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TRIL_MOUSE
ID   TRIL_MOUSE              Reviewed;         809 AA.
AC   Q9DBY4; Q80TV0; Q8BKM5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=TLR4 interactor with leucine rich repeats;
DE   AltName: Full=Leucine-rich repeat-containing protein KIAA0644;
DE   Flags: Precursor;
GN   Name=Tril; Synonyms=Kiaa0644;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Spinal ganglion;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   INDUCTION BY LPS, AND 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).
CC   -!- FUNCTION: Component of the TLR4 signaling complex. Mediates the innate
CC       immune response to bacterial lipopolysaccharide (LPS) leading to
CC       cytokine secretion (By similarity). {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 by LPS stimulation (By
CC       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 brain, spinal cord and lung.
CC       {ECO:0000269|PubMed:19710467}.
CC   -!- INDUCTION: By bacterial lipopolysaccharides (LPS) (in vivo and in
CC       vitro). {ECO:0000269|PubMed:19710467}.
CC   -!- PTM: N-glycolysaled. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65620.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK122338; BAC65620.1; ALT_FRAME; mRNA.
DR   EMBL; AK004681; BAB23469.1; -; mRNA.
DR   EMBL; AK033401; BAC28270.1; -; mRNA.
DR   EMBL; AK051421; BAC34634.1; -; mRNA.
DR   EMBL; BC043099; AAH43099.1; -; mRNA.
DR   EMBL; BC059224; AAH59224.1; -; mRNA.
DR   CCDS; CCDS51776.1; -.
DR   RefSeq; NP_080093.1; NM_025817.4.
DR   AlphaFoldDB; Q9DBY4; -.
DR   SMR; Q9DBY4; -.
DR   STRING; 10090.ENSMUSP00000116056; -.
DR   GlyConnect; 2770; 1 N-Linked glycan (1 site).
DR   GlyGen; Q9DBY4; 4 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9DBY4; -.
DR   PhosphoSitePlus; Q9DBY4; -.
DR   MaxQB; Q9DBY4; -.
DR   PaxDb; Q9DBY4; -.
DR   PRIDE; Q9DBY4; -.
DR   ProteomicsDB; 258847; -.
DR   Antibodypedia; 73340; 20 antibodies from 9 providers.
DR   DNASU; 66873; -.
DR   Ensembl; ENSMUST00000127748; ENSMUSP00000116056; ENSMUSG00000043496.
DR   GeneID; 66873; -.
DR   KEGG; mmu:66873; -.
DR   UCSC; uc009bzk.2; mouse.
DR   CTD; 9865; -.
DR   MGI; MGI:1914123; Tril.
DR   VEuPathDB; HostDB:ENSMUSG00000043496; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000161975; -.
DR   HOGENOM; CLU_357128_0_0_1; -.
DR   InParanoid; Q9DBY4; -.
DR   OMA; PHDVLTY; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q9DBY4; -.
DR   TreeFam; TF331598; -.
DR   BioGRID-ORCS; 66873; 5 hits in 71 CRISPR screens.
DR   ChiTaRS; Tril; mouse.
DR   PRO; PR:Q9DBY4; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9DBY4; protein.
DR   Bgee; ENSMUSG00000043496; Expressed in metanephric mesenchyme and 208 other tissues.
DR   Genevisible; Q9DBY4; MM.
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:MGI.
DR   GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
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:MGI.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:MGI.
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   2: Evidence at transcript 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..809
FT                   /note="TLR4 interactor with leucine rich repeats"
FT                   /id="PRO_0000349256"
FT   TOPO_DOM        26..694
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        695..715
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        716..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          412..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         796
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q496Z2"
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        587
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   809 AA;  88810 MW;  5E86F55B8AE419FA CRC64;
     MEGVGAVRFW LVVCGCLAFP PRAESVCPER CDCQHPQHLL CTNRGLRAVP KTSSLPSPQD
     VLTYSLGGNF ITNITAFDFH RLGQLRRLDL QYNQIRSLHP KTFEKLSRLE ELYLGNNLLQ
     ALVPGTLAPL RKLRILYANG NEIGRLSRGS FEGLESLVKL RLDGNVLGAL PDAVFAPLGN
     LLYLHLESNR IRFLGKNAFS QLGKLRFLNL SANELQPSLR HAATFVPLRS LSTLILSANS
     LQHLGPRVFQ HLPRLGLLSL SGNQLTHLAP EAFWGLEALR ELRLEGNRLN QLPLTLLEPL
     HSLEALDLSG NELSALHPAT FGHQGRLREL SLRDNALSAL SGDIFAASPA LYRLDLDGNG
     WTCDCRLRGL KRWMGNWHSQ GRLLTVFVQC RHPPALRGKY LDYLDDQLLQ NGSCVDPSPS
     PTAGSRQWPL PTSSEEGMTP PAGLSQELPL QPQPQPQQRG RLLPGVAWGG AAKELVGNRS
     ALRLSRRGPG PHQGPSAAAP GSAPQSLDLH EKPGRGRHTR ANLSQTEPTP TSEPASGTPS
     ARDSWQRAAK QRLASEQQES AVQSVSGVGL PPLVSDPCDF NKFILCNLTV EAVSANSASV
     RWAVREHRSP RPQGGARFRL LFDRFGQQPK FQRFVYLPER SDSATLHELR GDTPYLVCVE
     GVLGGRVCPV APRDHCAGLV TLPEAGGRGG VDYQLLTLVL LAVNALLVLL ALAAWGSRWL
     RRKLRARRKG GAPVHVRHMY STRRPLRSMG TGVSADFSGF QSHRPRTTVC ALSEADLIEF
     PCDRFMDSTG GGTSGSLRRE DHLLQRFAD
 
 
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