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Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]

 IL1R1_HUMAN             Reviewed;         569 AA.
P14778; Q587I7;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
12-AUG-2020, entry version 224.
RecName: Full=Interleukin-1 receptor type 1;
Short=IL-1R-1;
Short=IL-1RT-1;
Short=IL-1RT1;
EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
AltName: Full=CD121 antigen-like family member A;
AltName: Full=Interleukin-1 receptor alpha;
Short=IL-1R-alpha;
AltName: Full=Interleukin-1 receptor type I;
AltName: Full=p80;
AltName: CD_antigen=CD121a;
Contains:
RecName: Full=Interleukin-1 receptor type 1, membrane form;
Short=mIL-1R1;
Short=mIL-1RI;
Contains:
RecName: Full=Interleukin-1 receptor type 1, soluble form;
Short=sIL-1R1;
Short=sIL-1RI;
Flags: Precursor;
Name=IL1R1; Synonyms=IL1R, IL1RA, IL1RT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2532321; DOI=10.1093/nar/17.23.10114;
Chua A.O., Gubler U.;
"Sequence of the cDNA for the human fibroblast type interleukin-1
receptor.";
Nucleic Acids Res. 17:10114-10114(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=2530587; DOI=10.1073/pnas.86.22.8946;
Sims J.E., Acres R.B., Grubin C.E., McMahan C.J., Wignall J.M., March C.J.,
Dower S.K.;
"Cloning the interleukin 1 receptor from human T cells.";
Proc. Natl. Acad. Sci. U.S.A. 86:8946-8950(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-124.
SeattleSNPs variation discovery resource;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=8142597; DOI=10.1016/1043-4666(93)90032-z;
Svenson M., Hansen M.B., Heegaard P., Abell K., Bendtzen K.;
"Specific binding of interleukin 1 (IL-1) beta and IL-1 receptor antagonist
(IL-1ra) to human serum. High-affinity binding of IL-1ra to soluble IL-1
receptor type I.";
Cytokine 5:427-435(1993).
[8]
LIGAND-BINDING.
PubMed=7989776;
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.;
"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. 153:5802-5809(1994).
[9]
INTERACTION WITH IL1RAP AND IRAK1.
TISSUE=Placenta;
PubMed=9371760; DOI=10.1073/pnas.94.24.12829;
Huang J., Gao X., Li S., Cao Z.;
"Recruitment of IRAK to the interleukin 1 receptor complex requires
interleukin 1 receptor accessory protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:12829-12832(1997).
[10]
PHOSPHORYLATION AT TYR-496, AND INTERACTION WITH PIK3R1.
PubMed=9821957; DOI=10.1016/s0014-5793(98)01270-8;
Marmiroli S., Bavelloni A., Faenza I., Sirri A., Ognibene A., Cenni V.,
Tsukada J., Koyama Y., Ruzzene M., Ferri A., Auron P.E., Toker A.,
Maraldi N.M.;
"Phosphatidylinositol 3-kinase is recruited to a specific site in the
activated IL-1 receptor I.";
FEBS Lett. 438:49-54(1998).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10653850; DOI=10.1093/intimm/12.2.151;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K., Hada T.,
Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[12]
FUNCTION, AND MUTAGENESIS OF ASP-369 AND ARG-428.
PubMed=10671496; DOI=10.1074/jbc.275.7.4670;
Slack J.L., Schooley K., Bonnert T.P., Mitcham J.L., Qwarnstrom E.E.,
Sims J.E., Dower S.K.;
"Identification of two major sites in the type I interleukin-1 receptor
cytoplasmic region responsible for coupling to pro-inflammatory signaling
pathways.";
J. Biol. Chem. 275:4670-4678(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-332 IN COMPLEX WITH IL1B.
PubMed=9062193; DOI=10.1038/386190a0;
Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.;
"Crystal structure of the type-I interleukin-1 receptor complexed with
interleukin-1beta.";
Nature 386:190-194(1997).
[14]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-331 IN COMPLEX WITH IL1RA.
PubMed=9062194; DOI=10.1038/386194a0;
Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E.,
Akeson A., Bowlin T., Yanofsky S., Barrett R.W.;
"A new cytokine-receptor binding mode revealed by the crystal structure of
the IL-1 receptor with an antagonist.";
Nature 386:194-200(1997).
[15]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 4-315 IN COMPLEX WITH THE
ANTAGONIST PEPTIDE AF10847.
PubMed=10903327; DOI=10.1074/jbc.m006071200;
Vigers G.P.A., Dripps D.J., Edwards C.K. III, Brandhuber B.J.;
"X-ray crystal structure of a small antagonist peptide bound to
interleukin-1 receptor type 1.";
J. Biol. Chem. 275:36927-36933(2000).
-!- FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to
interleukin-1 associates with the coreceptor IL1RAP to form the high
affinity interleukin-1 receptor complex which mediates interleukin-1-
dependent activation of NF-kappa-B, MAPK and other pathways. Signaling
involves the recruitment of adapter molecules such as TOLLIP, MYD88,
and IRAK1 or IRAK2 via the respective TIR domains of the
receptor/coreceptor subunits. Binds ligands with comparable affinity
and binding of antagonist IL1RN prevents association with IL1RAP to
form a signaling complex. Involved in IL1B-mediated costimulation of
IFNG production from T-helper 1 (Th1) cells (PubMed:10653850).
{ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:10671496}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
-!- SUBUNIT: The interleukin-1 receptor complex is a heterodimer of IL1R1
and IL1RAP. Interacts with PIK3R1. {ECO:0000269|PubMed:10903327,
ECO:0000269|PubMed:9062193, ECO:0000269|PubMed:9062194,
ECO:0000269|PubMed:9371760, ECO:0000269|PubMed:9821957}.
-!- INTERACTION:
P14778; P09619: PDGFRB; NbExp=2; IntAct=EBI-525905, EBI-641237;
P14778; Q9Y4K3: TRAF6; NbExp=2; IntAct=EBI-525905, EBI-359276;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8142597}; Single-
pass type I membrane protein {ECO:0000269|PubMed:8142597}. Cell
membrane {ECO:0000305|PubMed:8142597}. Secreted
{ECO:0000269|PubMed:8142597}.
-!- TISSUE SPECIFICITY: Expressed in T-helper cell subsets. Preferentially
expressed in T-helper 1 (Th1) cells. {ECO:0000269|PubMed:10653850}.
-!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
Self-association of TIR domains is required for NADase activity.
{ECO:0000255|PROSITE-ProRule:PRU00204}.
-!- PTM: A soluble form (sIL1R1) is probably produced by proteolytic
cleavage at the cell surface (shedding). {ECO:0000269|PubMed:8142597}.
-!- PTM: Rapidly phosphorylated on Tyr-496 in response to IL-1, which
creates a SH2 binding site for the PI 3-kinase regulatory subunit
PIK3R1. {ECO:0000269|PubMed:9821957}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il1r1/";
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EMBL; X16896; CAA34773.1; -; mRNA.
EMBL; M27492; AAA59137.1; -; mRNA.
EMBL; AF531102; AAM88423.1; -; Genomic_DNA.
EMBL; AC007271; AAX81988.1; -; Genomic_DNA.
EMBL; CH471127; EAX01799.1; -; Genomic_DNA.
EMBL; BC067506; AAH67506.1; -; mRNA.
EMBL; BC075062; AAH75062.1; -; mRNA.
EMBL; BC075063; AAH75063.1; -; mRNA.
CCDS; CCDS2055.1; -.
PIR; A36187; A36187.
RefSeq; NP_000868.1; NM_000877.3.
RefSeq; NP_001275635.1; NM_001288706.1.
RefSeq; NP_001307907.1; NM_001320978.1.
RefSeq; NP_001307909.1; NM_001320980.1.
RefSeq; NP_001307910.1; NM_001320981.1.
RefSeq; NP_001307911.1; NM_001320982.1.
RefSeq; NP_001307912.1; NM_001320983.1.
RefSeq; NP_001307913.1; NM_001320984.1.
RefSeq; NP_001307914.1; NM_001320985.1.
RefSeq; XP_005263987.1; XM_005263930.4.
RefSeq; XP_005263991.1; XM_005263934.4.
RefSeq; XP_011509417.1; XM_011511115.2.
RefSeq; XP_011509418.1; XM_011511116.1.
RefSeq; XP_011509419.1; XM_011511117.1.
RefSeq; XP_011509420.1; XM_011511118.2.
RefSeq; XP_016859478.1; XM_017003989.1.
PDB; 1G0Y; X-ray; 3.00 A; R=21-332.
PDB; 1IRA; X-ray; 2.70 A; Y=18-336.
PDB; 1ITB; X-ray; 2.50 A; B=18-332.
PDB; 4DEP; X-ray; 3.10 A; B/E=18-336.
PDB; 4GAF; X-ray; 2.15 A; B=18-336.
PDBsum; 1G0Y; -.
PDBsum; 1IRA; -.
PDBsum; 1ITB; -.
PDBsum; 4DEP; -.
PDBsum; 4GAF; -.
SMR; P14778; -.
BioGRID; 109770; 27.
DIP; DIP-93N; -.
IntAct; P14778; 15.
STRING; 9606.ENSP00000386380; -.
ChEMBL; CHEMBL1959; -.
DrugBank; DB00026; Anakinra.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB05303; OMS-103HP.
DrugBank; DB05207; SD118.
DrugCentral; P14778; -.
GuidetoPHARMACOLOGY; 1734; -.
TCDB; 8.A.23.1.11; the basigin (basigin) family.
GlyGen; P14778; 6 sites.
iPTMnet; P14778; -.
PhosphoSitePlus; P14778; -.
BioMuta; IL1R1; -.
DMDM; 124308; -.
jPOST; P14778; -.
MassIVE; P14778; -.
MaxQB; P14778; -.
PaxDb; P14778; -.
PeptideAtlas; P14778; -.
PRIDE; P14778; -.
ProteomicsDB; 53081; -.
ABCD; P14778; 3 sequenced antibodies.
Antibodypedia; 3576; 888 antibodies.
Ensembl; ENST00000410023; ENSP00000386380; ENSG00000115594.
GeneID; 3554; -.
KEGG; hsa:3554; -.
UCSC; uc002tbq.5; human.
CTD; 3554; -.
DisGeNET; 3554; -.
EuPathDB; HostDB:ENSG00000115594.11; -.
GeneCards; IL1R1; -.
HGNC; HGNC:5993; IL1R1.
HPA; ENSG00000115594; Low tissue specificity.
MIM; 147810; gene.
neXtProt; NX_P14778; -.
OpenTargets; ENSG00000115594; -.
PharmGKB; PA29809; -.
eggNOG; ENOG502QWEU; Eukaryota.
GeneTree; ENSGT01000000214361; -.
HOGENOM; CLU_025552_3_1_1; -.
InParanoid; P14778; -.
KO; K04386; -.
OMA; EISGFSW; -.
OrthoDB; 1109920at2759; -.
PhylomeDB; P14778; -.
TreeFam; TF325519; -.
PathwayCommons; P14778; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SignaLink; P14778; -.
SIGNOR; P14778; -.
BioGRID-ORCS; 3554; 13 hits in 875 CRISPR screens.
ChiTaRS; IL1R1; human.
EvolutionaryTrace; P14778; -.
GeneWiki; Interleukin_1_receptor,_type_I; -.
GenomeRNAi; 3554; -.
Pharos; P14778; Tclin.
PRO; PR:P14778; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; P14778; protein.
Bgee; ENSG00000115594; Expressed in palpebral conjunctiva and 237 other tissues.
ExpressionAtlas; P14778; baseline and differential.
Genevisible; P14778; HS.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019966; F:interleukin-1 binding; IBA:GO_Central.
GO; GO:0004908; F:interleukin-1 receptor activity; IDA:BHF-UCL.
GO; GO:0004909; F:interleukin-1, type I, activating receptor activity; TAS:ProtInc.
GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:2000661; P:positive regulation of interleukin-1-mediated signaling pathway; IEA:Ensembl.
GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl.
GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
GO; GO:0070555; P:response to interleukin-1; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR041416; Ig_6.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004076; IL-1_rcpt_I-typ.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF18452; Ig_6; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01538; INTRLEUKN1R1.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
Immunoglobulin domain; Inflammatory response; Membrane; NAD;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..17
CHAIN 18..569
/note="Interleukin-1 receptor type 1, membrane form"
/id="PRO_0000015435"
CHAIN 18..?
/note="Interleukin-1 receptor type 1, soluble form"
/id="PRO_0000415344"
TOPO_DOM 18..336
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 337..356
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 357..569
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 23..110
/note="Ig-like C2-type 1"
DOMAIN 118..210
/note="Ig-like C2-type 2"
DOMAIN 226..328
/note="Ig-like C2-type 3"
DOMAIN 383..538
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
ACT_SITE 470
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
MOD_RES 496
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:9821957"
CARBOHYD 100
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 193
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 233
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 249
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 263
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 297
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 23..104
DISULFID 44..96
DISULFID 121..164
DISULFID 142..196
DISULFID 248..312
VARIANT 124
/note="A -> G (in dbSNP:rs2228139)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_019131"
VARIANT 344
/note="T -> M (in dbSNP:rs28362304)"
/id="VAR_029189"
MUTAGEN 369
/note="D->A: Reduces NF-kappa-B activation."
/evidence="ECO:0000269|PubMed:10671496"
MUTAGEN 428
/note="R->A: Reduces NF-kappa-B activation and receptor-
associated kinase activation."
/evidence="ECO:0000269|PubMed:10671496"
STRAND 24..27
/evidence="ECO:0000244|PDB:4GAF"
STRAND 32..35
/evidence="ECO:0000244|PDB:4GAF"
STRAND 40..43
/evidence="ECO:0000244|PDB:4GAF"
HELIX 48..50
/evidence="ECO:0000244|PDB:1IRA"
STRAND 56..59
/evidence="ECO:0000244|PDB:4GAF"
STRAND 72..77
/evidence="ECO:0000244|PDB:4GAF"
STRAND 80..83
/evidence="ECO:0000244|PDB:4GAF"
HELIX 88..90
/evidence="ECO:0000244|PDB:4GAF"
STRAND 92..97
/evidence="ECO:0000244|PDB:4GAF"
STRAND 100..102
/evidence="ECO:0000244|PDB:1ITB"
STRAND 105..114
/evidence="ECO:0000244|PDB:4GAF"
STRAND 120..122
/evidence="ECO:0000244|PDB:4GAF"
HELIX 124..126
/evidence="ECO:0000244|PDB:4GAF"
STRAND 127..133
/evidence="ECO:0000244|PDB:4GAF"
STRAND 135..137
/evidence="ECO:0000244|PDB:1G0Y"
STRAND 138..141
/evidence="ECO:0000244|PDB:4GAF"
HELIX 146..148
/evidence="ECO:0000244|PDB:4GAF"
TURN 151..153
/evidence="ECO:0000244|PDB:4GAF"
STRAND 159..162
/evidence="ECO:0000244|PDB:4GAF"
STRAND 171..177
/evidence="ECO:0000244|PDB:4GAF"
STRAND 180..183
/evidence="ECO:0000244|PDB:4GAF"
HELIX 188..190
/evidence="ECO:0000244|PDB:4GAF"
STRAND 192..202
/evidence="ECO:0000244|PDB:4GAF"
STRAND 205..218
/evidence="ECO:0000244|PDB:4GAF"
STRAND 227..230
/evidence="ECO:0000244|PDB:4GAF"
STRAND 233..237
/evidence="ECO:0000244|PDB:4GAF"
STRAND 240..242
/evidence="ECO:0000244|PDB:1ITB"
STRAND 244..252
/evidence="ECO:0000244|PDB:4GAF"
STRAND 256..262
/evidence="ECO:0000244|PDB:4GAF"
STRAND 272..281
/evidence="ECO:0000244|PDB:4GAF"
HELIX 287..289
/evidence="ECO:0000244|PDB:4GAF"
STRAND 290..300
/evidence="ECO:0000244|PDB:4GAF"
HELIX 303..306
/evidence="ECO:0000244|PDB:4GAF"
STRAND 310..316
/evidence="ECO:0000244|PDB:4GAF"
STRAND 319..328
/evidence="ECO:0000244|PDB:4GAF"
SEQUENCE 569 AA; 65402 MW; 5BAA83F8F0225C25 CRC64;
MKVLLRLICF IALLISSLEA DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD
DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL
CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR
LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL
GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE
IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKHMIG ICVTLTVIIV CSVFIYKIFK
IDIVLWYRDS CYDFLPIKAS DGKTYDAYIL YPKTVGEGST SDCDIFVFKV LPEVLEKQCG
YKLFIYGRDD YVGEDIVEVI NENVKKSRRL IIILVRETSG FSWLGGSSEE QIAMYNALVQ
DGIKVVLLEL EKIQDYEKMP ESIKFIKQKH GAIRWSGDFT QGPQSAKTRF WKNVRYHMPV
QRRSPSSKHQ LLSPATKEKL QREAHVPLG


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