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Database: UniProt
Entry: G1MJH0_AILME
LinkDB: G1MJH0_AILME
Original site: G1MJH0_AILME 
ID   G1MJH0_AILME            Unreviewed;       910 AA.
AC   G1MJH0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391};
GN   Name=TLR2 {ECO:0000313|Ensembl:ENSAMEP00000019505.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000019505.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000019505.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000019505.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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DR   AlphaFoldDB; G1MJH0; -.
DR   STRING; 9646.ENSAMEP00000019505; -.
DR   Ensembl; ENSAMET00000020274.2; ENSAMEP00000019505.2; ENSAMEG00000018451.2.
DR   eggNOG; KOG4641; Eukaryota.
DR   GeneTree; ENSGT00940000156323; -.
DR   HOGENOM; CLU_006000_3_0_1; -.
DR   InParanoid; G1MJH0; -.
DR   TreeFam; TF351113; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; IEA:Ensembl.
DR   GO; GO:0035355; C:Toll-like receptor 2-Toll-like receptor 6 protein complex; IEA:Ensembl.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR   GO; GO:0038187; F:pattern recognition receptor activity; IEA:Ensembl.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0035325; F:Toll-like receptor binding; IEA:Ensembl.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0042497; F:triacyl lipopeptide binding; IEA:Ensembl.
DR   GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IEA:Ensembl.
DR   GO; GO:0071223; P:cellular response to lipoteichoic acid; IEA:Ensembl.
DR   GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0042496; P:detection of diacyl bacterial lipopeptide; IEA:Ensembl.
DR   GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:1903974; P:positive regulation of cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR   GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:Ensembl.
DR   GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; IEA:Ensembl.
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; 3.
DR   Pfam; PF01582; TIR; 1.
DR   PRINTS; PR01537; INTRLKN1R1F.
DR   SMART; SM00364; LRR_BAC; 4.
DR   SMART; SM00365; LRR_SD22; 5.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS50104; TIR; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        714..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          765..908
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   910 AA;  103082 MW;  99EABF871CA71081 CRC64;
     MGAAGNLGSL FFAPDLQQPQ RPPRTRAACS RPPPPSRSPD AARGRGGGGG RGAPAAGARP
     ELGPRLPCAA ARSADGRSPQ PARRDIRPEH FSFRCQPRTG ASRPEAARRR GPTAARSSPR
     LDHWTMSRVL WTVWVLGAVT NLSKEEASDQ ASSLSCDPTG VCDGRSRSLN SMPSGLTAAV
     RSLDLSNNEI TYIGNSDLRG CVNLEALKLG SNGINTIEED SFFSLRSLEL LDLSYNLLSN
     LSSSWFRPLS SLTFLNLLGN LYKSLGETPL FSQLMNLRIL KVGNIYSFTE LQEKDFAGLT
     FLEELEIDAS NLQRYEPKSL KSIQNISHLA LRMKQPVFLL EIFADLSSSL KHLELRDTHL
     NTFRFSQASI SETNTLIKKW TFRNVKITDG SFSEVVKLLN YVSGVLEVEF EDCTLDGLGN
     FNIADMDTIK NIGGIETLTV RRLYIPYFYS FYDMSSIYSL TEDVKRVTVE SSKVFLVPCS
     LSKHLKSLEY LDLSDNLMVD EYLGNSACEH AWPLLQTLTL RQNRLKSLEK TGETLLTLKN
     LMNLDISKNN FVSMPETCQW PEKLKYLNLS NTRINSVTRC IPWTLEILDI SNNILESFSL
     ILPQLKELYI SGNKLKTLPD ASFLPILRVM RISRNTISTF SKAQLDSFHT LKALEAGGNN
     FFCSCEFLSF TQGQQALAQI LTDWPENYLC DSPFYVRGQR VRDTRLPVSE CHRAALVSAV
     CSVLFLLIVL TGVLCHRFHG LWYLKMMWAW LQAKRKPRKA PPGDVCYDAF VSYSEHDSYW
     VENLMVQELE HFNPPFKLCL HKRDFVPGKW IIDNIIDSIE KSHKTIFVLS ENFVKSEWCK
     YELDFSHFRL FDENNDAAIL ILLEPIEKKA IPQRFCKLRK IMNTKTYLEW PTDDTQQEGF
     WLNLRTAIRS
//
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