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Protein

Toll-like receptor 13

Gene

Tlr13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of innate and adaptive immunity that recognizes and binds 23S rRNA from bacteria. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Specifically binds the 5'-CGGAAAGACC-3' sequence on bacterial 23S rRNA, a sequence also bound by MLS group antibiotics (including erythromycin). May also recognize vesicular stomatitis virus; however, these data require additional evidences.3 Publications

GO - Molecular functioni

  • double-stranded RNA binding Source: GO_Central
  • protein homodimerization activity Source: MGI
  • rRNA binding Source: UniProtKB

GO - Biological processi

  • defense response to other organism Source: GO_Central
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB
  • MyD88-dependent toll-like receptor signaling pathway Source: MGI
  • regulation of MAPK cascade Source: MGI
  • response to virus Source: MGI
  • toll-like receptor 13 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 13
Gene namesi
Name:Tlr13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:3045213. Tlr13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini69 – 783715ExtracellularSequence analysisAdd
BLAST
Transmembranei784 – 80421HelicalSequence analysisAdd
BLAST
Topological domaini805 – 991187CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • endosome Source: UniProtKB
  • endosome membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 6868Sequence analysisAdd
BLAST
Chaini69 – 991923Toll-like receptor 13PRO_0000042795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence analysis
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence analysis
Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence analysis
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence analysis
Glycosylationi644 – 6441N-linked (GlcNAc...)Sequence analysis
Glycosylationi663 – 6631N-linked (GlcNAc...)Sequence analysis
Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence analysis
Glycosylationi742 – 7421N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6R5N8.
PaxDbiQ6R5N8.
PeptideAtlasiQ6R5N8.
PRIDEiQ6R5N8.

PTM databases

iPTMnetiQ6R5N8.
PhosphoSiteiQ6R5N8.

Expressioni

Gene expression databases

BgeeiQ6R5N8.
CleanExiMM_TLR13.
GenevisibleiQ6R5N8. MM.

Interactioni

Subunit structurei

Binds MYD88 via their respective TIR domains (By similarity). Interacts with UNC93B1.By similarity1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

DIPiDIP-61832N.
MINTiMINT-4997493.
STRINGi10090.ENSMUSP00000043101.

Structurei

Secondary structure

1
991
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi75 – 773Combined sources
Beta strandi80 – 856Combined sources
Helixi94 – 985Combined sources
Beta strandi107 – 1093Combined sources
Turni120 – 1256Combined sources
Beta strandi131 – 1333Combined sources
Turni144 – 1496Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi178 – 1803Combined sources
Turni191 – 1966Combined sources
Beta strandi202 – 2043Combined sources
Helixi213 – 2208Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi298 – 3003Combined sources
Helixi308 – 3103Combined sources
Helixi313 – 3164Combined sources
Beta strandi321 – 3233Combined sources
Helixi329 – 3313Combined sources
Helixi336 – 3438Combined sources
Beta strandi351 – 3533Combined sources
Helixi361 – 37010Combined sources
Beta strandi374 – 3774Combined sources
Turni391 – 3944Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi424 – 4263Combined sources
Turni437 – 4426Combined sources
Beta strandi448 – 4503Combined sources
Helixi461 – 4644Combined sources
Beta strandi472 – 4743Combined sources
Beta strandi496 – 4983Combined sources
Turni509 – 5146Combined sources
Beta strandi520 – 5223Combined sources
Turni533 – 5386Combined sources
Beta strandi544 – 5463Combined sources
Turni557 – 5626Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi578 – 5803Combined sources
Turni588 – 5914Combined sources
Beta strandi597 – 5993Combined sources
Turni612 – 6176Combined sources
Beta strandi623 – 6253Combined sources
Beta strandi632 – 6343Combined sources
Turni638 – 6414Combined sources
Beta strandi647 – 6493Combined sources
Helixi656 – 6594Combined sources
Beta strandi660 – 6623Combined sources
Turni664 – 6696Combined sources
Beta strandi675 – 6773Combined sources
Beta strandi699 – 7013Combined sources
Turni712 – 7176Combined sources
Beta strandi723 – 7253Combined sources
Helixi735 – 7373Combined sources
Helixi738 – 7469Combined sources
Helixi755 – 7573Combined sources
Helixi769 – 7713Combined sources
Helixi774 – 7763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Z0CX-ray2.30A/D69-777[»]
ProteinModelPortaliQ6R5N8.
SMRiQ6R5N8. Positions 69-975.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati104 – 12522LRR 1Add
BLAST
Repeati128 – 14922LRR 2Add
BLAST
Repeati152 – 17423LRR 3Add
BLAST
Repeati175 – 19622LRR 4Add
BLAST
Repeati199 – 22022LRR 5Add
BLAST
Repeati225 – 24622LRR 6Add
BLAST
Repeati248 – 26821LRR 7Add
BLAST
Repeati271 – 29222LRR 8Add
BLAST
Repeati295 – 31521LRR 9Add
BLAST
Repeati318 – 33821LRR 10Add
BLAST
Repeati348 – 36821LRR 11Add
BLAST
Repeati372 – 39423LRR 12Add
BLAST
Repeati397 – 41822LRR 13Add
BLAST
Repeati421 – 44222LRR 14Add
BLAST
Repeati445 – 46622LRR 15Add
BLAST
Repeati469 – 49022LRR 16Add
BLAST
Repeati493 – 51422LRR 17Add
BLAST
Repeati517 – 53822LRR 18Add
BLAST
Repeati541 – 56222LRR 19Add
BLAST
Repeati565 – 58521LRR 20Add
BLAST
Repeati594 – 61724LRR 21Add
BLAST
Repeati620 – 64122LRR 22Add
BLAST
Repeati644 – 66522LRR 23Add
BLAST
Repeati672 – 69322LRR 24Add
BLAST
Repeati696 – 71621LRR 25Add
BLAST
Domaini729 – 77951LRRCTAdd
BLAST
Domaini832 – 978147TIRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 25 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000203220.
HOVERGENiHBG094977.
InParanoidiQ6R5N8.
KOiK18808.
OMAiVEKENTH.
OrthoDBiEOG76471Z.
PhylomeDBiQ6R5N8.
TreeFamiTF325595.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 6 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 5 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 18 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 18 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6R5N8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLYRILVQ LEQSPYVKTV PLNMRRDFFF LVVTWMPKTV KMNGSSFVPS
60 70 80 90 100
LQLLLMLVGF SLPPVAETYG FNKCTQYEFD IHHVLCIRKK ITNLTEAISD
110 120 130 140 150
IPRYTTHLNL THNEIQVLPP WSFTNLSALV DLRLEWNSIW KIDEGAFRGL
160 170 180 190 200
ENLTLLNLVE NKIQSVNNSF EGLSSLKTLL LSHNQITHIH KDAFTPLIKL
210 220 230 240 250
KYLSLSRNNI SDFSGILEAV QHLPCLERLD LTNNSIMYLD HSPRSLVSLT
260 270 280 290 300
HLSFEGNKLR ELNFSALSLP NLTNLSASRN GNKVIQNVYL KTLPQLKSLN
310 320 330 340 350
LSGTVIKLEN LSAKHLQNLR AMDLSNWELR HGHLDMKTVC HLLGNLPKLE
360 370 380 390 400
TLVFQKNVTN AEGIKQLAKC TRLLFLDLGQ NSDLIYLNDS EFNALPSLQK
410 420 430 440 450
LNLNKCQLSF INNRTWSSLQ NLTSLDLSHN KFKSFPDFAF SPLKHLEFLS
460 470 480 490 500
LSRNPITELN NLAFSGLFAL KELNLAACWI VTIDRYSFTQ FPNLEVLDLG
510 520 530 540 550
DNNIRTLNHG TFRPLKKLQS LILSHNCLKI LEPNSFSGLT NLRSLDLMYN
560 570 580 590 600
SLSYFHEHLF SGLEKLLILK LGFNKITYET TRTLQYPPFI KLKSLKQLNL
610 620 630 640 650
EGQRHGIQVV PSNFFQGLGS LQELLLGKNP SVFLDHHQFD PLINLTKLDI
660 670 680 690 700
SGTKDGDRSL YLNASLFQNL KRLKILRLEN NNLESLVPDM FSSLQSLQVF
710 720 730 740 750
SLRFNNLKVI NQSHLKNLKS LMFFDVYGNK LQCTCDNLWF KNWSMNTEEV
760 770 780 790 800
HIPFLRSYPC QQPGSQSLLI DFDDAMCNFD LGKVYFLCSF SMVLSTMVFS
810 820 830 840 850
WFSTKMIASL WYGLYICRAW YLTKWHKTEK KFLYDAFVSF SATDEAWVYK
860 870 880 890 900
ELVPALEQGS QTTFKLCLHQ RDFEPGIDIF ENIQNAINTS RKTLCVVSNH
910 920 930 940 950
YLHSEWCRLE VQLASMKMFY EHKDVIILIF LEEIPNYKLS SYHRLRKLIN
960 970 980 990
KQTFITWPDS VHQQPLFWAR IRNALGKETV EKENTHLIVV E
Length:991
Mass (Da):114,443
Last modified:July 5, 2004 - v1
Checksum:i6FB622DC62F37E74
GO

Sequence cautioni

The sequence BAE41528.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY510706 mRNA. Translation: AAS37674.1.
AK170044 mRNA. Translation: BAE41528.1. Different initiation.
AL672288 Genomic DNA. Translation: CAM16892.1.
CH466564 Genomic DNA. Translation: EDL14060.1.
BC117913 mRNA. Translation: AAI17914.1.
BC117914 mRNA. Translation: AAI17915.1.
CCDSiCCDS30338.1.
RefSeqiNP_991389.1. NM_205820.1.
UniGeneiMm.336203.

Genome annotation databases

EnsembliENSMUST00000040065; ENSMUSP00000043101; ENSMUSG00000033777.
GeneIDi279572.
KEGGimmu:279572.
UCSCiuc009ubn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY510706 mRNA. Translation: AAS37674.1.
AK170044 mRNA. Translation: BAE41528.1. Different initiation.
AL672288 Genomic DNA. Translation: CAM16892.1.
CH466564 Genomic DNA. Translation: EDL14060.1.
BC117913 mRNA. Translation: AAI17914.1.
BC117914 mRNA. Translation: AAI17915.1.
CCDSiCCDS30338.1.
RefSeqiNP_991389.1. NM_205820.1.
UniGeneiMm.336203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Z0CX-ray2.30A/D69-777[»]
ProteinModelPortaliQ6R5N8.
SMRiQ6R5N8. Positions 69-975.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61832N.
MINTiMINT-4997493.
STRINGi10090.ENSMUSP00000043101.

PTM databases

iPTMnetiQ6R5N8.
PhosphoSiteiQ6R5N8.

Proteomic databases

MaxQBiQ6R5N8.
PaxDbiQ6R5N8.
PeptideAtlasiQ6R5N8.
PRIDEiQ6R5N8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040065; ENSMUSP00000043101; ENSMUSG00000033777.
GeneIDi279572.
KEGGimmu:279572.
UCSCiuc009ubn.1. mouse.

Organism-specific databases

CTDi279572.
MGIiMGI:3045213. Tlr13.

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000203220.
HOVERGENiHBG094977.
InParanoidiQ6R5N8.
KOiK18808.
OMAiVEKENTH.
OrthoDBiEOG76471Z.
PhylomeDBiQ6R5N8.
TreeFamiTF325595.

Miscellaneous databases

PROiQ6R5N8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6R5N8.
CleanExiMM_TLR13.
GenevisibleiQ6R5N8. MM.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 6 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 5 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 18 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 18 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection."
    Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S., Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.
    Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-682.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling."
    Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.
    J. Cell Biol. 177:265-275(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UNC93B1.
  7. "A novel Toll-like receptor that recognizes vesicular stomatitis virus."
    Shi Z., Cai Z., Sanchez A., Zhang T., Wen S., Wang J., Yang J., Fu S., Zhang D.
    J. Biol. Chem. 286:4517-4524(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: FUNCTION, RNA-BINDING.
  9. Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTLR13_MOUSE
AccessioniPrimary (citable) accession number: Q6R5N8
Secondary accession number(s): Q148Y7, Q3TDS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence 23S rRNA from clinical isolates of erythromycin-resistant S.aureus is methylated and is not recognized by Tlr13 anymore, suggesting a link between antibiotic resistance and evasion from Tlr13 recognition. 23S rRNA modifications generating resistance toward MLS antibiotics preventing recognition of bacteria from Tlr13. These data may also explain why Tlr13 is not conserved in human: human may instead possess a related rRNA-sensing pattern recognition receptor that has evolved to recognize species that can hide from Tlr13 owing to rRNA modifications (PubMed:22821982).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.