TLR12_MOUSE
ID TLR12_MOUSE Reviewed; 906 AA.
AC Q6QNU9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Toll-like receptor 12 {ECO:0000303|PubMed:14993594};
DE AltName: Full=Toll-like receptor 11 {ECO:0000303|PubMed:15001781};
DE Flags: Precursor;
GN Name=Tlr12 {ECO:0000303|PubMed:14993594, ECO:0000312|MGI:MGI:3045221};
GN Synonyms=Gm1365 {ECO:0000312|MGI:MGI:3045221},
GN Tlr11 {ECO:0000303|PubMed:15001781};
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], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF PRO-804.
RC STRAIN=C57BL/6J;
RX PubMed=15001781; DOI=10.1126/science.1094351;
RA Zhang D., Zhang G., Hayden M.S., Greenblatt M.B., Bussey C., Flavell R.A.,
RA Ghosh S.;
RT "A toll-like receptor that prevents infection by uropathogenic bacteria.";
RL Science 303:1522-1526(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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. Plays a role in
CC preventing infection of internal organs of the urogenital system.
CC {ECO:0000269|PubMed:15001781}.
CC -!- SUBUNIT: Binds MYD88 via their respective TIR domains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Macrophages, liver, kidney and bladder epithelial
CC cells. {ECO:0000269|PubMed:15001781}.
CC -!- DISRUPTION PHENOTYPE: Has increased susceptibility to the uropathogenic
CC E.coli strain 8NU. Following infection, kidneys show a significantly
CC increased bacterial load and increased inflammatory response, whereas
CC bladder shows a similar response to wild type.
CC {ECO:0000269|PubMed:15001781}.
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, Tlr12 is frequently referred to as Tlr11 and
CC vice-versa. {ECO:0000305|PubMed:15001781}.
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; AY531552; AAS83531.1; -; mRNA.
DR EMBL; AY510705; AAS37673.1; -; mRNA.
DR EMBL; AK137624; BAE23434.1; -; mRNA.
DR CCDS; CCDS18673.1; -.
DR RefSeq; NP_991392.1; NM_205823.2.
DR AlphaFoldDB; Q6QNU9; -.
DR SMR; Q6QNU9; -.
DR STRING; 10090.ENSMUSP00000074381; -.
DR GlyGen; Q6QNU9; 4 sites.
DR iPTMnet; Q6QNU9; -.
DR PhosphoSitePlus; Q6QNU9; -.
DR MaxQB; Q6QNU9; -.
DR PaxDb; Q6QNU9; -.
DR PRIDE; Q6QNU9; -.
DR ProteomicsDB; 258892; -.
DR DNASU; 384059; -.
DR Ensembl; ENSMUST00000074829; ENSMUSP00000074381; ENSMUSG00000062545.
DR GeneID; 384059; -.
DR KEGG; mmu:384059; -.
DR UCSC; uc008uvf.1; mouse.
DR CTD; 384059; -.
DR MGI; MGI:3045221; Tlr12.
DR VEuPathDB; HostDB:ENSMUSG00000062545; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000165464; -.
DR HOGENOM; CLU_318753_0_0_1; -.
DR InParanoid; Q6QNU9; -.
DR OMA; NEMILAM; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q6QNU9; -.
DR TreeFam; TF351113; -.
DR BioGRID-ORCS; 384059; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q6QNU9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6QNU9; protein.
DR Bgee; ENSMUSG00000062545; Expressed in right kidney and 44 other tissues.
DR ExpressionAtlas; Q6QNU9; baseline and differential.
DR Genevisible; Q6QNU9; MM.
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:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; -; 3.
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; 2.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 7.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..906
FT /note="Toll-like receptor 12"
FT /id="PRO_0000042794"
FT TOPO_DOM 22..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..906
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 91..114
FT /note="LRR 1"
FT REPEAT 115..140
FT /note="LRR 2"
FT REPEAT 142..170
FT /note="LRR 3"
FT REPEAT 198..222
FT /note="LRR 4"
FT REPEAT 224..247
FT /note="LRR 5"
FT REPEAT 267..290
FT /note="LRR 6"
FT REPEAT 291..314
FT /note="LRR 7"
FT REPEAT 316..338
FT /note="LRR 8"
FT REPEAT 341..364
FT /note="LRR 9"
FT REPEAT 366..388
FT /note="LRR 10"
FT REPEAT 389..412
FT /note="LRR 11"
FT REPEAT 414..436
FT /note="LRR 12"
FT REPEAT 462..484
FT /note="LRR 13"
FT REPEAT 485..508
FT /note="LRR 14"
FT REPEAT 510..533
FT /note="LRR 15"
FT REPEAT 562..586
FT /note="LRR 16"
FT REPEAT 591..614
FT /note="LRR 17"
FT DOMAIN 759..905
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 804
FT /note="P->H: Fails to activate NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:15001781"
SQ SEQUENCE 906 AA; 99945 MW; 9D6372CCB42DFA14 CRC64;
MGRYWLLPGL LLSLPLVTGW STSNCLVTEG SRLPLVSRYF TFCRHSKLSF LAACLSVSNL
TQTLEVVPRT VEGLCLGGTV STLLPDAFSA FPGLKVLALS LHLTQLLPGA LRGLGQLQSL
SFFDSPLRRS LFLPPDAFSD LISLQRLHIS GPCLDKKAGI RLPPGLQWLG VTLSCIQDVG
ELAGMFPDLV QGSSSRVSWT LQKLDLSSNW KLKMASPGSL QGLQVEILDL TRTPLDAVWL
KGLGLQKLDV LYAQTATAEL AAEAVAHFEL QGLIVKESKI GSISQEALAS CHSLKTLGLS
STGLTKLPPG FLTAMPRLQR LELSGNQLQS AVLCMNETGD VSGLTTLDLS GNRLRILPPA
AFSCLPHLRE LLLRYNQLLS LEGYLFQELQ QLETLKLDGN PLLHLGKNWL AALPALTTLS
LLDTQIRMSP EPGFWGAKNL HTLSLKLPAL PAPAVLFLPM YLTSLELHIA SGTTEHWTLS
PAIFPSLETL TISGGGLKLK LGSQNASGVF PALQKLSLLK NSLDAFCSQG TSNLFLWQLP
KLQSLRVWGA GNSSRPCLIT GLPSLRELKL ASLQSITQPR SVQLEELVGD LPQLQALVLS
STGLKSLSAA AFQRLHSLQV LVLEYEKDLM LQDSLREYSP QMPHYIYILE SNLACHCANA
WMEPWVKRST KTYIYIRDNR LCPGQDRLSA RGSLPSFLWD HCPQTLELKL FLASSALVFM
LIALPLLQEA RNSWIPYLQA LFRVWLQGLR GKGDKGKRFL FDVFVSHCRQ DQGWVIEELL
PALEGFLPAG LGLRLCLPER DFEPGKDVVD NVVDSMLSSR TTLCVLSGQA LCNPRCRLEL
RLATSLLLAA PSPPVLLLVF LEPISRHQLP GYHRLARLLR RGDYCLWPEE EERKSGFWTW
LRSRLG
