TLR6_MOUSE
ID TLR6_MOUSE Reviewed; 795 AA.
AC Q9EPW9; Q9WTQ4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Toll-like receptor 6;
DE AltName: CD_antigen=CD286;
DE Flags: Precursor;
GN Name=Tlr6;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=10231569; DOI=10.1016/s0378-1119(99)00098-0;
RA Takeuchi O., Kawai T., Sanjo H., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Takeda K., Akira S.;
RT "TLR6: a novel member of an expanding Toll-like receptor family.";
RL Gene 231:59-65(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PRO-680, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Macrophage;
RX PubMed=11095740; DOI=10.1073/pnas.250476497;
RA Ozinsky A., Underhill D.M., Fontenot J.D., Hajjar A.M., Smith K.D.,
RA Wilson C.B., Schroeder L., Aderem A.;
RT "The repertoire for pattern recognition of pathogens by the innate immune
RT system is defined by cooperation between Toll-like receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13766-13771(2000).
RN [3]
RP FUNCTION.
RX PubMed=20037584; DOI=10.1038/ni.1836;
RA Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A.,
RA Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A.,
RA El Khoury J., Golenbock D.T., Moore K.J.;
RT "CD36 ligands promote sterile inflammation through assembly of a Toll-like
RT receptor 4 and 6 heterodimer.";
RL Nat. Immunol. 11:155-161(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23812099; DOI=10.1038/ni.2639;
RA Sheedy F.J., Grebe A., Rayner K.J., Kalantari P., Ramkhelawon B.,
RA Carpenter S.B., Becker C.E., Ediriweera H.N., Mullick A.E., Golenbock D.T.,
RA Stuart L.M., Latz E., Fitzgerald K.A., Moore K.J.;
RT "CD36 coordinates NLRP3 inflammasome activation by facilitating
RT intracellular nucleation of soluble ligands into particulate ligands in
RT sterile inflammation.";
RL Nat. Immunol. 14:812-820(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-483 IN COMPLEX WITH TLR2 AND
RP LIPOPEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-144; ASN-195; ASN-214;
RP ASN-253; ASN-359; ASN-401 AND ASN-434, FUNCTION, LRR REPEATS, AND SUBUNIT.
RX PubMed=19931471; DOI=10.1016/j.immuni.2009.09.018;
RA Kang J.Y., Nan X., Jin M.S., Youn S.J., Ryu Y.H., Mah S., Han S.H., Lee H.,
RA Paik S.G., Lee J.O.;
RT "Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like
RT receptor 6 heterodimer.";
RL Immunity 31:873-884(2009).
CC -!- FUNCTION: Participates in the innate immune response to Gram-positive
CC bacteria and fungi. Specifically recognizes diacylated and, to a lesser
CC extent, triacylated lipopeptides (PubMed:19931471). In response to
CC diacylated lipopeptides, forms the activation cluster
CC TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell
CC surface and subsequently is targeted to the Golgi in a lipid-raft
CC dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B
CC activation, cytokine secretion and the inflammatory response.
CC Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2),
CC soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and
CC B.burgdorferi outer surface protein A lipoprotein (OspA-L)
CC cooperatively with TLR2. In complex with TLR4, promotes sterile
CC inflammation in monocytes/macrophages in response to oxidized low-
CC density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the
CC initial signal is provided by oxLDL- or amyloid-beta 42-binding to
CC CD36. This event induces the formation of a heterodimer of TLR4 and
CC TLR6, which is rapidly internalized and triggers inflammatory response,
CC leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9
CC cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1
CC signaling pathway, as well as IL1B secretion (PubMed:20037584,
CC PubMed:23812099). {ECO:0000269|PubMed:19931471,
CC ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:23812099}.
CC -!- SUBUNIT: Homodimer (via cytoplasmic TIR domain) (By similarity).
CC Heterodimer with TLR2 via their respective extracellular domains
CC (PubMed:19931471). Binds MYD88 via their respective TIR domains
CC (Probable). Interacts with CD36, following CD36 stimulation by oxLDL or
CC amyloid-beta 42, and forms a heterodimer with TLR4. The trimeric
CC complex is internalized and triggers inflammatory response. LYN kinase
CC activity facilitates TLR4:TLR6 heterodimerization and signal initiation
CC (By similarity). The heterodimer TLR2:TLR6 interacts with CD14 and CD36
CC in response to triacylated lipopeptides (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2C9, ECO:0000269|PubMed:19931471,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11095740};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000269|PubMed:11095740}; Single-pass type I
CC membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9Y2C9}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9Y2C9}. Note=Upon complex formation with CD36
CC and TLR4, internalized through dynamin-dependent endocytosis. Does not
CC reside in lipid rafts before stimulation but accumulates increasingly
CC in the raft upon the presence of the microbial ligand. In response to
CC diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid
CC rafts, this recruitment determine the intracellular targeting to the
CC Golgi apparatus. {ECO:0000250|UniProtKB:Q9Y2C9}.
CC -!- TISSUE SPECIFICITY: Detected in thymus, spleen, ovary and lung.
CC Expressed in macrohpages. {ECO:0000269|PubMed:23812099}.
CC -!- DISRUPTION PHENOTYPE: Animals with a double knockout of APOE and TLR6,
CC fed a Western diet for 12 weeks, have less aortic plaque formation than
CC single APOE knockout mice. They also show lower serum concentrations of
CC IL1A, ILB and IL18. {ECO:0000269|PubMed:23812099}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG38563.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA78632.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020808; BAA78632.1; ALT_INIT; mRNA.
DR EMBL; AF314636; AAG38563.1; ALT_INIT; mRNA.
DR RefSeq; NP_035734.3; NM_011604.3.
DR RefSeq; XP_006503920.1; XM_006503857.2.
DR RefSeq; XP_006503921.1; XM_006503858.3.
DR RefSeq; XP_006503922.1; XM_006503859.3.
DR RefSeq; XP_006503923.1; XM_006503860.1.
DR PDB; 3A79; X-ray; 2.90 A; B=1-482.
DR PDBsum; 3A79; -.
DR AlphaFoldDB; Q9EPW9; -.
DR SMR; Q9EPW9; -.
DR IntAct; Q9EPW9; 4.
DR STRING; 10090.ENSMUSP00000062096; -.
DR ChEMBL; CHEMBL2146341; -.
DR GlyGen; Q9EPW9; 10 sites.
DR iPTMnet; Q9EPW9; -.
DR PhosphoSitePlus; Q9EPW9; -.
DR MaxQB; Q9EPW9; -.
DR PaxDb; Q9EPW9; -.
DR PRIDE; Q9EPW9; -.
DR ProteomicsDB; 258895; -.
DR Antibodypedia; 10461; 876 antibodies from 46 providers.
DR DNASU; 21899; -.
DR Ensembl; ENSMUST00000062315; ENSMUSP00000062096; ENSMUSG00000051498.
DR GeneID; 21899; -.
DR KEGG; mmu:21899; -.
DR CTD; 10333; -.
DR MGI; MGI:1341296; Tlr6.
DR VEuPathDB; HostDB:ENSMUSG00000051498; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000162201; -.
DR InParanoid; Q9EPW9; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q9EPW9; -.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR BioGRID-ORCS; 21899; 0 hits in 71 CRISPR screens.
DR EvolutionaryTrace; Q9EPW9; -.
DR PRO; PR:Q9EPW9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9EPW9; protein.
DR Bgee; ENSMUSG00000051498; Expressed in granulocyte and 54 other tissues.
DR ExpressionAtlas; Q9EPW9; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0035355; C:Toll-like receptor 2-Toll-like receptor 6 protein complex; IDA:MGI.
DR GO; GO:0042498; F:diacyl lipopeptide binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0071723; F:lipopeptide binding; IMP:UniProtKB.
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:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0035663; F:Toll-like receptor 2 binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0001775; P:cell activation; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0071221; P:cellular response to bacterial lipopeptide; IBA:GO_Central.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IGI:ARUK-UCL.
DR GO; GO:0042496; P:detection of diacyl bacterial lipopeptide; ISO:MGI.
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; IGI:ARUK-UCL.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IGI:ARUK-UCL.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IGI:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:ARUK-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; NAS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IGI:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IGI:ARUK-UCL.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IGI:ARUK-UCL.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0034150; P:toll-like receptor 6 signaling pathway; IEA:InterPro.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; ISO:MGI.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IGI:ARUK-UCL.
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; IPR027187; TLR6.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF422; PTHR24365:SF422; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 10.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Immunity; Inflammatory response;
KW Innate immunity; Leucine-rich repeat; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..795
FT /note="Toll-like receptor 6"
FT /id="PRO_0000034732"
FT TOPO_DOM 28..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 54..77
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 78..101
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 102..125
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 126..150
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 151..175
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 176..199
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 200..223
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 224..250
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 251..278
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 279..308
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 309..337
FT /note="LRR 11"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 338..361
FT /note="LRR 12"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 362..388
FT /note="LRR 13"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 389..414
FT /note="LRR 14"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 415..437
FT /note="LRR 15"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 438..457
FT /note="LRR 16"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 458..478
FT /note="LRR 17"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 479..500
FT /note="LRR 18"
FT /evidence="ECO:0000269|PubMed:19931471"
FT REPEAT 501..524
FT /note="LRR 19"
FT /evidence="ECO:0000269|PubMed:19931471"
FT DOMAIN 525..576
FT /note="LRRCT"
FT DOMAIN 640..781
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19931471"
FT DISULFID 117..139
FT /evidence="ECO:0000269|PubMed:19931471"
FT DISULFID 235..265
FT /evidence="ECO:0000269|PubMed:19931471"
FT DISULFID 348..373
FT /evidence="ECO:0000269|PubMed:19931471"
FT DISULFID 424..447
FT /evidence="ECO:0000269|PubMed:19931471"
FT MUTAGEN 680
FT /note="P->H: Dominant negative mutant, blocks response to
FT Gram-positive pathogens."
FT /evidence="ECO:0000269|PubMed:11095740"
FT CONFLICT 181
FT /note="Y -> H (in Ref. 1; BAA78632)"
FT /evidence="ECO:0000305"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3A79"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3A79"
FT TURN 93..98
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3A79"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 214..229
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 276..288
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:3A79"
FT TURN 367..372
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:3A79"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:3A79"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:3A79"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:3A79"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:3A79"
SQ SEQUENCE 795 AA; 91116 MW; 34D8BD175A26C233 CRC64;
MSQDRKPIVG SFHFVCALAL IVGSMTPFSN ELESMVDYSN RNLTHVPKDL PPRTKALSLS
QNSISELRMP DISFLSELRV LRLSHNRIRS LDFHVFLFNQ DLEYLDVSHN RLQNISCCPM
ASLRHLDLSF NDFDVLPVCK EFGNLTKLTF LGLSAAKFRQ LDLLPVAHLH LSCILLDLVS
YHIKGGETES LQIPNTTVLH LVFHPNSLFS VQVNMSVNAL GHLQLSNIKL NDENCQRLMT
FLSELTRGPT LLNVTLQHIE TTWKCSVKLF QFFWPRPVEY LNIYNLTITE RIDREEFTYS
ETALKSLMIE HVKNQVFLFS KEALYSVFAE MNIKMLSISD TPFIHMVCPP SPSSFTFLNF
TQNVFTDSVF QGCSTLKRLQ TLILQRNGLK NFFKVALMTK NMSSLETLDV SLNSLNSHAY
DRTCAWAESI LVLNLSSNML TGSVFRCLPP KVKVLDLHNN RIMSIPKDVT HLQALQELNV
ASNSLTDLPG CGAFSSLSVL VIDHNSVSHP SEDFFQSCQN IRSLTAGNNP FQCTCELRDF
VKNIGWVARE VVEGWPDSYR CDYPESSKGT ALRDFHMSPL SCDTVLLTVT IGATMLVLAV
TGAFLCLYFD LPWYVRMLCQ WTQTRHRARH IPLEELQRNL QFHAFVSYSE HDSAWVKNEL
LPNLEKDDIR VCLHERNFVP GKSIVENIIN FIEKSYKAIF VLSPHFIQSE WCHYELYFAH
HNLFHEGSDN LILILLEPIL QNNIPSRYHK LRALMAQRTY LEWPTEKGKR GLFWANLRAS
FIMKLALVNE DDVKT
