TLR8_HUMAN
ID TLR8_HUMAN Reviewed; 1041 AA.
AC Q9NR97; B3Y654; D1CS70; D1CS76; Q495P4; Q6UXL6; Q9NYG9;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Toll-like receptor 8 {ECO:0000305};
DE AltName: CD_antigen=CD288;
DE Flags: Precursor;
GN Name=TLR8 {ECO:0000312|HGNC:HGNC:15632}; ORFNames=UNQ249/PRO286;
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 2).
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] (ISOFORM 1).
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 [MRNA] (ISOFORM 1).
RX PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
RA Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.;
RT "Natural selection in the TLR-related genes in the course of primate
RT evolution.";
RL Immunogenetics 60:727-735(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP FUNCTION IN NF-KAPPA-B ACTIVATION.
RX PubMed=16737960; DOI=10.1074/jbc.m512908200;
RA Qin J., Yao J., Cui G., Xiao H., Kim T.W., Fraczek J., Wightman P.,
RA Sato S., Akira S., Puel A., Casanova J.L., Su B., Li X.;
RT "TLR8-mediated NF-kappaB and JNK activation are TAK1-independent and MEKK3-
RT dependent.";
RL J. Biol. Chem. 281:21013-21021(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH BTK.
RX PubMed=17932028; DOI=10.1074/jbc.m707682200;
RA Doyle S.L., Jefferies C.A., Feighery C., O'Neill L.A.;
RT "Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine
RT kinase.";
RL J. Biol. Chem. 282:36953-36960(2007).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-88.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND CLEAVAGE.
RX PubMed=25297876; DOI=10.4049/jimmunol.1401375;
RA Ishii N., Funami K., Tatematsu M., Seya T., Matsumoto M.;
RT "Endosomal localization of TLR8 confers distinctive proteolytic processing
RT on human myeloid cells.";
RL J. Immunol. 193:5118-5128(2014).
RN [13]
RP UBIQUITINATION BY RNF216.
RX PubMed=31385713; DOI=10.1165/rcmb.2018-0373oc;
RA Evankovich J., Lear T., Baldwin C., Chen Y., White V., Villandre J.,
RA Londino J., Liu Y., McVerry B., Kitsios G.D., Mallampalli R.K., Chen B.B.;
RT "Toll-Like Receptor 8 Stability is Regulated by Ring Finger 216 in response
RT to circulating MicroRNAs.";
RL Am. J. Respir. Cell Mol. Biol. 62:157-167(2020).
RN [14]
RP FUNCTION.
RX PubMed=31778653; DOI=10.1016/j.cell.2019.11.001;
RA Greulich W., Wagner M., Gaidt M.M., Stafford C., Cheng Y., Linder A.,
RA Carell T., Hornung V.;
RT "TLR8 Is a Sensor of RNase T2 Degradation Products.";
RL Cell 179:1264-1275.E13(2019).
RN [15]
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 [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=33718825; DOI=10.1016/j.isci.2021.102295;
RA Campbell G.R., To R.K., Hanna J., Spector S.A.;
RT "SARS-CoV-2, SARS-CoV-1, and HIV-1 derived ssRNA sequences activate the
RT NLRP3 inflammasome in human macrophages through a non-classical pathway.";
RL IScience 1:102295-102295(2021).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-827 IN COMPLEXES WITH
RP RESIQUIMOD AND OTHER SYNTHETIC AGONISTS, FUNCTION, SUBUNIT, LEUCINE-RICH
RP REPEATS, MUTAGENESIS OF TYR-348; VAL-378; PHE-405; VAL-520; ASP-543 AND
RP THR-574, GLYCOSYLATION AT ASN-293; ASN-395; ASN-511; ASN-546; ASN-590;
RP ASN-640 AND ASN-680, AND DISULFIDE BONDS.
RX PubMed=23520111; DOI=10.1126/science.1229159;
RA Tanji H., Ohto U., Shibata T., Miyake K., Shimizu T.;
RT "Structural reorganization of the Toll-like receptor 8 dimer induced by
RT agonistic ligands.";
RL Science 339:1426-1429(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-827 IN COMPLEX WITH URIDINE,
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF TYR-348;
RP PHE-405; ASP-543 AND THR-574.
RX PubMed=25599397; DOI=10.1038/nsmb.2943;
RA Tanji H., Ohto U., Shibata T., Taoka M., Yamauchi Y., Isobe T., Miyake K.,
RA Shimizu T.;
RT "Toll-like receptor 8 senses degradation products of single-stranded RNA.";
RL Nat. Struct. Mol. Biol. 22:109-115(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 27-827, SUBUNIT, MUTAGENESIS OF
RP 452-ARG--ARG-455, CLEAVAGE, AND ACTIVITY REGULATION.
RX PubMed=26929371; DOI=10.1073/pnas.1516000113;
RA Tanji H., Ohto U., Motoi Y., Shibata T., Miyake K., Shimizu T.;
RT "Autoinhibition and relief mechanism by the proteolytic processing of Toll-
RT like receptor 8.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:3012-3017(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 27-827, SUBUNIT, AND FUNCTION.
RX PubMed=29155428; DOI=10.1038/nchembio.2518;
RA Zhang S., Hu Z., Tanji H., Jiang S., Das N., Li J., Sakaniwa K., Jin J.,
RA Bian Y., Ohto U., Shimizu T., Yin H.;
RT "Small-molecule inhibition of TLR8 through stabilization of its resting
RT state.";
RL Nat. Chem. Biol. 14:58-64(2018).
CC -!- FUNCTION: Endosomal receptor that plays a key role in innate and
CC adaptive immunity (PubMed:25297876, PubMed:32433612). Controls host
CC immune response against pathogens through recognition of RNA
CC degradation products specific to microorganisms that are initially
CC processed by RNASET2 (PubMed:31778653). Recognizes GU-rich single-
CC stranded RNA (GU-rich RNA) derived from SARS-CoV-2, SARS-CoV-1 and HIV-
CC 1 viruses (PubMed:33718825). Upon binding to agonists, undergoes
CC dimerization that brings TIR domains from the two molecules into direct
CC contact, leading to the recruitment of TIR-containing downstream
CC adapter MYD88 through homotypic interaction (PubMed:23520111,
CC PubMed:25599397, PubMed:26929371, PubMed:33718825). In turn, the
CC Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6,
CC TRAF3 leading to activation of downstream transcription factors NF-
CC kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons,
CC respectively (PubMed:16737960, PubMed:17932028, PubMed:29155428).
CC {ECO:0000269|PubMed:16737960, ECO:0000269|PubMed:17932028,
CC ECO:0000269|PubMed:23520111, ECO:0000269|PubMed:25297876,
CC ECO:0000269|PubMed:25599397, ECO:0000269|PubMed:26929371,
CC ECO:0000269|PubMed:29155428, ECO:0000269|PubMed:31778653,
CC ECO:0000269|PubMed:32433612, ECO:0000269|PubMed:33718825}.
CC -!- ACTIVITY REGULATION: Activated by RNAs having enough uridines.
CC {ECO:0000269|PubMed:25599397, ECO:0000269|PubMed:26929371}.
CC -!- SUBUNIT: Homodimer (PubMed:23520111, PubMed:25599397, PubMed:26929371,
CC PubMed:29155428). Interacts with MYD88 via their respective TIR domains
CC (Probable). Interacts with UNC93B1 (By similarity). Interacts with BTK
CC (PubMed:17932028). Interacts with SMPDL3B (By similarity).
CC {ECO:0000250|UniProtKB:P58682, ECO:0000269|PubMed:17932028,
CC ECO:0000269|PubMed:23520111, ECO:0000269|PubMed:25599397,
CC ECO:0000269|PubMed:26929371, ECO:0000269|PubMed:29155428, ECO:0000305}.
CC -!- INTERACTION:
CC Q9NR97-1; Q9NR97-1: TLR8; NbExp=4; IntAct=EBI-16041685, EBI-16041685;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:25297876};
CC Single-pass type I membrane protein {ECO:0000250}. Note=Endosomal
CC localization confers distinctive proteolytic processing.
CC {ECO:0000269|PubMed:25297876}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR97-2; Sequence=VSP_053412;
CC -!- TISSUE SPECIFICITY: Expressed in myeloid dendritic cells, monocytes,
CC and monocyte-derived dendritic cells. {ECO:0000269|PubMed:33718825}.
CC -!- PTM: Ubiquitinated by RNF216; leading to degradation by the proteasome.
CC {ECO:0000269|PubMed:31385713}.
CC -!- PTM: Proteolytic processing occurs in monocytes and monocyte-derived
CC macrophages by both furin-like proprotein convertase and cathepsins
CC (PubMed:25297876). The cleavage is necessary for dimer formation and
CC subsequent activation (PubMed:26929371). {ECO:0000269|PubMed:25297876,
CC ECO:0000269|PubMed:26929371}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; AF246971; AAF64061.1; -; mRNA.
DR EMBL; AF245703; AAF78036.1; -; mRNA.
DR EMBL; AB445666; BAG55063.1; -; mRNA.
DR EMBL; DQ023132; AAZ95433.1; -; Genomic_DNA.
DR EMBL; DQ023133; AAZ95434.1; -; Genomic_DNA.
DR EMBL; DQ023134; AAZ95435.1; -; Genomic_DNA.
DR EMBL; DQ023135; AAZ95436.1; -; Genomic_DNA.
DR EMBL; DQ023136; AAZ95437.1; -; Genomic_DNA.
DR EMBL; DQ023137; AAZ95438.1; -; Genomic_DNA.
DR EMBL; DQ023138; AAZ95439.1; -; Genomic_DNA.
DR EMBL; DQ023139; AAZ95440.1; -; Genomic_DNA.
DR EMBL; DQ023140; AAZ95441.1; -; Genomic_DNA.
DR EMBL; CH471074; EAW98808.1; -; Genomic_DNA.
DR EMBL; AY358296; AAQ88663.1; -; mRNA.
DR EMBL; AC005859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98809.1; -; Genomic_DNA.
DR EMBL; BC101076; AAI01077.1; -; mRNA.
DR EMBL; BC101077; AAI01078.1; -; mRNA.
DR CCDS; CCDS14152.1; -. [Q9NR97-1]
DR CCDS; CCDS14153.1; -. [Q9NR97-2]
DR RefSeq; NP_057694.2; NM_016610.3. [Q9NR97-2]
DR RefSeq; NP_619542.1; NM_138636.5. [Q9NR97-1]
DR RefSeq; XP_011543831.1; XM_011545529.1. [Q9NR97-2]
DR RefSeq; XP_011543832.1; XM_011545530.2. [Q9NR97-2]
DR PDB; 3W3G; X-ray; 2.30 A; A/B=27-827.
DR PDB; 3W3J; X-ray; 2.00 A; A/B=27-827.
DR PDB; 3W3K; X-ray; 2.30 A; A/B=27-827.
DR PDB; 3W3L; X-ray; 2.33 A; A/B/C/D=27-827.
DR PDB; 3W3M; X-ray; 2.70 A; A=27-827.
DR PDB; 3W3N; X-ray; 2.10 A; A/B=27-827.
DR PDB; 3WN4; X-ray; 1.81 A; A=27-827.
DR PDB; 4QBZ; X-ray; 2.00 A; A/B=27-827.
DR PDB; 4QC0; X-ray; 2.10 A; A/B=27-827.
DR PDB; 4R07; X-ray; 2.00 A; A/B/C/D=27-827.
DR PDB; 4R08; X-ray; 2.40 A; A/B/C/D=27-827.
DR PDB; 4R09; X-ray; 2.62 A; A/B/C/D=27-827.
DR PDB; 4R0A; X-ray; 1.90 A; A=27-827.
DR PDB; 4R6A; X-ray; 2.10 A; A/B=27-827.
DR PDB; 5AWA; X-ray; 2.20 A; A=27-827.
DR PDB; 5AWB; X-ray; 2.10 A; A=27-827.
DR PDB; 5AWC; X-ray; 2.50 A; A/B/C/D=27-827.
DR PDB; 5AWD; X-ray; 2.05 A; A=27-827.
DR PDB; 5AZ5; X-ray; 2.40 A; A/B/C/D=27-827.
DR PDB; 5HDH; X-ray; 2.60 A; A=27-827.
DR PDB; 5WYX; X-ray; 2.40 A; A/B=27-827.
DR PDB; 5WYZ; X-ray; 2.30 A; A/B=27-827.
DR PDB; 5Z14; X-ray; 2.80 A; A/B=27-827.
DR PDB; 5Z15; X-ray; 2.90 A; A/B=27-827.
DR PDB; 6KYA; X-ray; 2.89 A; A/B=27-827.
DR PDB; 6TY5; X-ray; 2.79 A; A/B=27-827.
DR PDB; 6V9U; X-ray; 2.65 A; A/B=27-827.
DR PDB; 6WML; X-ray; 2.50 A; A/B/C/D=27-827.
DR PDB; 6ZJZ; X-ray; 2.49 A; A/B=27-827.
DR PDB; 7CRF; X-ray; 2.89 A; A/B=27-827.
DR PDB; 7R52; X-ray; 2.94 A; A/B=27-827.
DR PDB; 7R53; X-ray; 3.12 A; A/B=27-827.
DR PDB; 7R54; X-ray; 2.84 A; A/B=27-827.
DR PDBsum; 3W3G; -.
DR PDBsum; 3W3J; -.
DR PDBsum; 3W3K; -.
DR PDBsum; 3W3L; -.
DR PDBsum; 3W3M; -.
DR PDBsum; 3W3N; -.
DR PDBsum; 3WN4; -.
DR PDBsum; 4QBZ; -.
DR PDBsum; 4QC0; -.
DR PDBsum; 4R07; -.
DR PDBsum; 4R08; -.
DR PDBsum; 4R09; -.
DR PDBsum; 4R0A; -.
DR PDBsum; 4R6A; -.
DR PDBsum; 5AWA; -.
DR PDBsum; 5AWB; -.
DR PDBsum; 5AWC; -.
DR PDBsum; 5AWD; -.
DR PDBsum; 5AZ5; -.
DR PDBsum; 5HDH; -.
DR PDBsum; 5WYX; -.
DR PDBsum; 5WYZ; -.
DR PDBsum; 5Z14; -.
DR PDBsum; 5Z15; -.
DR PDBsum; 6KYA; -.
DR PDBsum; 6TY5; -.
DR PDBsum; 6V9U; -.
DR PDBsum; 6WML; -.
DR PDBsum; 6ZJZ; -.
DR PDBsum; 7CRF; -.
DR PDBsum; 7R52; -.
DR PDBsum; 7R53; -.
DR PDBsum; 7R54; -.
DR AlphaFoldDB; Q9NR97; -.
DR SMR; Q9NR97; -.
DR BioGRID; 119462; 4.
DR DIP; DIP-61413N; -.
DR IntAct; Q9NR97; 7.
DR STRING; 9606.ENSP00000312082; -.
DR BindingDB; Q9NR97; -.
DR ChEMBL; CHEMBL5805; -.
DR DrugBank; DB16580; Afimetoran.
DR DrugBank; DB00724; Imiquimod.
DR DrugBank; DB06530; Resiquimod.
DR GuidetoPHARMACOLOGY; 1758; -.
DR GlyGen; Q9NR97; 24 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NR97; -.
DR PhosphoSitePlus; Q9NR97; -.
DR BioMuta; TLR8; -.
DR DMDM; 20140873; -.
DR CPTAC; CPTAC-2235; -.
DR jPOST; Q9NR97; -.
DR MassIVE; Q9NR97; -.
DR PaxDb; Q9NR97; -.
DR PeptideAtlas; Q9NR97; -.
DR PRIDE; Q9NR97; -.
DR ProteomicsDB; 12724; -.
DR ProteomicsDB; 82313; -. [Q9NR97-1]
DR Antibodypedia; 458; 874 antibodies from 43 providers.
DR DNASU; 51311; -.
DR Ensembl; ENST00000218032.7; ENSP00000218032.7; ENSG00000101916.12. [Q9NR97-1]
DR Ensembl; ENST00000311912.5; ENSP00000312082.5; ENSG00000101916.12. [Q9NR97-2]
DR GeneID; 51311; -.
DR KEGG; hsa:51311; -.
DR MANE-Select; ENST00000218032.7; ENSP00000218032.7; NM_138636.5; NP_619542.1.
DR UCSC; uc004cvd.4; human. [Q9NR97-1]
DR CTD; 51311; -.
DR DisGeNET; 51311; -.
DR GeneCards; TLR8; -.
DR HGNC; HGNC:15632; TLR8.
DR HPA; ENSG00000101916; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 300366; gene.
DR neXtProt; NX_Q9NR97; -.
DR OpenTargets; ENSG00000101916; -.
DR PharmGKB; PA38009; -.
DR VEuPathDB; HostDB:ENSG00000101916; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000160879; -.
DR HOGENOM; CLU_006000_2_0_1; -.
DR InParanoid; Q9NR97; -.
DR OMA; HDIACLN; -.
DR OrthoDB; 1235561at2759; -.
DR PhylomeDB; Q9NR97; -.
DR TreeFam; TF351113; -.
DR PathwayCommons; Q9NR97; -.
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-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q9NR97; -.
DR SIGNOR; Q9NR97; -.
DR BioGRID-ORCS; 51311; 12 hits in 701 CRISPR screens.
DR ChiTaRS; TLR8; human.
DR GeneWiki; TLR8; -.
DR GenomeRNAi; 51311; -.
DR Pharos; Q9NR97; Tchem.
DR PRO; PR:Q9NR97; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NR97; protein.
DR Bgee; ENSG00000101916; Expressed in monocyte and 124 other tissues.
DR Genevisible; Q9NR97; HS.
DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0038187; F:pattern recognition receptor activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA: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:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; TAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:CAFA.
DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:UniProtKB.
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:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:CAFA.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0034158; P:toll-like receptor 8 signaling pathway; IDA:UniProtKB.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR027175; TLR8.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR47410:SF1; PTHR47410:SF1; 1.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 15.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 20.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Endosome; Glycoprotein;
KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1041
FT /note="Toll-like receptor 8"
FT /id="PRO_0000034735"
FT TOPO_DOM 27..827
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 849..1041
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 126..147
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 148..168
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 171..193
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 202..223
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 224..244
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 247..268
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 288..309
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 312..334
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 338..360
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 368..389
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 395..416
FT /note="LRR 11"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 419..440
FT /note="LRR 12"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 482..503
FT /note="LRR 13"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 506..527
FT /note="LRR 14"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 531..551
FT /note="LRR 15"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 555..577
FT /note="LRR 16"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 585..606
FT /note="LRR 17"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 609..630
FT /note="LRR 18"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 640..661
FT /note="LRR 19"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 665..685
FT /note="LRR 20"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 689..710
FT /note="LRR 21"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 713..734
FT /note="LRR 22"
FT /evidence="ECO:0000269|PubMed:23520111"
FT REPEAT 737..758
FT /note="LRR 23"
FT /evidence="ECO:0000269|PubMed:23520111"
FT DOMAIN 772..824
FT /note="LRRCT"
FT DOMAIN 878..1022
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23520111"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..49
FT /evidence="ECO:0000269|PubMed:23520111"
FT DISULFID 181..187
FT /evidence="ECO:0000269|PubMed:23520111"
FT DISULFID 257..270
FT /evidence="ECO:0000269|PubMed:23520111"
FT DISULFID 260..267
FT /evidence="ECO:0000269|PubMed:23520111"
FT DISULFID 479..509
FT /evidence="ECO:0000269|PubMed:23520111"
FT DISULFID 776..803
FT /evidence="ECO:0000269|PubMed:23520111"
FT VAR_SEQ 1
FT /note="M -> MKESSLQNSSCSLGKETKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11022119"
FT /id="VSP_053412"
FT VARIANT 10
FT /note="M -> V (in dbSNP:rs5744077)"
FT /id="VAR_024667"
FT VARIANT 715
FT /note="R -> Q (in dbSNP:rs5744082)"
FT /id="VAR_052363"
FT MUTAGEN 348
FT /note="Y->A: Abolishes activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:23520111"
FT MUTAGEN 348
FT /note="Y->A: Abolishes responses to both ssRNA and chemical
FT ligands."
FT /evidence="ECO:0000269|PubMed:25599397"
FT MUTAGEN 378
FT /note="V->A: Increases activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:23520111"
FT MUTAGEN 405
FT /note="F->A: Abolishes activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:23520111"
FT MUTAGEN 405
FT /note="F->A: Abolishes responses to both ssRNA and chemical
FT ligands."
FT /evidence="ECO:0000269|PubMed:25599397"
FT MUTAGEN 452..455
FT /note="RKRR->NQSN: Monomeric and inactive."
FT /evidence="ECO:0000269|PubMed:26929371"
FT MUTAGEN 520
FT /note="V->A: Strongly decreases activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:23520111"
FT MUTAGEN 543
FT /note="D->A: Abolishes activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:23520111"
FT MUTAGEN 543
FT /note="D->A: Abolishes responses to both ssRNA and chemical
FT ligands."
FT /evidence="ECO:0000269|PubMed:25599397"
FT MUTAGEN 574
FT /note="T->A: Abolishes responses to both ssRNA and chemical
FT ligands."
FT /evidence="ECO:0000269|PubMed:25599397"
FT MUTAGEN 574
FT /note="T->A: Strongly decreases activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:23520111"
FT CONFLICT 217
FT /note="P -> S (in Ref. 1; AAF64061)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> V (in Ref. 5; AAQ88663)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="L -> P (in Ref. 1; AAF64061)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="D -> N (in Ref. 4; AAZ95439)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="V -> I (in Ref. 1; AAF64061)"
FT /evidence="ECO:0000305"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4R0A"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 80..85
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3W3J"
FT TURN 118..123
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5WYX"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6ZJZ"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 280..285
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3W3K"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:6ZJZ"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3W3N"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:4R07"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6V9U"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6ZJZ"
FT TURN 498..503
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 525..528
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 547..552
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:3W3G"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:5WYZ"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 620..623
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:5HDH"
FT TURN 630..637
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:3W3M"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 681..686
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 729..733
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:5AZ5"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 753..756
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 765..768
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 781..789
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:4R0A"
FT HELIX 798..800
FT /evidence="ECO:0007829|PDB:3WN4"
FT STRAND 801..806
FT /evidence="ECO:0007829|PDB:3WN4"
FT TURN 807..811
FT /evidence="ECO:0007829|PDB:3WN4"
FT HELIX 814..816
FT /evidence="ECO:0007829|PDB:4QBZ"
FT HELIX 819..821
FT /evidence="ECO:0007829|PDB:6ZJZ"
SQ SEQUENCE 1041 AA; 119828 MW; 39A38B60629291C8 CRC64;
MENMFLQSSM LTCIFLLISG SCELCAEENF SRSYPCDEKK QNDSVIAECS NRRLQEVPQT
VGKYVTELDL SDNFITHITN ESFQGLQNLT KINLNHNPNV QHQNGNPGIQ SNGLNITDGA
FLNLKNLREL LLEDNQLPQI PSGLPESLTE LSLIQNNIYN ITKEGISRLI NLKNLYLAWN
CYFNKVCEKT NIEDGVFETL TNLELLSLSF NSLSHVPPKL PSSLRKLFLS NTQIKYISEE
DFKGLINLTL LDLSGNCPRC FNAPFPCVPC DGGASINIDR FAFQNLTQLR YLNLSSTSLR
KINAAWFKNM PHLKVLDLEF NYLVGEIASG AFLTMLPRLE ILDLSFNYIK GSYPQHINIS
RNFSKLLSLR ALHLRGYVFQ ELREDDFQPL MQLPNLSTIN LGINFIKQID FKLFQNFSNL
EIIYLSENRI SPLVKDTRQS YANSSSFQRH IRKRRSTDFE FDPHSNFYHF TRPLIKPQCA
AYGKALDLSL NSIFFIGPNQ FENLPDIACL NLSANSNAQV LSGTEFSAIP HVKYLDLTNN
RLDFDNASAL TELSDLEVLD LSYNSHYFRI AGVTHHLEFI QNFTNLKVLN LSHNNIYTLT
DKYNLESKSL VELVFSGNRL DILWNDDDNR YISIFKGLKN LTRLDLSLNR LKHIPNEAFL
NLPASLTELH INDNMLKFFN WTLLQQFPRL ELLDLRGNKL LFLTDSLSDF TSSLRTLLLS
HNRISHLPSG FLSEVSSLKH LDLSSNLLKT INKSALETKT TTKLSMLELH GNPFECTCDI
GDFRRWMDEH LNVKIPRLVD VICASPGDQR GKSIVSLELT TCVSDVTAVI LFFFTFFITT
MVMLAALAHH LFYWDVWFIY NVCLAKVKGY RSLSTSQTFY DAYISYDTKD ASVTDWVINE
LRYHLEESRD KNVLLCLEER DWDPGLAIID NLMQSINQSK KTVFVLTKKY AKSWNFKTAF
YLALQRLMDE NMDVIIFILL EPVLQHSQYL RLRQRICKSS ILQWPDNPKA EGLFWQTLRN
VVLTENDSRY NNMYVDSIKQ Y
