressed in epithelial cells.
Involvement in disease	Genetic variation in IL1RN is associated with susceptibility to microvascular complications of diabetes type 4 (MVCD4) [MIM:612628]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in IL1RN are the cause of interleukin 1 receptor antagonist deficiency (DIRA) [MIM:612852]; also known as deficiency of interleukin 1 receptor antagonist. Autoinflammatory diseases manifest inflammation without evidence of infection, high-titer autoantibodies, or autoreactive T-cells. DIRA is a rare, autosomal recessive, genetic autoinflammatory disease that results in sterile multifocal osteomyelitis (bone inflammation in multiple places), periostitis (inflammation of the membrane surrounding the bones), and pustulosis (due to skin inflammation) from birth. Ref.20
Pharmaceutical use	Available under the name Kineret (Amgen). Used for the reduction in signs and symptoms and slowing the progression of structural damage in moderately to severely active rheumatoid arthritis.

Ontologies

Keywords
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological process	acute-phase response Inferred from direct assay. Source: BHF-UCL immune response Non-traceable author statement Ref.7. Source: UniProtKB negative regulation of heterotypic cell-cell adhesion Inferred from direct assay Ref.1. Source: BHF-UCL negative regulation of interleukin-1-mediated signaling pathway Inferred from direct assay Ref.1. Source: BHF-UCL response to glucocorticoid stimulus Inferred from direct assay. Source: BHF-UCL
Cellular component	centrosome Inferred from direct assay. Source: HPA extracellular space Inferred from direct assay Ref.12. Source: BHF-UCL nucleus Inferred from direct assay. Source: HPA plasma membrane Traceable author statement. Source: Reactome
Molecular function	interleukin-1 Type I receptor antagonist activity Inferred from direct assay. Source: BHF-UCL interleukin-1 Type II receptor antagonist activity Inferred from direct assay. Source: BHF-UCL interleukin-1 receptor antagonist activity Inferred from direct assay Ref.12Ref.1. Source: BHF-UCL interleukin-1 receptor binding Inferred from direct assay Ref.12. Source: BHF-UCL interleukin-1, Type I receptor binding Inferred from physical interaction. Source: BHF-UCL interleukin-1, Type II receptor binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P18510-1)

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 2 (identifier: P18510-2)

Also known as: icIL-1ra;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEICRGLRSHLITLLLFLFHS → MAL

Isoform 3 (identifier: P18510-3)

Also known as: icIL-1ra type II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEICRGLRSHLITLLLFLFHS → MALADLYEEGGGGGGEGEDNADSK

Isoform 4 (identifier: P18510-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.12 Ref.13

Chain

26 – 177

152

Interleukin-1 receptor antagonist protein Ref.1

PRO_0000015328

Amino acid modifications

Glycosylation

109

1

N-linked (GlcNAc...) Ref.12 Ref.19

Disulfide bond

91 ↔ 141

Natural variations

Alternative sequence

1 – 34

34

Missing in isoform 4.

VSP_002651

Alternative sequence

1 – 21

21

MEICR…FLFHS → MAL in isoform 2.

VSP_002649

Alternative sequence

1 – 21

21

MEICR…FLFHS → MALADLYEEGGGGGGEGEDN ADSK in isoform 3.

VSP_002650

Natural variant

124

1

A → T. Ref.26
Corresponds to variant rs45507693 [ dbSNP | Ensembl ].

VAR_049573

Secondary structure

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177

Helix Strand Turn

Details...

Beta strand

36 – 42

7

Beta strand

47 – 51

5

Beta strand

54 – 58

5

Helix

62 – 67

6

Beta strand

71 – 76

6

Turn

77 – 79

3

Beta strand

80 – 85

6

Turn

86 – 89

4

Beta strand

90 – 97

8

Beta strand

100 – 106

7

Helix

110 – 112

3

Helix

118 – 123

6

Beta strand

124 – 130

7

Beta strand

133 – 141

9

Beta strand

145 – 151

7

Beta strand

157 – 160

4

Beta strand

162 – 168

7

Beta strand

171 – 175

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: D1690776A7394057	FASTA	177	20,055
	10 20 30 40 50 60 MEICRGLRSH LITLLLFLFH SETICRPSGR KSSKMQAFRI WDVNQKTFYL RNNQLVAGYL 70 80 90 100 110 120 QGPNVNLEEK IDVVPIEPHA LFLGIHGGKM CLSCVKSGDE TRLQLEAVNI TDLSENRKQD 130 140 150 160 170 KRFAFIRSDS GPTTSFESAA CPGWFLCTAM EADQPVSLTN MPDEGVMVTK FYFQEDE
	Isoform 2 (icIL-1ra) [UniParc]. Checksum: C1D66CDF0D2F7B44	FASTA	159	17,888
	10 20 30 40 50 60 MALETICRPS GRKSSKMQAF RIWDVNQKTF YLRNNQLVAG YLQGPNVNLE EKIDVVPIEP 70 80 90 100 110 120 HALFLGIHGG KMCLSCVKSG DETRLQLEAV NITDLSENRK QDKRFAFIRS DSGPTTSFES 130 140 150 AACPGWFLCT AMEADQPVSL TNMPDEGVMV TKFYFQEDE
	Isoform 3 (icIL-1ra type II) [UniParc]. Checksum: 624A1574C2334229	FASTA	180	19,897
	10 20 30 40 50 60 MALADLYEEG GGGGGEGEDN ADSKETICRP SGRKSSKMQA FRIWDVNQKT FYLRNNQLVA 70 80 90 100 110 120 GYLQGPNVNL EEKIDVVPIE PHALFLGIHG GKMCLSCVKS GDETRLQLEA VNITDLSENR 130 140 150 160 170 180 KQDKRFAFIR SDSGPTTSFE SAACPGWFLC TAMEADQPVS LTNMPDEGVM VTKFYFQEDE
	Isoform 4 [UniParc]. Checksum: 4CAD6784B890906B	FASTA	143	16,142
	10 20 30 40 50 60 MQAFRIWDVN QKTFYLRNNQ LVAGYLQGPN VNLEEKIDVV PIEPHALFLG IHGGKMCLSC 70 80 90 100 110 120 VKSGDETRLQ LEAVNITDLS ENRKQDKRFA FIRSDSGPTT SFESAACPGW FLCTAMEADQ 130 140 PVSLTNMPDE GVMVTKFYFQ EDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, cloning, expression and biological characterization of an interleukin-1 receptor antagonist protein." Carter D.B., Deibel M.R. Jr., Dunn C.J., Tomich C.S.C., Laborde A.L., Slightom J.L., Berger A.E., Bienkowski M.J., Sun F.F., McEwan R.N., Harris P.K.W., Yem A.W., Waszak G.A., Chosay J.G., Sieu L.C., Hardee M.M., Zurcher-Neely H.A., Reardon I.M. , Heinrikson R.L., Truesdell S.E., Shelly J.A., Eessalu T.E., Taylor B.M., Tracey D.E. Nature 344:633-638(1990) [PubMed: 2139180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Primary structure and functional expression from complementary DNA of a human interleukin-1 receptor antagonist." Eisenberg S.P., Evans R.J., Arend W.P., Verderber E., Brewer M.T., Hannum C.H., Thompson R.C. Nature 343:341-346(1990) [PubMed: 2137201] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanism." Eisenberg S.P., Brewer M.T., Verderber E., Heimdal P., Brandhuber B.J., Thompson R.C. Proc. Natl. Acad. Sci. U.S.A. 88:5232-5236(1991) [PubMed: 1828896] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"Cloning and chromosome mapping of the human interleukin-1 receptor antagonist gene." Lennard A., Gorman P., Carrier M., Griffiths S., Scotney H., Sheer D., Solari R. Cytokine 4:83-89(1992) [PubMed: 1385987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]	"Intracellular IL-1 receptor antagonist promoter: cell type-specific and inducible regulatory regions." Jenkins J.K., Drong R.F., Shuck M.E., Bienkowski M.J., Slightom J.L., Arend W.P., Smith M.F. Jr. J. Immunol. 158:748-755(1997) [PubMed: 8992991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
[6]	"cDNA cloning of an intracellular form of the human interleukin 1 receptor antagonist associated with epithelium." Haskill S., Martin G., van Le L., Morris J., Peace A., Bigler C.F., Jaffe G.J., Hammerberg C., Sporn S.A., Fong S., Arend W.P., Ralph P. Proc. Natl. Acad. Sci. U.S.A. 88:3681-3685(1991) [PubMed: 1827201] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]	"Cloning and characterization of a new isoform of the interleukin 1 receptor antagonist." Muzio M., Polentarutti N., Sironi M., Poli G., De Gioia L., Introna M., Mantovani A., Colotta F. J. Exp. Med. 182:623-628(1995) [PubMed: 7629520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[8]	SeattleSNPs variation discovery resource Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Pancreas.
[12]	"Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor." Hannum C.H., Wilcox C.J., Arend W.P., Joslin F.G., Dripps D.J., Heimdal P.L., Armes L.G., Sommer A., Eisenberg S.P., Thompson R.C. Nature 343:336-340(1990) [PubMed: 2137200] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-45, GLYCOSYLATION AT ASN-109.
[13]	"Purification and characterization of interleukin 1 receptor level antagonist proteins from THP-1 cells." Bienkowski M.J., Eessalu T.E., Berger A.E., Truesdell S.E., Shelly J.A., Laborde A.L., Zurcher-Neely H.A., Reardon I.M., Heinrikson R.L., Chosay J.G., Tracey D.E. J. Biol. Chem. 265:14505-14511(1990) [PubMed: 2143761] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-52.
[14]	"Detection of an interleukin-1 intracellular receptor antagonist mRNA variant." Weissbach L., Tran K., Colquhoun S.A., Champliaud M.-F., Towle C.A. Biochem. Biophys. Res. Commun. 244:91-95(1998) [PubMed: 9514884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-177 (ISOFORM 4).
[15]	"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: 7989776] [Abstract] Cited for: RECEPTOR-BINDING.
[16]	"Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex." Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G. J. Biol. Chem. 270:13757-13765(1995) [PubMed: 7775431] [Abstract] Cited for: FUNCTION.
[17]	"A sequence-based map of the nine genes of the human interleukin-1 cluster." Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G., Kornman K. Genomics 79:718-725(2002) [PubMed: 11991722] [Abstract] Cited for: IDENTIFICATION (ISOFORM 2).
[18]	"Interleukin-1 receptor antagonist allele (IL1RN*2) associated with nephropathy in diabetes mellitus." Blakemore A.I.F., Cox A., Gonzalez A.-M., Maskil J.K., Hughes M.E., Wilson R.M., Ward J.D., Duff G.W. Hum. Genet. 97:369-374(1996) [PubMed: 8786086] [Abstract] Cited for: INVOLVEMENT IN DIABETIC NEPHROPATHY SUSCEPTIBILITY.
[19]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109, MASS SPECTROMETRY. Tissue: Plasma.
[20]	"An autoinflammatory disease with deficiency of the interleukin-1-receptor antagonist." Aksentijevich I., Masters S.L., Ferguson P.J., Dancey P., Frenkel J., van Royen-Kerkhoff A., Laxer R., Tedgard U., Cowen E.W., Pham T.H., Booty M., Estes J.D., Sandler N.G., Plass N., Stone D.L., Turner M.L., Hill S., Butman J.A. , Schneider R., Babyn P., El-Shanti H.I., Pope E., Barron K., Bing X., Laurence A., Lee C.C., Chapelle D., Clarke G.I., Ohson K., Nicholson M., Gadina M., Yang B., Korman B.D., Gregersen P.K., van Hagen P.M., Hak A.E., Huizing M., Rahman P., Douek D.C., Remmers E.F., Kastner D.L., Goldbach-Mansky R. N. Engl. J. Med. 360:2426-2437(2009) [PubMed: 19494218] [Abstract] Cited for: INVOLVEMENT IN DIRA.
[21]	"Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy." Stockman B.J., Scahill T.A., Roy M., Ulrich E.L., Strakalaitis N.A., Brunner D.P., Yem A.W., Deibel M.R. Jr. Biochemistry 31:5237-5244(1992) [PubMed: 1534997] [Abstract] Cited for: STRUCTURE BY NMR.
[22]	"Solution structure of human interleukin-1 receptor antagonist protein." Stockman B.J., Scahill T.A., Strakalaitis N.A., Brunner D.P., Yem A.W., Deibel M.R. Jr. FEBS Lett. 349:79-83(1994) [PubMed: 8045306] [Abstract] Cited for: STRUCTURE BY NMR.
[23]	"X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution." Vigers G.P.A., Caffes P., Evans R.J., Thompson R.C., Eisenberg S.P., Brandhuber B.J. J. Biol. Chem. 269:12874-12879(1994) [PubMed: 8175703] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[24]	"Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline." Schreuder H.A., Rondeau J.-M., Tardif C., Soffientini A., Sarubbi E., Akeson A., Bowlin T.L., Yanofsky S., Barrett R.W. Eur. J. Biochem. 227:838-847(1995) [PubMed: 7867645] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[25]	"A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist." Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E., Akeson A., Bowlin T., Yanofsky S., Barrett R.W. Nature 386:194-200(1997) [PubMed: 9062194] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 32-177 IN COMPLEX WITH IL1R.
[26]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed: 18987736] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-124.
+	Additional computationally mapped references.

Web resources

R&D Systems' cytokine source book: IL-1ra

Wikipedia

Interleukin-1 entry

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Kineret professional medical information"

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53296 mRNA. Translation: CAA37386.1.
X52015 mRNA. Translation: CAA36262.1.
M63099 Genomic DNA. Translation: AAB41943.1.
X64532 Genomic DNA. Translation: CAA45832.1.
U65590 Genomic DNA. Translation: AAB92270.1.
U65590 Genomic DNA. Translation: AAB92268.1.
U65590 Genomic DNA. Translation: AAB92269.1.
M55646 mRNA. Translation: AAA59138.1.
X84348 mRNA. Translation: CAA59087.1.
AY196903 Genomic DNA. Translation: AAN87150.1.
AK290926 mRNA. Translation: BAF83615.1.
CH471217 Genomic DNA. Translation: EAW73625.1.
BC009745 mRNA. Translation: AAH09745.1.
AF043143 mRNA. Translation: AAC39672.1.
BN000002 Genomic DNA. Translation: CAD29879.1.

IPI

IPI00000045.
IPI00174541.
IPI00175024.
IPI00218573.

PIR

A30368. A40956.
A39386. I37893.

RefSeq

NP_000568.1. NM_000577.4.
NP_776213.1. NM_173841.2.
NP_776214.1. NM_173842.2.
NP_776215.1. NM_173843.2.

UniGene

Hs.81134.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ILR	X-ray	2.10	1/2	26-177	[»]
1ILT	X-ray	2.00	A/B	26-177	[»]
1IRA	X-ray	2.70	X	26-177	[»]
1IRP	NMR	-	A	26-177	[»]
1ITN	model	-	A	31-177	[»]
2IRT	X-ray	3.20	A/B	26-177	[»]

ProteinModelPortal

P18510.

SMR

P18510. Positions 33-177.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3513N.

IntAct

P18510. 1 interaction.

STRING

P18510.

Polymorphism databases

DMDM

124312.

2D gel databases

Aarhus/Ghent-2DPAGE

7104. IEF.
7105. IEF.

Proteomic databases

PRIDE

P18510.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000409930; ENSP00000387173; ENSG00000136689.

GeneID

3557.

KEGG

hsa:3557.

UCSC

uc002tiy.1. human.
uc002tjb.1. human.

Organism-specific databases

CTD

3557.

GeneCards

GC02P113864.

HGNC

HGNC:6000. IL1RN.

HPA

CAB009633.
HPA001482.

MIM

147679. gene.
612628. phenotype.
612852. phenotype.

neXtProt

NX_P18510.

Orphanet

210115. Autoinflammatory disease due to interleukin-1 receptor antagonist deficiency.

PharmGKB

PA29816.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14050.

GeneTree

ENSGT00530000062899.

HOVERGEN

HBG052099.

OMA

KLCLACV.

Enzyme and pathway databases

Pathway_Interaction_DB

il1pathway. IL1-mediated signaling events.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P18510.

Bgee

P18510.

CleanEx

HS_IL1RN.

Genevestigator

P18510.

GermOnline

ENSG00000136689. Homo sapiens.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR003297. IL_rcpt_IL1RA.
IPR020877. Interleukin-1_CS.
IPR000975. Interleukin_1.
[Graphical view]

KO

K05481.

Pfam

PF00340. IL1. 1 hit.
[Graphical view]

PRINTS

PR00264. INTERLEUKIN1.
PR01360. INTRLEUKIN1X.

SMART

SM00125. IL1. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

ProtoNet

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Other

DrugBank

DB00026. Anakinra.

NextBio

13886.

SOURCE

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Entry information

Entry name

IL1RA_HUMAN

Accession

Primary (citable) accession number: P18510
Secondary accession number(s): A8K4G1 , Q14628, Q7RTZ4, Q96GD6, Q9UPC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 141 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.