TRIL_RAT
ID TRIL_RAT Reviewed; 811 AA.
AC Q496Z2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=TLR4 interactor with leucine rich repeats;
DE AltName: Full=Leucine-rich repeat-containing protein KIAA0644 homolog;
DE Flags: Precursor;
GN Name=Tril;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP TISSUE SPECIFICITY.
RX PubMed=19710467; DOI=10.4049/jimmunol.0901518;
RA Carpenter S., Carlson T., Dellacasagrande J., Garcia A., Gibbons S.,
RA Hertzog P., Lyons A., Lin L.L., Lynch M., Monie T., Murphy C., Seidl K.J.,
RA Wells C., Dunne A., O'Neill L.A.;
RT "TRIL, a functional component of the TLR4 signaling complex, highly
RT expressed in brain.";
RL J. Immunol. 183:3989-3995(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-798, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the TLR4 signaling complex. Mediates the innate
CC immune response to bacterial lipopolysaccharide (LPS) leading to
CC cytokine secretion and the inflammatory response (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-
CC protein complex containing at least CD14, MD-2 and TLR4. Interacts with
CC TLR4; this interaction is greatly enhanced following LPS stimulation
CC (By similarity). Interacts with LPS (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cortical astrocytes and in
CC cerebellar granule neurons. {ECO:0000269|PubMed:19710467}.
CC -!- PTM: N-glycolysaled. {ECO:0000250}.
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DR EMBL; BC100659; AAI00660.1; -; mRNA.
DR RefSeq; NP_001029182.1; NM_001034010.1.
DR AlphaFoldDB; Q496Z2; -.
DR SMR; Q496Z2; -.
DR STRING; 10116.ENSRNOP00000037327; -.
DR GlyGen; Q496Z2; 3 sites.
DR iPTMnet; Q496Z2; -.
DR PhosphoSitePlus; Q496Z2; -.
DR PaxDb; Q496Z2; -.
DR PRIDE; Q496Z2; -.
DR Ensembl; ENSRNOT00000036951; ENSRNOP00000037327; ENSRNOG00000026941.
DR GeneID; 362364; -.
DR KEGG; rno:362364; -.
DR UCSC; RGD:1310827; rat.
DR CTD; 9865; -.
DR RGD; 1310827; Tril.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161975; -.
DR HOGENOM; CLU_357128_0_0_1; -.
DR InParanoid; Q496Z2; -.
DR OMA; PHDVLTY; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q496Z2; -.
DR TreeFam; TF331598; -.
DR PRO; PR:Q496Z2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000026941; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; Q496Z2; RN.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; ISO:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002718; P:regulation of cytokine production involved in immune response; ISO:RGD.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:RGD.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS51450; LRR; 13.
PE 1: Evidence at protein level;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..811
FT /note="TLR4 interactor with leucine rich repeats"
FT /id="PRO_0000349257"
FT TOPO_DOM 26..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..57
FT /note="LRRNT"
FT REPEAT 61..81
FT /note="LRR 1"
FT REPEAT 84..105
FT /note="LRR 2"
FT REPEAT 108..129
FT /note="LRR 3"
FT REPEAT 132..153
FT /note="LRR 4"
FT REPEAT 156..177
FT /note="LRR 5"
FT REPEAT 180..201
FT /note="LRR 6"
FT REPEAT 204..223
FT /note="LRR 7"
FT REPEAT 230..251
FT /note="LRR 8"
FT REPEAT 254..275
FT /note="LRR 9"
FT REPEAT 278..298
FT /note="LRR 10"
FT REPEAT 302..323
FT /note="LRR 11"
FT REPEAT 326..347
FT /note="LRR 12"
FT DOMAIN 359..416
FT /note="LRRCT"
FT REGION 414..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 811 AA; 89053 MW; 2913EFA8BBFBB355 CRC64;
MEGVGAVRFW LVVCGCLAFP PRAESVCPER CDCQHPQHLL CTNRGLRAVP KTSSLPSPQD
VLTYSLGGNF ITNITAFDFH RLGQLRRLDL QYNQIRSLHP KTFEKLSRLE ELYLGNNLLQ
ALAPGTLAPL RKLRILYANG NEIGRLSRGS FEGLESLVKL RLDGNVLGAL PDAVFAPLGN
LLYLHLEANR IRFLGKNAFT QLGKLRFLNL SANELQPSLR HAATFVPLRS LSTLILSANS
LQHLGPRVFQ HLPRLGLLSL SGNQLTHLAP EAFWGLEALR ELRLEGNRLN QLPLTLLEPL
HSLEALDLSG NELSALHPAT FGHQGRLREL SLRDNALSAL SGDIFAASPA LYRLDLDGNG
WTCDCRLRGL KRWMGNWHSQ GRLLTVFVQC RHPPALRGKY LDYLDDQLLQ NGSCVDPSPS
PTAGSRQWPI STAPGEGMTP PAGLAQELPL QPQPQPQQRG RLLPGVAWAG AAKELVGNRS
ALRLNRRGPG LQHQSPSAAA ASGSAPQSLD LHEKPERGRP TRANLPQTEP TPTSEPASGT
PSARDSWQRA AKQRLASEQQ GRAVQYDSGV GLPPLVSDPC DFNKFILCNL TVEAVSANSA
SVRWAVREHR SPRPQGGARF RLLFDRFGQQ PKFQRFVYLP ERSDSATLHE LRGDTPYLVC
VEGVLGGRVC PVAPRDHCAG LVTLPEAGGR GGVDYQLLTL VLLAINALLV LLALAAWGSR
WLRRKLRARR KGGAPVHVRH MYSTRRPLRS MGTGVSADFS GFQSHRPRTT VCALSEADLI
EFPCDRFMDS SGGGTGGSLR REDHLLQRFA D
