TLR11_MOUSE
ID TLR11_MOUSE Reviewed; 926 AA.
AC Q6R5P0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Toll-like receptor 11 {ECO:0000303|PubMed:14993594};
DE AltName: Full=Toll-like receptor 12 {ECO:0000305};
DE Flags: Precursor;
GN Name=Tlr11 {ECO:0000303|PubMed:14993594, ECO:0000312|MGI:MGI:3045226};
GN Synonyms=Gm287 {ECO:0000312|MGI:MGI:3045226}, Tlr12 {ECO:0000305};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=14993594; DOI=10.1073/pnas.0400525101;
RA Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S.,
RA Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.;
RT "Toll-like receptors 9 and 3 as essential components of innate immune
RT defense against mouse cytomegalovirus infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004).
RN [2]
RP INTERACTION WITH HSP90B1.
RX PubMed=20865800; DOI=10.1038/ncomms1070;
RA Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B.,
RA Bona R., Han D., Li Z.;
RT "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
RT substrate-specific cochaperone.";
RL Nat. Commun. 1:79-79(2010).
RN [3]
RP ERRATUM OF PUBMED:20865800.
RA Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B.,
RA Bona R., Han D., Li Z.;
RL Nat. Commun. 3:653-653(2012).
CC -!- FUNCTION: Participates in the innate immune response to microbial
CC agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation,
CC cytokine secretion and the inflammatory response.
CC {ECO:0000250|UniProtKB:Q6QNU9}.
CC -!- SUBUNIT: Binds MYD88 via their respective TIR domains (By similarity).
CC Interacts with HSP90B1; this interaction is required for proper folding
CC in the endoplasmic reticulum (PubMed:20865800).
CC {ECO:0000250|UniProtKB:Q9EQU3, ECO:0000269|PubMed:20865800}.
CC -!- INTERACTION:
CC Q6R5P0; A0A0H3NMJ6: fliC; Xeno; NbExp=2; IntAct=EBI-6548549, EBI-6548383;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
CC -!- CAUTION: There is some confusion regarding the nomenclature of this
CC gene. In the literature, Tlr11 is frequently referred to as Tlr12 and
CC vice-versa. {ECO:0000305}.
CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has
CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite
CC the presence of the catalytic Asp residue, the isolated TIR domain of
CC human TLR4 lacks NADase activity (By similarity). Based on this, it is
CC unlikely that Toll-like receptors have NADase activity.
CC {ECO:0000250|UniProtKB:O00206, ECO:0000305}.
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DR EMBL; AY510704; AAS37672.1; -; mRNA.
DR RefSeq; NP_991388.2; NM_205819.3.
DR AlphaFoldDB; Q6R5P0; -.
DR SMR; Q6R5P0; -.
DR BioGRID; 232041; 3.
DR IntAct; Q6R5P0; 4.
DR STRING; 10090.ENSMUSP00000068906; -.
DR GlyGen; Q6R5P0; 9 sites.
DR PaxDb; Q6R5P0; -.
DR PRIDE; Q6R5P0; -.
DR ProteomicsDB; 259205; -.
DR DNASU; 239081; -.
DR Ensembl; ENSMUST00000063570; ENSMUSP00000068906; ENSMUSG00000051969.
DR GeneID; 239081; -.
DR KEGG; mmu:239081; -.
DR UCSC; uc007tkz.3; mouse.
DR CTD; 239081; -.
DR MGI; MGI:3045226; Tlr11.
DR VEuPathDB; HostDB:ENSMUSG00000051969; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000163623; -.
DR HOGENOM; CLU_318753_0_0_1; -.
DR InParanoid; Q6R5P0; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q6R5P0; -.
DR TreeFam; TF351113; -.
DR BioGRID-ORCS; 239081; 0 hits in 70 CRISPR screens.
DR PRO; PR:Q6R5P0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6R5P0; protein.
DR Bgee; ENSMUSG00000051969; Expressed in spleen and 14 other tissues.
DR ExpressionAtlas; Q6R5P0; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
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; -; 4.
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; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 10.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Leucine-rich repeat; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..926
FT /note="Toll-like receptor 11"
FT /id="PRO_0000042793"
FT TOPO_DOM 31..721
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 240..263
FT /note="LRR 1"
FT REPEAT 264..286
FT /note="LRR 2"
FT REPEAT 288..309
FT /note="LRR 3"
FT REPEAT 313..334
FT /note="LRR 4"
FT REPEAT 337..358
FT /note="LRR 5"
FT REPEAT 362..383
FT /note="LRR 6"
FT REPEAT 386..407
FT /note="LRR 7"
FT REPEAT 410..433
FT /note="LRR 8"
FT REPEAT 434..455
FT /note="LRR 9"
FT REPEAT 458..479
FT /note="LRR 10"
FT DOMAIN 772..922
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 926 AA; 105873 MW; DF86FED308671285 CRC64;
MPRMERHQFC SVLLILILLT LVSLTLTGWA WTIPDCIIAD SLLFPNLSYY IPFCTSAPGL
HLLASCSNVK NLNQTLKRVP RNTEVLCLQG MVPTLPAKAF IRFHSLQLLR LQLRTTSVTS
RTFQGLDQLQ YLFFDHHAPC CLSLFLSPNC FESLRSLSSL SFQGYCLTYS QSIYLPTSLR
HLTLRNSCLT KFQDLQRLFP DLLLSTSSTP NIKPGAPFLE TLDLSYNLQL KQAGVRDLYG
LTLHSLILDG TPLKALDLTD SGLLHLHFLS LVGTGIEKVP ASLTGYSELR ALDLGKNQIQ
NILENGEIPG YKALEFLSLH DNHLQTLPTR FLHTLPQLQK LNLSMNKLGP ILELPEGLFS
TNLKVLDLSY NQLCDVPHGA LSLLSQLQEL WLSGNNISSL SNESLQGLRQ LRTLDLSWNQ
IKVLKPGWLS HLPALTTLNL LGTYLEYILG IQLQGPKMLR HLQLGSYPIL DIYPPWPPTL
LSLEIQAESC IQFMIHSGQP FLFLENLTLE TSILLLKPDN ITIHFPSLRR LTLRGYSFIF
STSQLQRFFP QQLPLLEHFF IWCENSYAVD LYLFGMPRLR VLELGYLNFF YESSTMKLEM
LLKEVPQLQV LALSHLNLRN LSVSSFKSLQ DLKLLLFNSE RALEMNSNLQ EFIPQMPQYV
YFSDVTFTCQ CEASWLESWA TRAPNTFVYG LEKSICIANA SDYSKTLLFS FLATNCPHGT
EFWGFLTSFI LLLLLIILPL ISCPKWSWLH HLWTLFHTCW WKLCGHRLRG QFNYDVFISY
CEEDQAWVLE ELVPVLEKAP PEGEGLRLCL PARDFGIGND RMESMIASMG KSRATLCVLT
GQALASPWCN LELRLATYHL VARPGTTHLL LLFLEPLDRQ RLHSYHRLSR WLQKEDYFDL
SQGKVEWNSF CEQLKRRLSK AGQERD
