CLC7A_MOUSE
ID CLC7A_MOUSE Reviewed; 244 AA.
AC Q6QLQ4; E9QPW2; Q8K1L4; Q9JI50;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=C-type lectin domain family 7 member A;
DE AltName: Full=Beta-glucan receptor {ECO:0000303|PubMed:11544516};
DE AltName: Full=C-type lectin superfamily member 12;
DE AltName: Full=Dendritic cell-associated C-type lectin 1 {ECO:0000303|PubMed:10779524};
DE Short=DC-associated C-type lectin 1 {ECO:0000303|PubMed:10779524};
DE Short=Dectin-1 {ECO:0000303|PubMed:10779524};
DE AltName: CD_antigen=CD369;
GN Name=Clec7a {ECO:0000312|MGI:MGI:1861431};
GN Synonyms=Bgr, Clecsf12, Dectin1 {ECO:0000303|PubMed:10779524};
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], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Dendritic cell;
RX PubMed=10779524; DOI=10.1074/jbc.m909512199;
RA Ariizumi K., Shen G.-L., Shikano S., Xu S., Ritter R. III, Kumamoto T.,
RA Edelbaum D., Morita A., Bergstresser P.R., Takashima A.;
RT "Identification of a novel, dendritic cell-associated molecule, dectin-1,
RT by subtractive cDNA cloning.";
RL J. Biol. Chem. 275:20157-20167(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11544516; DOI=10.1038/35092620;
RA Brown G.D., Gordon S.;
RT "Immune recognition. A new receptor for beta-glucans.";
RL Nature 413:36-37(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=12719479; DOI=10.1084/jem.20021787;
RA Gantner B.N., Simmons R.M., Canavera S.J., Akira S., Underhill D.M.;
RT "Collaborative induction of inflammatory responses by dectin-1 and Toll-
RT like receptor 2.";
RL J. Exp. Med. 197:1107-1117(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-221; HIS-223 AND
RP CYS-232.
RX PubMed=15213161; DOI=10.1128/iai.72.7.4159-4171.2004;
RA Adachi Y., Ishii T., Ikeda Y., Hoshino A., Tamura H., Aketagawa J.,
RA Tanaka S., Ohno N.;
RT "Characterization of beta-glucan recognition site on C-type lectin, dectin
RT 1.";
RL Infect. Immun. 72:4159-4171(2004).
RN [7]
RP FUNCTION.
RX PubMed=15729357; DOI=10.1038/sj.emboj.7600594;
RA Gantner B.N., Simmons R.M., Underhill D.M.;
RT "Dectin-1 mediates macrophage recognition of Candida albicans yeast but not
RT filaments.";
RL EMBO J. 24:1277-1286(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH SYK.
RX PubMed=15845454; DOI=10.1016/j.immuni.2005.03.004;
RA Rogers N.C., Slack E.C., Edwards A.D., Nolte M.A., Schulz O.,
RA Schweighoffer E., Williams D.L., Gordon S., Tybulewicz V.L., Brown G.D.,
RA Reis e Sousa C.;
RT "Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern
RT recognition pathway for C type lectins.";
RL Immunity 22:507-517(2005).
RN [9]
RP FUNCTION.
RX PubMed=15731053; DOI=10.1128/iai.73.3.1553-1560.2005;
RA Viriyakosol S., Fierer J., Brown G.D., Kirkland T.N.;
RT "Innate immunity to the pathogenic fungus Coccidioides posadasii is
RT dependent on Toll-like receptor 2 and Dectin-1.";
RL Infect. Immun. 73:1553-1560(2005).
RN [10]
RP FUNCTION.
RX PubMed=16825490; DOI=10.1182/blood-2006-05-024406;
RA Yadav M., Schorey J.S.;
RT "The beta-glucan receptor dectin-1 functions together with TLR2 to mediate
RT macrophage activation by mycobacteria.";
RL Blood 108:3168-3175(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17159984; DOI=10.1038/ni1408;
RA Taylor P.R., Tsoni S.V., Willment J.A., Dennehy K.M., Rosas M., Findon H.,
RA Haynes K., Steele C., Botto M., Gordon S., Brown G.D.;
RT "Dectin-1 is required for beta-glucan recognition and control of fungal
RT infection.";
RL Nat. Immunol. 8:31-38(2007).
RN [12]
RP FUNCTION.
RX PubMed=27288407; DOI=10.1074/jbc.m116.717157;
RA Kralova J., Fabisik M., Pokorna J., Skopcova T., Malissen B., Brdicka T.;
RT "The Transmembrane Adaptor Protein SCIMP Facilitates Sustained Dectin-1
RT Signaling in Dendritic Cells.";
RL J. Biol. Chem. 291:16530-16540(2016).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32358020; DOI=10.4049/jimmunol.1900793;
RA Campuzano A., Zhang H., Ostroff G.R., Dos Santos Dias L., Wuethrich M.,
RA Klein B.S., Yu J.J., Lara H.H., Lopez-Ribot J.L., Hung C.Y.;
RT "CARD9-associated Dectin-1 and Dectin-2 are required for protective
RT immunity of a multivalent vaccine against coccidioides posadasii
RT infection.";
RL J. Immunol. 204:3296-3306(2020).
RN [14] {ECO:0007744|PDB:2BPD, ECO:0007744|PDB:2BPE, ECO:0007744|PDB:2BPH, ECO:0007744|PDB:2CL8}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 113-244 IN COMPLEX WITH METAL ION
RP AND BETA-GLUCAN ANALOG LAMINARIN, METAL-BINDING SITES, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=17473009; DOI=10.1110/ps.072791207;
RA Brown J., O'Callaghan C.A., Marshall A.S., Gilbert R.J., Siebold C.,
RA Gordon S., Brown G.D., Jones E.Y.;
RT "Structure of the fungal beta-glucan-binding immune receptor dectin-1:
RT implications for function.";
RL Protein Sci. 16:1042-1052(2007).
CC -!- FUNCTION: Lectin that functions as pattern recognizing receptor (PRR)
CC specific for beta-1,3-linked and beta-1,6-linked glucans, which
CC constitute cell wall constituents from pathogenic bacteria and fungi
CC (PubMed:11544516, PubMed:17159984, PubMed:15213161). Necessary for the
CC TLR2-mediated inflammatory response and activation of NF-kappa-B: upon
CC beta-glucan binding, recruits SYK via its ITAM motif and promotes a
CC signaling cascade that activates some CARD domain-BCL10-MALT1 (CBM)
CC signalosomes, leading to the activation of NF-kappa-B and MAP kinase
CC p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate
CC expression of genes encoding pro-inflammatory cytokines and chemokines
CC (PubMed:12719479, PubMed:15731053, PubMed:16825490, PubMed:32358020).
CC Enhances cytokine production in macrophages and dendritic cells
CC (PubMed:15845454). Mediates production of reactive oxygen species in
CC the cell (PubMed:12719479, PubMed:15731053, PubMed:16825490). Mediates
CC phagocytosis of C.albicans conidia (PubMed:15729357, PubMed:16825490).
CC Binds T-cells in a way that does not involve their surface glycans and
CC plays a role in T-cell activation (PubMed:10779524). Stimulates T-cell
CC proliferation (PubMed:10779524). Induces phosphorylation of SCIMP after
CC binding beta-glucans (PubMed:27288407). {ECO:0000269|PubMed:10779524,
CC ECO:0000269|PubMed:11544516, ECO:0000269|PubMed:12719479,
CC ECO:0000269|PubMed:15213161, ECO:0000269|PubMed:15729357,
CC ECO:0000269|PubMed:15731053, ECO:0000269|PubMed:15845454,
CC ECO:0000269|PubMed:16825490, ECO:0000269|PubMed:17159984,
CC ECO:0000269|PubMed:27288407, ECO:0000269|PubMed:32358020}.
CC -!- SUBUNIT: Homodimer (PubMed:17473009). Interacts with SYK; participates
CC in leukocyte activation in presence of fungal pathogens
CC (PubMed:15845454). {ECO:0000269|PubMed:15845454,
CC ECO:0000269|PubMed:17473009}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779524,
CC ECO:0000269|PubMed:15213161}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:15213161}.
CC Note=Enriched on zymosan phagosomes. Enrichment does not depend on
CC opsonization.
CC -!- TISSUE SPECIFICITY: Detected in spleen (at protein level). Highly
CC expressed in dendritic cells, spleen and thymus. Detected in epidermal
CC Langerhans cells. Detected in macrophages, liver and lung.
CC {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:11544516,
CC ECO:0000269|PubMed:12719479}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10779524}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to beta-glucan
CC binding. {ECO:0000269|PubMed:12719479}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at the normal Mendelian ratio
CC without obvious anatomical defects but are susceptible to infection
CC with C.albicans (PubMed:17159984). They show impaired myeloid cell
CC activation by fungal particles (PubMed:17159984). Deficient leukocytes
CC display impaired responses to fungi, characterized by reduced
CC inflammatory cell recruitment after fungal infection, resulting in
CC substantially increased fungal burdens and enhanced fungal
CC dissemination (PubMed:32358020). {ECO:0000269|PubMed:17159984,
CC ECO:0000269|PubMed:32358020}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Mouse recombinant soluble Dectin-1 CTLD from insect cells origin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_793";
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DR EMBL; AF262985; AAF72710.1; -; mRNA.
DR EMBL; AY534909; AAS37670.1; -; mRNA.
DR EMBL; AC138620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027742; AAH27742.1; -; mRNA.
DR PDB; 2BPD; X-ray; 1.50 A; A/B=113-244.
DR PDB; 2BPE; X-ray; 2.25 A; A/B=113-244.
DR PDB; 2BPH; X-ray; 2.20 A; A/B=113-244.
DR PDB; 2CL8; X-ray; 2.80 A; A/B=113-244.
DR PDBsum; 2BPD; -.
DR PDBsum; 2BPE; -.
DR PDBsum; 2BPH; -.
DR PDBsum; 2CL8; -.
DR AlphaFoldDB; Q6QLQ4; -.
DR SMR; Q6QLQ4; -.
DR BioGRID; 208119; 1.
DR STRING; 10090.ENSMUSP00000107707; -.
DR ChEMBL; CHEMBL2034809; -.
DR UniLectin; Q6QLQ4; -.
DR GlyGen; Q6QLQ4; 2 sites.
DR iPTMnet; Q6QLQ4; -.
DR PhosphoSitePlus; Q6QLQ4; -.
DR MaxQB; Q6QLQ4; -.
DR PRIDE; Q6QLQ4; -.
DR ProteomicsDB; 283374; -.
DR Antibodypedia; 23238; 745 antibodies from 37 providers.
DR Ensembl; ENSMUST00000112076; ENSMUSP00000107707; ENSMUSG00000079293.
DR MGI; MGI:1861431; Clec7a.
DR VEuPathDB; HostDB:ENSMUSG00000079293; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161161; -.
DR InParanoid; Q6QLQ4; -.
DR PhylomeDB; Q6QLQ4; -.
DR TreeFam; TF336674; -.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR ChiTaRS; Clec7a; mouse.
DR EvolutionaryTrace; Q6QLQ4; -.
DR PRO; PR:Q6QLQ4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6QLQ4; protein.
DR Bgee; ENSMUSG00000079293; Expressed in granulocyte and 121 other tissues.
DR ExpressionAtlas; Q6QLQ4; baseline and differential.
DR Genevisible; Q6QLQ4; MM.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:UniProtKB.
DR GO; GO:0001874; F:(1->3)-beta-D-glucan immune receptor activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001846; F:opsonin binding; IDA:MGI.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:ARUK-UCL.
DR GO; GO:0030247; F:polysaccharide binding; IDA:MGI.
DR GO; GO:0061760; P:antifungal innate immune response; IDA:ARUK-UCL.
DR GO; GO:0001775; P:cell activation; IDA:ARUK-UCL.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0071226; P:cellular response to molecule of fungal origin; IDA:UniProtKB.
DR GO; GO:0016046; P:detection of fungus; IBA:GO_Central.
DR GO; GO:0032491; P:detection of molecule of fungal origin; IDA:UniProtKB.
DR GO; GO:0001879; P:detection of yeast; IDA:ARUK-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0002366; P:leukocyte activation involved in immune response; IDA:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IDA:UniProtKB.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IBA:GO_Central.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:ARUK-UCL.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:ARUK-UCL.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IMP:ARUK-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:ARUK-UCL.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IBA:GO_Central.
DR GO; GO:0051251; P:positive regulation of lymphocyte activation; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:ARUK-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:UniProtKB.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; IBA:GO_Central.
DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IMP:ARUK-UCL.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:ARUK-UCL.
DR GO; GO:0002238; P:response to molecule of fungal origin; IDA:MGI.
DR GO; GO:0001878; P:response to yeast; IDA:ARUK-UCL.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IDA:ARUK-UCL.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR042808; CLEC7A.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47218; PTHR47218; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Lectin; Membrane; Metal-binding;
KW Phosphoprotein; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..244
FT /note="C-type lectin domain family 7 member A"
FT /id="PRO_0000269493"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 126..241
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..18
FT /note="ITAM-like"
FT COMPBIAS 74..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145..152
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /evidence="ECO:0000305|PubMed:17473009,
FT ECO:0007744|PDB:2CL8"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:17473009,
FT ECO:0007744|PDB:2BPE, ECO:0007744|PDB:2BPH,
FT ECO:0007744|PDB:2CL8"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:17473009,
FT ECO:0007744|PDB:2BPE, ECO:0007744|PDB:2BPH,
FT ECO:0007744|PDB:2CL8"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:17473009,
FT ECO:0007744|PDB:2BPE, ECO:0007744|PDB:2BPH,
FT ECO:0007744|PDB:2CL8"
FT BINDING 194
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /evidence="ECO:0000305|PubMed:17473009,
FT ECO:0007744|PDB:2CL8"
FT BINDING 241
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:17473009,
FT ECO:0007744|PDB:2BPE, ECO:0007744|PDB:2BPH,
FT ECO:0007744|PDB:2CL8"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17473009"
FT DISULFID 147..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17473009"
FT DISULFID 219..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17473009"
FT MUTAGEN 221
FT /note="W->A: Loss of glucan binding. Abolishes activation
FT of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:15213161"
FT MUTAGEN 223
FT /note="H->A: Loss of glucan binding. Abolishes activation
FT of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:15213161"
FT MUTAGEN 232
FT /note="C->A: Abolishes cell surface expression."
FT /evidence="ECO:0000269|PubMed:15213161"
FT CONFLICT 37
FT /note="Q -> R (in Ref. 1; AAF72710, 2; AAS37670 and 4;
FT AAH27742)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..71
FT /note="GEYG -> AFWR (in Ref. 1; AAF72710, 2; AAS37670 and
FT 4; AAH27742)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="N -> S (in Ref. 2; AAS37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="L -> P (in Ref. 4; AAH27742)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="P -> S (in Ref. 1; AAF72710 and 2; AAS37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="I -> T (in Ref. 4; AAH27742)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..176
FT /note="RIN -> HIT (in Ref. 4; AAH27742)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="TA -> AV (in Ref. 2; AAS37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="A -> V (in Ref. 1; AAF72710)"
FT /evidence="ECO:0000305"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2BPD"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:2BPD"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:2BPD"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2BPD"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2BPD"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:2BPD"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2BPE"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2BPD"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2BPE"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2BPD"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:2BPD"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:2BPD"
SQ SEQUENCE 244 AA; 27420 MW; C9435DD135D2F122 CRC64;
MKYHSHIENL DEDGYTQLDF STQDIHKRPR GSEKGSQAPS SPWRPIAVGL GILCFVVVVV
AAVLGALGEY GHNSGRNPEE KDNFLSRNKE NHKPTESSLD EKVAPSKASQ TTGGFSQPCL
PNWIMHGKSC YLFSFSGNSW YGSKRHCSQL GAHLLKIDNS KEFEFIESQT SSHRINAFWI
GLSRNQSEGP WFWEDGSAFF PNSFQVRNTA PQESLLHNCV WIHGSEVYNQ ICNTSSYSIC
EKEL
