TLR4_PINIB
ID TLR4_PINIB Reviewed; 899 AA.
AC V5NAL9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Toll-like receptor 4 {ECO:0000305};
DE AltName: Full=PmTLR4 {ECO:0000305|PubMed:28893645};
DE Flags: Precursor;
OS Pinctada imbricata (Atlantic pearl-oyster) (Pinctada martensii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX NCBI_TaxID=66713 {ECO:0000312|EMBL:AHA85007.1};
RN [1] {ECO:0000312|EMBL:AHA85007.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=28893645; DOI=10.1016/j.cbpb.2017.08.006;
RA Wu Y., Liang H., Wang Z., Lei Q., Xia L.;
RT "A novel toll-like receptor from the pearl oyster Pinctada fucata martensii
RT is induced in response to stress.";
RL Comp. Biochem. Physiol. 214B:19-26(2017).
CC -!- FUNCTION: May be involved in the innate immune response.
CC {ECO:0000305|PubMed:28893645}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. The highest
CC expression is in the hepatopancreas, with moderate expression in the
CC gills, and low expression in the gonads, adductor muscle, hemocytes,
CC and mantle. {ECO:0000269|PubMed:28893645}.
CC -!- INDUCTION: Induced by lipopolysaccharide (LPS) exposure, where
CC expression increases significantly at 3 and 6 hours post-exposure, and
CC gradually decreases to control levels by 12 hours post-exposure. Also
CC induced during the nucleus insertion operation used in pearl culturing,
CC which involves the implantation of a round pearl bead and a piece of
CC mantle tissue from a donor oyster. Expression is highest at 2 days
CC post-insertion and gradually decreases to control levels at 5 days
CC post-insertion, maintaining that level until the end of the experiment
CC at 20 days. {ECO:0000269|PubMed:28893645}.
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; KF524262; AHA85007.1; -; mRNA.
DR AlphaFoldDB; V5NAL9; -.
DR SMR; V5NAL9; -.
DR PRIDE; V5NAL9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 5.
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; 2.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 8.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Immunity; Innate immunity;
KW Leucine-rich repeat; Membrane; NAD; Receptor; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000255"
FT CHAIN 47..899
FT /note="Toll-like receptor 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000444011"
FT TOPO_DOM 47..702
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 83..103
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 104..126
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 128..150
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 155..179
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 181..202
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 203..229
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 230..253
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 257..282
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 313..336
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 338..360
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 363..386
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 468..493
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 501..524
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 526..549
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 554..577
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 579..601
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 602..624
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 631..654
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT DOMAIN 756..897
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 899 AA; 103847 MW; E80782BF14338665 CRC64;
MCPLQIHVLH LIQGNQKNRK GKYVNMTRQL WYILPLLFLL CHCVTSERRC YFSKISKTCS
HASKCLLKAD CSDRNLTESP KFNESVVQID LSNNSINVFP DLPRSLLVLD ISRNPLKQFQ
KNAFARLQNL TTLSIVNNTY GLQPSNLTAG IFKGLTRLTY LDLRGSWNGT AYPEEVLSDL
VSLNALRING KQKGFGVLMR KIHALKRLDI SGSEGDCKID CLHAGYFQNV HGIQELNVSN
CHLTNILEGT FSYITNLTHL DISYNEELSF NILRNISKDL KNTKIEVLKI NKIHCTFGVG
TQIYVSDLKD LQNTSLRELH ANSNRLETIQ SGVLMYLPKT LQHASVSDNK LTMGMYALET
ANLVNLKTYD MSLQFKSHDP RDIFSNCNDT RNGYIRNRRP HESEGEISVR KKLLNDQIYR
WKDDQAFEVY QNTSNNNQHK LMFPFPSPFP VPLPQRLEIA YFNTSTLHYP LLKYRIGNNK
IKEIYAQDNV FYDLQGPLEN LEGLEILDLS NNFCTNLSTF FFDYLTGLKS VKLNHNILGF
SLAKDEKGET FKNLLKLKHL EIKYNRIQVL PKKILRNLIS LETLDLADNW LRKFKVDLKH
IKGLRHIDLS NNQISELPPG VMRELDEIAK SSNLTVNLTG NSLLCNCENE HFLRWIVTST
IRFGFHGNDT CQTRFSKTGR VLMSQGNEFL LVLERNCRSY TAVIVLFSCV FVILLTVIVC
GVVYRYRWKL RYLYYMTKGR YKGYSSLKTK SEEGDYEFDA FISYADEDRQ FALHDMMKNV
EREGNLKLCF HNRDFIPGFD IAVNITNAIN NSRKTICVIS SNYLNSYWCM YELNIGRMES
IYSRNGEDVL FLVILENCSS SNIPFSVFDI IEKKSYIEYP NDTEGDIIFW RKLRDPISM
