TLR10_BOVIN
ID TLR10_BOVIN Reviewed; 812 AA.
AC Q6GV17; A7YK74;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Toll-like receptor 10;
DE AltName: CD_antigen=CD290;
DE Flags: Precursor;
GN Name=TLR10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16701904; DOI=10.1016/j.vetimm.2006.03.007;
RA Werling D., Piercy J., Coffey T.J.;
RT "Expression of TOLL-like receptors (TLR) by bovine antigen-presenting
RT cells-potential role in pathogen discrimination?";
RL Vet. Immunol. Immunopathol. 112:2-11(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17719743; DOI=10.1016/j.ygeno.2007.07.001;
RA Seabury C.M., Cargill E.J., Womack J.E.;
RT "Sequence variability and protein domain architectures for bovine Toll-like
RT receptors 1, 5, and 10.";
RL Genomics 90:502-515(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the Toll-like receptor family. {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; AY634632; AAT48490.2; -; mRNA.
DR EMBL; EU006655; ABU86944.1; -; Genomic_DNA.
DR EMBL; EU006656; ABU86945.1; -; Genomic_DNA.
DR EMBL; EU006657; ABU86946.1; -; Genomic_DNA.
DR EMBL; BC123541; AAI23542.1; -; mRNA.
DR RefSeq; NP_001070386.1; NM_001076918.2.
DR AlphaFoldDB; Q6GV17; -.
DR SMR; Q6GV17; -.
DR STRING; 9913.ENSBTAP00000018658; -.
DR PaxDb; Q6GV17; -.
DR PRIDE; Q6GV17; -.
DR Ensembl; ENSBTAT00000018658; ENSBTAP00000018658; ENSBTAG00000014042.
DR GeneID; 539791; -.
DR KEGG; bta:539791; -.
DR CTD; 81793; -.
DR VEuPathDB; HostDB:ENSBTAG00000014042; -.
DR VGNC; VGNC:50019; TLR10.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000163662; -.
DR HOGENOM; CLU_006000_3_0_1; -.
DR InParanoid; Q6GV17; -.
DR OMA; CHHEKNF; -.
DR OrthoDB; 282372at2759; -.
DR TreeFam; TF351113; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000014042; Expressed in nasopharynx and 80 other tissues.
DR ExpressionAtlas; Q6GV17; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:InterPro.
DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; IEA:InterPro.
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; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR027182; TLR10.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF23; PTHR24365:SF23; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 9.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..812
FT /note="Toll-like receptor 10"
FT /id="PRO_0000281927"
FT TOPO_DOM 20..577
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..812
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 24..46
FT /note="LRR 1"
FT REPEAT 49..70
FT /note="LRR 2"
FT REPEAT 73..94
FT /note="LRR 3"
FT REPEAT 97..118
FT /note="LRR 4"
FT REPEAT 119..139
FT /note="LRR 5"
FT REPEAT 143..166
FT /note="LRR 6"
FT REPEAT 296..321
FT /note="LRR 7"
FT REPEAT 325..348
FT /note="LRR 8"
FT REPEAT 350..373
FT /note="LRR 9"
FT REPEAT 374..395
FT /note="LRR 10"
FT REPEAT 399..420
FT /note="LRR 11"
FT REPEAT 423..443
FT /note="LRR 12"
FT REPEAT 445..467
FT /note="LRR 13"
FT REPEAT 468..489
FT /note="LRR 14"
FT REPEAT 490..510
FT /note="LRR 15"
FT DOMAIN 523..577
FT /note="LRRCT"
FT DOMAIN 633..776
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 812 AA; 93826 MW; 0876E0D10119B14C CRC64;
MRYIRSIYIF CSIVTSVRSG ASELPEEREL TTNFSSMSLT KVPEGLTPIT TTLDLSYNLL
FQLQHSDFRS LSKLKVLILC HNRIQELDIK TFEFNKELSY LDVSNNRLKS VTWFSLAGLR
HLDLSFNDFD TLPISVETGN MSHLETLGLS GAKIQKSDFQ KIAHLQLNTV LLGLRTLSHY
EEGSLPILNT TRLHIVLPVN TNFWVLLHDG IKTSKILEVI NIDLQKSQFT SYESQQIPIL
ENAKTSILLL NKVDLSWDDL FLIFQLVWHT SVEYFQIQHV TFGGKVYLDH NSFDYSNTVM
RTIKLEHVHF RIFNIPQESI YLLFTKMDIE NLTISDAQMP HMLFPMYPTR FQYLNFANNI
LTDDVFKKSI QLPHLKTLIL KDNKLETLSL VSHFASNTSL RHLDLSENLL QHENDENCLW
PETLVTMNLS FNKFADSVFG CLPRNIQILD LNSNKIQTVP KAITHLTSLR ELNLAFNFLT
DLPGCSHFRR LLVLNVEMNL ILSSSLDFFQ SCQEVKTLNA GRNPFRCTCE LRDFIQLGKY
SEGMMVGWSD SYICEYPLNL KGTQLKDVHL PEISCNTGLL IVTIVVVMLV LGMAVAFCCL
HFDLPWYLRM LHQWTQTWLR VRKTTQEQLK RSVQFHVFIS YSEHDSAWVK YELIPSLEKE
DGSVLICLHE GNSDPGKSMT EDTINCIEKS YKSIFVLSPS FVQTEWCHYE PYFAHHNLFH
ESLDYIILIL LEPIPLYCIP TRYPELKALM EKKAYLEWPK DRRKCGLFWA NLRAALHVNL
LDTRGTCELQ TFTELNEGFG GSAISLIRTD CL
