ID A0A384AQS6_BALAS Unreviewed; 785 AA.
AC A0A384AQS6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391, ECO:0000256|PIRNR:PIRNR037595};
GN Name=TLR2 {ECO:0000313|RefSeq:XP_007189504.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007189504.1};
RN [1] {ECO:0000313|RefSeq:XP_007189504.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007189504.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- FUNCTION: Cooperates with LY96 to mediate the innate immune response to
CC bacterial lipoproteins and other microbial cell wall components.
CC Cooperates with TLR1 or TLR6 to mediate the innate immune response to
CC bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6,
CC leading to NF-kappa-B activation, cytokine secretion and the
CC inflammatory response (By similarity). May also promote apoptosis in
CC response to lipoproteins. Forms activation clusters composed of several
CC receptors depending on the ligand, these clusters trigger signaling
CC from the cell surface and subsequently are targeted to the Golgi in a
CC lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in
CC response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to
CC triacylated lipopeptides. {ECO:0000256|ARBA:ARBA00025293}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000256|ARBA:ARBA00004596}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004596}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family.
CC {ECO:0000256|ARBA:ARBA00009634, ECO:0000256|PIRNR:PIRNR037595}.
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DR RefSeq; XP_007189504.1; XM_007189442.1.
DR AlphaFoldDB; A0A384AQS6; -.
DR STRING; 310752.A0A384AQS6; -.
DR KEGG; bacu:102998386; -.
DR CTD; 7097; -.
DR InParanoid; A0A384AQS6; -.
DR OrthoDB; 21383at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:UniProtKB-UniRule.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 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; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; TOLL-LIKE RECEPTOR; 1.
DR PANTHER; PTHR24365:SF17; TOLL-LIKE RECEPTOR 2; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR PRINTS; PR01537; INTRLKN1R1F.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS50104; TIR; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Immunity {ECO:0000256|ARBA:ARBA00022859, ECO:0000256|PIRNR:PIRNR037595};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198,
KW ECO:0000256|PIRNR:PIRNR037595};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588,
KW ECO:0000256|PIRNR:PIRNR037595};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037595};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..785
FT /note="Toll-like receptor 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017061930"
FT TRANSMEM 589..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 640..783
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
SQ SEQUENCE 785 AA; 90273 MW; 96AF9F9CDA45FE30 CRC64;
MPPALWIVWV LGSVISLPKE GASDQASSLS CDPTGVCDGR SRSFNSIPSG LTAAVKSLDL
SSNEITYVSN SDLRRCVDLR TLRLGANEIH TVEEDSFFSL RSLEYLDLSY NRLSNFSSSW
FRSLSALKFL NLLGNLYKTL GERSLFSHLP NLRILKVGNS NSFTEIQEKD FAGLTLLEKL
EINAPNLQTY APKSLKSIQN ISHLILHLKQ PILLLEIFVD ILSSLECLEL RDTNLNTFHF
SEVSINETNT SIKKFAFRNV QITDESFIEV VKLFNYVSGV LEVEFDDCTH DGVGDFRTLT
LDTIKYLGDV ETLTIRKLHI PQFFLYHDLS NIYSLTGKVK RITIENSKVF LVPCLLSQHL
KSLEYLDLSE NLMSEETLKN SACEHAWPFL KTLVLRQNRL ESLEKTGEIL LTLQNLTNLD
ISKNNFHSMP ETCQWPGKMK YLNLSSTRIQ SLTRCIPQTL EILDISNNNL DSFSLILPEL
KELYISRNKL KTLPDASFLP VLLVMRISRN IINTFSKEQL DSFQKLKTLE AGGNSFICSC
DFLSFTQGQQ DLAQVLIDWP EDYLCDSPSP VRGQRVQDTR LSPSECHRAA VVSAVCCALF
LLLLLMGILC HRFHGLWYMK MMWAWLQAKR KPRKAPRRDI CYDAFVSYSE RDSYWVENLM
VQELEHFNPP FKLCLHKRDF IPGKWIIDNI IDSIEKSHKT IFVLSENFVK SEWCKYELDF
SHFRLFDEND DAAILILLEP IEKKAIPQRF CKLRKIMNTK TYLEWPADEM QQEGFWLNLR
AAIKS
//