BGBP_PLOIN
ID BGBP_PLOIN Reviewed; 488 AA.
AC Q8MU95;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Beta-1,3-glucan-binding protein {ECO:0000305};
DE Short=BGBP {ECO:0000305};
DE AltName: Full=Beta-1,3-glucan recognition protein {ECO:0000303|PubMed:12770576, ECO:0000303|PubMed:15084591, ECO:0000303|PubMed:21697086, ECO:0000303|PubMed:23237493};
DE Short=BetaGRP {ECO:0000303|PubMed:12770576, ECO:0000303|PubMed:15084591, ECO:0000303|PubMed:21697086, ECO:0000303|PubMed:23237493};
DE AltName: Full=Gram-negative bacteria-binding protein {ECO:0000303|PubMed:23237493};
DE Short=GNBP {ECO:0000303|PubMed:23237493};
DE AltName: Full=PibetaGRP {ECO:0000303|PubMed:15084591};
DE Flags: Precursor;
OS Plodia interpunctella (Indianmeal moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Pyralidae; Phycitinae; Plodia.
OX NCBI_TaxID=58824;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM95970.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-30, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PTM.
RC STRAIN=HD198 {ECO:0000312|EMBL:AAM95970.1};
RC TISSUE=Larva {ECO:0000269|PubMed:12770576}, and
RC Larval plasma {ECO:0000269|PubMed:12770576};
RX PubMed=12770576; DOI=10.1016/s0965-1748(03)00029-8;
RA Fabrick J.A., Baker J.E., Kanost M.R.;
RT "cDNA cloning, purification, properties and function of a beta-1,3-glucan
RT recognition protein from a pyralid moth, Plodia interpunctella.";
RL Insect Biochem. Mol. Biol. 33:579-594(2003).
RN [2]
RP PROTEIN SEQUENCE OF 21-26, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REGION,
RP AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=15084591; DOI=10.1074/jbc.m403382200;
RA Fabrick J.A., Baker J.E., Kanost M.R.;
RT "Innate immunity in a pyralid moth: functional evaluation of domains from a
RT beta-1,3-glucan recognition protein.";
RL J. Biol. Chem. 279:26605-26611(2004).
RN [3] {ECO:0007744|PDB:3AQY, ECO:0007744|PDB:3AQZ}
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 24-127 AND IN COMPLEX WITH
RP LAMINARIHEXAOSE, FUNCTION, REGION, AND MUTAGENESIS OF HIS-54; LEU-64;
RP ARG-71; ASP-72; TRP-99; TYR-101 AND ARG-110.
RX PubMed=21697086; DOI=10.1074/jbc.m111.256701;
RA Kanagawa M., Satoh T., Ikeda A., Adachi Y., Ohno N., Yamaguchi Y.;
RT "Structural insights into recognition of triple-helical beta-glucans by an
RT insect fungal receptor.";
RL J. Biol. Chem. 286:29158-29165(2011).
RN [4] {ECO:0007744|PDB:2KHA}
RP STRUCTURE BY NMR OF 18-135, FUNCTION, SUBUNIT, REGION, AND MUTAGENESIS OF
RP ASP-62.
RX PubMed=23237493; DOI=10.1021/bi301440p;
RA Dai H., Hiromasa Y., Takahashi D., VanderVelde D., Fabrick J.A.,
RA Kanost M.R., Krishnamoorthi R.;
RT "An initial event in the insect innate immune response: structural and
RT biological studies of interactions between beta-1,3-glucan and the N-
RT terminal domain of beta-1,3-glucan recognition protein.";
RL Biochemistry 52:161-170(2013).
CC -!- FUNCTION: Involved in the recognition of invading microorganisms
CC causing their aggregation (PubMed:12770576, PubMed:15084591). Activates
CC the phenoloxidase cascade (PubMed:12770576, PubMed:15084591,
CC PubMed:23237493). Binds specifically to beta-1,3-glucan
CC (PubMed:12770576, PubMed:15084591, PubMed:21697086, PubMed:23237493).
CC Binds to curdlan, a linear water-insoluble beta-1,3-glucan
CC polysaccharide, and to laminarin, a water-soluble beta-1,3-glucan
CC polysaccharide containing beta-1,6 branches (PubMed:15084591,
CC PubMed:21697086, PubMed:23237493). Binds also to lipopolysaccharide and
CC lipoteichoic acid (PubMed:15084591). {ECO:0000269|PubMed:12770576,
CC ECO:0000269|PubMed:15084591, ECO:0000269|PubMed:21697086,
CC ECO:0000269|PubMed:23237493}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Denaturates after heat treatment at 100 degrees Celsius for 10 min.
CC The N-terminal region (18-198) is thermostable and retains its
CC ability to bind to curdlan after heat treatment at 100 degrees
CC Celsius for 10 min. The C-terminal region (199-488) is heat-labile
CC after the same treatment. {ECO:0000269|PubMed:15084591};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12770576,
CC ECO:0000269|PubMed:23237493}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12770576}.
CC -!- TISSUE SPECIFICITY: Fat body and hemolymph.
CC {ECO:0000269|PubMed:12770576}.
CC -!- DEVELOPMENTAL STAGE: Expression is maintained at a moderate level
CC throughout development from embryo to adult.
CC {ECO:0000269|PubMed:12770576}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12770576}.
CC -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC family. {ECO:0000305}.
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DR EMBL; AF532603; AAM95970.1; -; mRNA.
DR PDB; 2KHA; NMR; -; A=18-135.
DR PDB; 3AQY; X-ray; 1.58 A; A/B=24-127.
DR PDB; 3AQZ; X-ray; 2.20 A; A/B=24-127.
DR PDBsum; 2KHA; -.
DR PDBsum; 3AQY; -.
DR PDBsum; 3AQZ; -.
DR AlphaFoldDB; Q8MU95; -.
DR BMRB; Q8MU95; -.
DR SMR; Q8MU95; -.
DR CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IDA:UniProtKB.
DR GO; GO:0070891; F:lipoteichoic acid binding; IDA:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0001873; F:polysaccharide immune receptor activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB.
DR CDD; cd02179; GH16_beta_GRP; 1.
DR Gene3D; 2.60.40.2140; -; 1.
DR InterPro; IPR031756; BGBP_N.
DR InterPro; IPR043030; BGBP_N_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR035806; GH16_GRP_C.
DR Pfam; PF15886; CBM39; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51969; CBM39; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Immunity;
KW Innate immunity; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..488
FT /note="Beta-1,3-glucan-binding protein"
FT /id="PRO_0000002823"
FT DOMAIN 24..123
FT /note="CBM39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT DOMAIN 144..488
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 18..198
FT /note="Binds to curdlan, lipopolysaccharide and
FT lipoteichoic acid, activates the phenoloxidase cascade and
FT is resistant to proteolytic degradation by trypsin or
FT chymotrypsin, but is not as effective as the full-length
FT protein in aggregation of microorganisms"
FT /evidence="ECO:0000269|PubMed:15084591"
FT REGION 18..135
FT /note="Binds to curdlan, laminarihexaose and laminarin. The
FT complex formation with laminarin induces self-association
FT of the complexes into a macro structure, likely containing
FT six protein and three laminarin molecules. The macro
FT structures may form a platform on a microbial surface for
FT recruitment of downstream proteases, as a means of
FT amplification of the initial signal of pathogen recognition
FT for the activation of the phenoloxidase cascade"
FT /evidence="ECO:0000269|PubMed:23237493"
FT REGION 24..127
FT /note="Binds to laminarihexaose and laminarin"
FT /evidence="ECO:0000269|PubMed:21697086"
FT REGION 125..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..488
FT /note="Binds to laminarin, but not to curdlan, does not
FT activate the phenoloxidase cascade, is susceptible to
FT proteinase digestion by trypsin or chymotrypsin and does
FT not cause aggregation of microorganisms"
FT /evidence="ECO:0000269|PubMed:15084591"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21697086,
FT ECO:0007744|PDB:3AQZ"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21697086,
FT ECO:0007744|PDB:3AQZ"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21697086,
FT ECO:0007744|PDB:3AQZ"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 54
FT /note="H->A: Reduced binding affinity to laminarin by the
FT N-terminal domain. Loss of binding to laminarin by the N-
FT terminal domain; when associated with A-71."
FT /evidence="ECO:0000269|PubMed:21697086"
FT MUTAGEN 62
FT /note="D->A: No effect in binding to curdlan or laminarin
FT by the N-terminal domain. No effect in stability of the N-
FT terminal domain and laminarin macro structures nor in
FT activation of the phenoloxidase cascade."
FT /evidence="ECO:0000269|PubMed:23237493"
FT MUTAGEN 62
FT /note="D->K: No effect in binding to curdlan or laminarin
FT by the N-terminal domain. Reduced stability of the N-
FT terminal domain and laminarin macro structures accompanied
FT by a reduced level of activation of the phenoloxidase
FT cascade."
FT /evidence="ECO:0000269|PubMed:23237493"
FT MUTAGEN 64
FT /note="L->A: Reduced binding affinity to laminarin by the
FT N-terminal domain."
FT /evidence="ECO:0000269|PubMed:21697086"
FT MUTAGEN 71
FT /note="R->A: Loss of binding to laminarin by the N-terminal
FT domain; when associated with A-54. Reduced binding affinity
FT to laminarin by the N-terminal domain; when associated with
FT A-110."
FT /evidence="ECO:0000269|PubMed:21697086"
FT MUTAGEN 72
FT /note="D->A: Loss of binding to laminarin by the N-terminal
FT domain."
FT /evidence="ECO:0000269|PubMed:21697086"
FT MUTAGEN 99
FT /note="W->A: Loss of binding to laminarin by the N-terminal
FT domain."
FT /evidence="ECO:0000269|PubMed:21697086"
FT MUTAGEN 101
FT /note="Y->A: No effect in binding to laminarin by the N-
FT terminal domain."
FT /evidence="ECO:0000269|PubMed:21697086"
FT MUTAGEN 110
FT /note="R->A: Reduced binding affinity to laminarin by the
FT N-terminal domain. Reduced binding affinity to laminarin by
FT the N-terminal domain; when associated with A-71."
FT /evidence="ECO:0000269|PubMed:21697086"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:3AQY"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2KHA"
SQ SEQUENCE 488 AA; 55213 MW; 38E21D6C94D446F5 CRC64;
MFVTFICFLA CLTCSYGQPR AQQYVVPSAK LEAIYPKGLR VSIPDDGFSL FAFHGKLNEE
MDGLEAGHWA RDITKPKEGR WTFRDRNVKL KLGDKIYFWT YVIKDGLGYR QDNGEWTVTE
FVNEDGTPAD TSLEPTTAPT PVRPDQPNQP IPTHRPDPPC TVSATMVDGR KSVCQGTLLF
SEEFEKANLK DLANWEAEVK FPEEPDYPFN VYMVDGTLEL EDGSLVLTPK LLESRFHAGI
LNDALDLTNR CSGQVDTTEC RRQASGAQIL PPVMTGKITT KNKFTFKFGR VEVRAKLPAG
NWLLPEINLE PKDNVFGSRR YESGLMRVAF AKGNAVFAKK LNGGPVLADT EPFRSLLMKE
KIGIDNWNRD YHNYTLIWKQ DGIDMLVDGE KYGSISPGEG FYALGREHAV PHAAHWLRGS
VMAPLDQYFF LSLGLRVGGV HDFADSPDKP WKNRSNKAVL NFWNDRDNWF PTWFDANLKV
DYVRVYAL
