TLR7_HUMAN
ID TLR7_HUMAN Reviewed; 1049 AA.
AC Q9NYK1; D1CS69; Q9NR98;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Toll-like receptor 7 {ECO:0000305};
DE Flags: Precursor;
GN Name=TLR7 {ECO:0000312|HGNC:HGNC:15631}; ORFNames=UNQ248/PRO285;
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=11022119;
RA Du X., Poltorak A., Wei Y., Beutler B.;
RT "Three novel mammalian Toll-like receptors: gene structure, expression, and
RT evolution.";
RL Eur. Cytokine Netw. 11:362-371(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=11022120;
RA Chuang T.-H., Ulevitch R.J.;
RT "Cloning and characterization of a sub-family of human Toll-like receptors:
RT hTLR7, hTLR8 and hTLR9.";
RL Eur. Cytokine Netw. 11:372-378(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-11.
RX PubMed=19924287; DOI=10.1371/journal.pone.0007803;
RA Georgel P., Macquin C., Bahram S.;
RT "The heterogeneous allelic repertoire of human Toll-Like receptor (TLR)
RT genes.";
RL PLoS ONE 4:E7803-E7803(2009).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=12738885; DOI=10.1073/pnas.0631696100;
RA Lee J., Chuang T.H., Redecke V., She L., Pitha P.M., Carson D.A., Raz E.,
RA Cottam H.B.;
RT "Molecular basis for the immunostimulatory activity of guanine nucleoside
RT analogs: activation of Toll-like receptor 7.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6646-6651(2003).
RN [7]
RP FUNCTION.
RX PubMed=14976261; DOI=10.1126/science.1093616;
RA Diebold S.S., Kaisho T., Hemmi H., Akira S., Reis e Sousa C.;
RT "Innate antiviral responses by means of TLR7-mediated recognition of
RT single-stranded RNA.";
RL Science 303:1529-1531(2004).
RN [8]
RP FUNCTION.
RX PubMed=18250417; DOI=10.4049/jimmunol.180.4.2117;
RA Gantier M.P., Tong S., Behlke M.A., Xu D., Phipps S., Foster P.S.,
RA Williams B.R.;
RT "TLR7 is involved in sequence-specific sensing of single-stranded RNAs in
RT human macrophages.";
RL J. Immunol. 180:2117-2124(2008).
RN [9]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=27742543; DOI=10.1016/j.immuni.2016.09.011;
RA Zhang Z., Ohto U., Shibata T., Krayukhina E., Taoka M., Yamauchi Y.,
RA Tanji H., Isobe T., Uchiyama S., Miyake K., Shimizu T.;
RT "Structural Analysis Reveals that Toll-like Receptor 7 Is a Dual Receptor
RT for Guanosine and Single-Stranded RNA.";
RL Immunity 45:737-748(2016).
RN [10]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=31608988; DOI=10.1002/eji.201948151;
RA Davenne T., Bridgeman A., Rigby R.E., Rehwinkel J.;
RT "Deoxyguanosine is a TLR7 agonist.";
RL Eur. J. Immunol. 50:56-62(2020).
RN [11]
RP FUNCTION.
RX PubMed=32433612; DOI=10.1038/s41586-020-2282-0;
RA Heinz L.X., Lee J., Kapoor U., Kartnig F., Sedlyarov V., Papakostas K.,
RA Cesar-Razquin A., Essletzbichler P., Goldmann U., Stefanovic A.,
RA Bigenzahn J.W., Scorzoni S., Pizzagalli M.D., Bensimon A., Mueller A.C.,
RA King F.J., Li J., Girardi E., Mbow M.L., Whitehurst C.E., Rebsamen M.,
RA Superti-Furga G.;
RT "TASL is the SLC15A4-associated adaptor for IRF5 activation by TLR7-9.";
RL Nature 581:316-322(2020).
RN [12]
RP FUNCTION, INVOLVEMENT IN IMD74, VARIANT IMD74 PHE-795, CHARACTERIZATION OF
RP VARIANT IMD74 PHE-795, AND ACTIVITY REGULATION.
RX PubMed=32706371; DOI=10.1001/jama.2020.13719;
RA van der Made C.I., Simons A., Schuurs-Hoeijmakers J., van den Heuvel G.,
RA Mantere T., Kersten S., van Deuren R.C., Steehouwer M.,
RA van Reijmersdal S.V., Jaeger M., Hofste T., Astuti G.,
RA Corominas Galbany J., van der Schoot V., van der Hoeven H.,
RA Hagmolen Of Ten Have W., Klijn E., van den Meer C., Fiddelaers J.,
RA de Mast Q., Bleeker-Rovers C.P., Joosten L.A.B., Yntema H.G., Gilissen C.,
RA Nelen M., van der Meer J.W.M., Brunner H.G., Netea M.G.,
RA van de Veerdonk F.L., Hoischen A.;
RT "Presence of Genetic Variants Among Young Men With Severe COVID-19.";
RL JAMA 324:663-673(2020).
RN [13] {ECO:0007744|PDB:7CYN}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH UNC93B1,
RP AND INTERACTION WITH UNC93B1.
RX PubMed=33432245; DOI=10.1038/s41594-020-00542-w;
RA Ishida H., Asami J., Zhang Z., Nishizawa T., Shigematsu H., Ohto U.,
RA Shimizu T.;
RT "Cryo-EM structures of Toll-like receptors in complex with UNC93B1.";
RL Nat. Struct. Mol. Biol. 28:173-180(2021).
CC -!- FUNCTION: Endosomal receptor that plays a key role in innate and
CC adaptive immunity (PubMed:14976261, PubMed:32433612). Controls host
CC immune response against pathogens through recognition of uridine-
CC containing single strand RNAs (ssRNAs) of viral origin or guanosine
CC analogs (PubMed:31608988, PubMed:27742543, PubMed:12738885,
CC PubMed:32706371). Upon binding to agonists, undergoes dimerization that
CC brings TIR domains from the two molecules into direct contact, leading
CC to the recruitment of TIR-containing downstream adapter MYD88 through
CC homotypic interaction (PubMed:27742543). In turn, the Myddosome
CC signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3
CC leading to activation of downstream transcription factors NF-kappa-B
CC and IRF7 to induce pro-inflammatory cytokines and interferons,
CC respectively (PubMed:27742543, PubMed:32706371).
CC {ECO:0000269|PubMed:12738885, ECO:0000269|PubMed:14976261,
CC ECO:0000269|PubMed:27742543, ECO:0000269|PubMed:31608988,
CC ECO:0000269|PubMed:32433612, ECO:0000269|PubMed:32706371}.
CC -!- ACTIVITY REGULATION: Activated by guanosine analogs including
CC deoxyguanosine, 7-thia-8-oxoguanosine or 7-deazaguanosine in a RNA-
CC independent manner. Activated by imiquimod (PubMed:32706371).
CC {ECO:0000269|PubMed:12738885, ECO:0000269|PubMed:31608988,
CC ECO:0000269|PubMed:32706371}.
CC -!- SUBUNIT: Homodimer (PubMed:27742543). Interacts with MYD88 via their
CC respective TIR domains (Probable). Interacts with UNC93B1
CC (PubMed:33432245). Interacts with SMPDL3B (By similarity).
CC {ECO:0000250|UniProtKB:P58681, ECO:0000269|PubMed:27742543,
CC ECO:0000269|PubMed:33432245, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P58681}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P58681}. Endosome
CC {ECO:0000250|UniProtKB:P58681}. Lysosome
CC {ECO:0000250|UniProtKB:P58681}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P58681}. Note=Relocalizes from endoplasmic
CC reticulum to endosome and lysosome upon stimulation with agonist.
CC {ECO:0000250|UniProtKB:P58681}.
CC -!- TISSUE SPECIFICITY: Detected in brain, placenta, spleen, stomach, small
CC intestine, lung and in plasmacytoid pre-dendritic cells. Expressed in
CC peripheral mononuclear blood cells (PubMed:32706371).
CC {ECO:0000269|PubMed:32706371}.
CC -!- DOMAIN: Contains two binding domains, first site for small ligands and
CC second site for ssRNA. {ECO:0000269|PubMed:27742543}.
CC -!- DISEASE: Immunodeficiency 74, COVID19-related, X-linked (IMD74)
CC [MIM:301051]: An X-linked recessive immunologic disorder characterized
CC by impaired type I and type II interferon responses due to defective
CC TLR7 signaling. Individuals with TLR7 deficiency develop severe
CC respiratory insufficiency in response to infection with SARS-CoV-2
CC coronavirus. Death from respiratory failure may occur.
CC {ECO:0000269|PubMed:32706371}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; AF240467; AAF60188.1; -; mRNA.
DR EMBL; AF245702; AAF78035.1; -; mRNA.
DR EMBL; DQ022185; AAZ99026.1; -; Genomic_DNA.
DR EMBL; AY358292; AAQ88659.1; -; mRNA.
DR EMBL; BC033651; AAH33651.1; -; mRNA.
DR CCDS; CCDS14151.1; -.
DR RefSeq; NP_057646.1; NM_016562.3.
DR PDB; 7CYN; EM; 4.20 A; A/B=1-1049.
DR PDBsum; 7CYN; -.
DR AlphaFoldDB; Q9NYK1; -.
DR SMR; Q9NYK1; -.
DR BioGRID; 119436; 25.
DR IntAct; Q9NYK1; 12.
DR STRING; 9606.ENSP00000370034; -.
DR BindingDB; Q9NYK1; -.
DR ChEMBL; CHEMBL5936; -.
DR DrugBank; DB16580; Afimetoran.
DR DrugBank; DB05127; ANA971.
DR DrugBank; DB05475; Golotimod.
DR DrugBank; DB01611; Hydroxychloroquine.
DR DrugBank; DB00724; Imiquimod.
DR DrugBank; DB04860; Isatoribine.
DR DrugBank; DB06530; Resiquimod.
DR DrugBank; DB06329; RG-7795.
DR DrugCentral; Q9NYK1; -.
DR GuidetoPHARMACOLOGY; 1757; -.
DR GlyGen; Q9NYK1; 14 sites.
DR iPTMnet; Q9NYK1; -.
DR PhosphoSitePlus; Q9NYK1; -.
DR BioMuta; TLR7; -.
DR DMDM; 20140876; -.
DR jPOST; Q9NYK1; -.
DR MassIVE; Q9NYK1; -.
DR PaxDb; Q9NYK1; -.
DR PeptideAtlas; Q9NYK1; -.
DR PRIDE; Q9NYK1; -.
DR ProteomicsDB; 83240; -.
DR Antibodypedia; 8500; 1008 antibodies from 45 providers.
DR DNASU; 51284; -.
DR Ensembl; ENST00000380659.4; ENSP00000370034.3; ENSG00000196664.5.
DR GeneID; 51284; -.
DR KEGG; hsa:51284; -.
DR MANE-Select; ENST00000380659.4; ENSP00000370034.3; NM_016562.4; NP_057646.1.
DR UCSC; uc004cvc.4; human.
DR CTD; 51284; -.
DR DisGeNET; 51284; -.
DR GeneCards; TLR7; -.
DR HGNC; HGNC:15631; TLR7.
DR HPA; ENSG00000196664; Tissue enhanced (placenta).
DR MalaCards; TLR7; -.
DR MIM; 300365; gene.
DR MIM; 301051; phenotype.
DR neXtProt; NX_Q9NYK1; -.
DR OpenTargets; ENSG00000196664; -.
DR PharmGKB; PA38008; -.
DR VEuPathDB; HostDB:ENSG00000196664; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000159771; -.
DR HOGENOM; CLU_006000_2_0_1; -.
DR InParanoid; Q9NYK1; -.
DR OMA; CNSKYLR; -.
DR OrthoDB; 303561at2759; -.
DR PhylomeDB; Q9NYK1; -.
DR TreeFam; TF325595; -.
DR PathwayCommons; Q9NYK1; -.
DR Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-HSA-168181; Toll Like Receptor 7/8 (TLR7/8) Cascade.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
DR SignaLink; Q9NYK1; -.
DR SIGNOR; Q9NYK1; -.
DR BioGRID-ORCS; 51284; 10 hits in 696 CRISPR screens.
DR ChiTaRS; TLR7; human.
DR GeneWiki; TLR_7; -.
DR GenomeRNAi; 51284; -.
DR Pharos; Q9NYK1; Tclin.
DR PRO; PR:Q9NYK1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NYK1; protein.
DR Bgee; ENSG00000196664; Expressed in monocyte and 116 other tissues.
DR ExpressionAtlas; Q9NYK1; baseline and differential.
DR Genevisible; Q9NYK1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0007252; P:I-kappaB phosphorylation; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IBA:GO_Central.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IBA:GO_Central.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Leucine-rich repeat; Lysosome; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1049
FT /note="Toll-like receptor 7"
FT /id="PRO_0000034733"
FT TOPO_DOM 27..839
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..1049
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 43..64
FT /note="LRR 1"
FT REPEAT 65..87
FT /note="LRR 2"
FT REPEAT 110..126
FT /note="LRR 3"
FT REPEAT 127..149
FT /note="LRR 4"
FT REPEAT 151..170
FT /note="LRR 5"
FT REPEAT 171..195
FT /note="LRR 6"
FT REPEAT 203..226
FT /note="LRR 7"
FT REPEAT 228..247
FT /note="LRR 8"
FT REPEAT 248..275
FT /note="LRR 9"
FT REPEAT 289..312
FT /note="LRR 10"
FT REPEAT 314..337
FT /note="LRR 11"
FT REPEAT 339..368
FT /note="LRR 12"
FT REPEAT 369..392
FT /note="LRR 13"
FT REPEAT 396..419
FT /note="LRR 14"
FT REPEAT 421..443
FT /note="LRR 15"
FT REPEAT 492..515
FT /note="LRR 16"
FT REPEAT 516..540
FT /note="LRR 17"
FT REPEAT 541..564
FT /note="LRR 18"
FT REPEAT 566..588
FT /note="LRR 19"
FT REPEAT 595..618
FT /note="LRR 20"
FT REPEAT 619..644
FT /note="LRR 21"
FT REPEAT 649..672
FT /note="LRR 22"
FT REPEAT 674..697
FT /note="LRR 23"
FT REPEAT 698..721
FT /note="LRR 24"
FT REPEAT 723..745
FT /note="LRR 25"
FT REPEAT 746..769
FT /note="LRR 26"
FT REPEAT 772..795
FT /note="LRR 27"
FT DOMAIN 889..1033
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 11
FT /note="Q -> L (in dbSNP:rs179008)"
FT /evidence="ECO:0000269|PubMed:19924287"
FT /id="VAR_034554"
FT VARIANT 448
FT /note="A -> V (in dbSNP:rs5743781)"
FT /id="VAR_024665"
FT VARIANT 795
FT /note="V -> F (in IMD74; no enhanced expression after
FT stimulation by imiquimod; defective up-regulation of type I
FT IFN-related genes; decreased expression of IFNG;
FT dbSNP:rs200553089)"
FT /evidence="ECO:0000269|PubMed:32706371"
FT /id="VAR_084629"
FT CONFLICT 725
FT /note="L -> H (in Ref. 2; AAF78035)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="L -> P (in Ref. 2; AAF78035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1049 AA; 120922 MW; 8C701E9E437F2721 CRC64;
MVFPMWTLKR QILILFNIIL ISKLLGARWF PKTLPCDVTL DVPKNHVIVD CTDKHLTEIP
GGIPTNTTNL TLTINHIPDI SPASFHRLDH LVEIDFRCNC VPIPLGSKNN MCIKRLQIKP
RSFSGLTYLK SLYLDGNQLL EIPQGLPPSL QLLSLEANNI FSIRKENLTE LANIEILYLG
QNCYYRNPCY VSYSIEKDAF LNLTKLKVLS LKDNNVTAVP TVLPSTLTEL YLYNNMIAKI
QEDDFNNLNQ LQILDLSGNC PRCYNAPFPC APCKNNSPLQ IPVNAFDALT ELKVLRLHSN
SLQHVPPRWF KNINKLQELD LSQNFLAKEI GDAKFLHFLP SLIQLDLSFN FELQVYRASM
NLSQAFSSLK SLKILRIRGY VFKELKSFNL SPLHNLQNLE VLDLGTNFIK IANLSMFKQF
KRLKVIDLSV NKISPSGDSS EVGFCSNART SVESYEPQVL EQLHYFRYDK YARSCRFKNK
EASFMSVNES CYKYGQTLDL SKNSIFFVKS SDFQHLSFLK CLNLSGNLIS QTLNGSEFQP
LAELRYLDFS NNRLDLLHST AFEELHKLEV LDISSNSHYF QSEGITHMLN FTKNLKVLQK
LMMNDNDISS STSRTMESES LRTLEFRGNH LDVLWREGDN RYLQLFKNLL KLEELDISKN
SLSFLPSGVF DGMPPNLKNL SLAKNGLKSF SWKKLQCLKN LETLDLSHNQ LTTVPERLSN
CSRSLKNLIL KNNQIRSLTK YFLQDAFQLR YLDLSSNKIQ MIQKTSFPEN VLNNLKMLLL
HHNRFLCTCD AVWFVWWVNH TEVTIPYLAT DVTCVGPGAH KGQSVISLDL YTCELDLTNL
ILFSLSISVS LFLMVMMTAS HLYFWDVWYI YHFCKAKIKG YQRLISPDCC YDAFIVYDTK
DPAVTEWVLA ELVAKLEDPR EKHFNLCLEE RDWLPGQPVL ENLSQSIQLS KKTVFVMTDK
YAKTENFKIA FYLSHQRLMD EKVDVIILIF LEKPFQKSKF LQLRKRLCGS SVLEWPTNPQ
AHPYFWQCLK NALATDNHVA YSQVFKETV
