BGBP_BOMMO
ID BGBP_BOMMO Reviewed; 495 AA.
AC Q9NL89;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
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:10671539, ECO:0000303|PubMed:19561300, ECO:0000303|PubMed:21697086, ECO:0000303|PubMed:3136171};
DE Short=BetaGRP {ECO:0000303|PubMed:10671539, ECO:0000303|PubMed:19561300, ECO:0000303|PubMed:21697086};
DE AltName: Full=Gram-negative bacteria-binding protein 3 {ECO:0000303|PubMed:19561300, ECO:0000303|PubMed:21697086};
DE Short=GNBP3 {ECO:0000303|PubMed:19561300, ECO:0000303|PubMed:21697086};
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA92243.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-84; 98-159; 183-199;
RP 241-274; 305-332; 346-389; 415-423 AND 464-495, FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION, AND MASS SPECTROMETRY.
RC STRAIN=Kinshu X Showa {ECO:0000312|EMBL:BAA92243.1};
RC TISSUE=Hemocyte {ECO:0000269|PubMed:10671539}, and
RC Larval hemolymph {ECO:0000269|PubMed:10671539};
RX PubMed=10671539; DOI=10.1074/jbc.275.7.4995;
RA Ochiai M., Ashida M.;
RT "A pattern-recognition protein for beta-1,3-glucan. The binding domain and
RT the cDNA cloning of beta-1,3-glucan recognition protein from the silkworm,
RT Bombyx mori.";
RL J. Biol. Chem. 275:4995-5002(2000).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBUNIT.
RX PubMed=3136171; DOI=10.1016/s0021-9258(18)37892-x;
RA Ochiai M., Ashida M.;
RT "Purification of a beta-1,3-glucan recognition protein in the
RT prophenoloxidase activating system from hemolymph of the silkworm, Bombyx
RT mori.";
RL J. Biol. Chem. 263:12056-12062(1988).
RN [3] {ECO:0007744|PDB:2RQE}
RP STRUCTURE BY NMR OF 17-118, FUNCTION, REGION, MUTAGENESIS OF TYR-17;
RP LEU-24; ALA-26; LYS-30; ARG-33; ASP-38; PHE-41; SER-42; HIS-61; SER-63;
RP ARG-64; LYS-68; LYS-70; ILE-75; PHE-76; ARG-77; ASP-78; ARG-79; ALA-81;
RP ALA-82; PHE-94; LEU-100; TYR-102; TRP-109; PHE-114 AND VAL-115, AND
RP CIRCULAR DICHROISM ANALYSIS.
RX PubMed=19561300; DOI=10.1073/pnas.0901671106;
RA Takahasi K., Ochiai M., Horiuchi M., Kumeta H., Ogura K., Ashida M.,
RA Inagaki F.;
RT "Solution structure of the silkworm betaGRP/GNBP3 N-terminal domain reveals
RT the mechanism for beta-1,3-glucan-specific recognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11679-11684(2009).
RN [4] {ECO:0007744|PDB:3AQX}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 17-118 IN COMPLEX WITH
RP LAMINARIHEXAOSE, AND FUNCTION.
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).
CC -!- FUNCTION: Involved in the recognition of invading microorganisms
CC activating the phenoloxidase cascade (PubMed:10671539, PubMed:3136171,
CC PubMed:19561300). Binds specifically to beta-1,3-glucan
CC (PubMed:10671539, PubMed:3136171, PubMed:19561300, PubMed:21697086).
CC Binds to both curdlan, a linear water-insoluble beta-1,3-glucan
CC polysaccharide, and laminarin, a water-soluble beta-1,3-glucan
CC polysaccharide containing beta-1,6 branches (PubMed:19561300).
CC {ECO:0000269|PubMed:10671539, ECO:0000269|PubMed:19561300,
CC ECO:0000269|PubMed:21697086, ECO:0000269|PubMed:3136171}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3136171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q76DI2}.
CC -!- TISSUE SPECIFICITY: Hemocytes, fat body and epidermal cells.
CC {ECO:0000269|PubMed:10671539}.
CC -!- INDUCTION: By bacterial and yeast infection.
CC {ECO:0000269|PubMed:10671539}.
CC -!- PTM: Glycosylated. {ECO:0000303|PubMed:10671539, ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=54594; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10671539};
CC -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC family. {ECO:0000305}.
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DR EMBL; AB026441; BAA92243.1; -; mRNA.
DR RefSeq; NP_001036840.1; NM_001043375.1.
DR PDB; 2RQE; NMR; -; A=17-118.
DR PDB; 3AQX; X-ray; 2.05 A; A/B=17-118.
DR PDBsum; 2RQE; -.
DR PDBsum; 3AQX; -.
DR AlphaFoldDB; Q9NL89; -.
DR SMR; Q9NL89; -.
DR STRING; 7091.BGIBMGA011608-TA; -.
DR CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GeneID; 692379; -.
DR KEGG; bmor:692379; -.
DR CTD; 692379; -.
DR eggNOG; ENOG502RVCU; Eukaryota.
DR HOGENOM; CLU_019533_2_0_1; -.
DR OrthoDB; 1209387at2759; -.
DR EvolutionaryTrace; Q9NL89; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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: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: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 Pfam; PF00722; Glyco_hydro_16; 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255, ECO:0000269|PubMed:10671539"
FT CHAIN 17..495
FT /note="Beta-1,3-glucan-binding protein"
FT /id="PRO_0000002816"
FT DOMAIN 17..116
FT /note="CBM39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT DOMAIN 188..495
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 17..118
FT /note="Binds to curdlan and laminarin"
FT /evidence="ECO:0000269|PubMed:19561300"
FT REGION 118..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21697086,
FT ECO:0007744|PDB:3AQX"
FT BINDING 92..94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21697086,
FT ECO:0007744|PDB:3AQX"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21697086,
FT ECO:0007744|PDB:3AQX"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT MUTAGEN 17
FT /note="Y->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 24
FT /note="L->A: Decreased binding affinity to curdlan to less
FT than 40% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 26
FT /note="A->Q: Decreased binding affinity to curdlan to less
FT than 40% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 30
FT /note="K->A: Increased binding affinity to curdlan compared
FT to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 33
FT /note="R->A: Decreased binding affinity to curdlan to less
FT than 70% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 38
FT /note="D->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 41
FT /note="F->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 42
FT /note="S->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 61
FT /note="H->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 63
FT /note="S->A: Decreased binding affinity to curdlan to less
FT than 90% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 64
FT /note="R->A: Increased binding affinity to curdlan compared
FT to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 68
FT /note="K->A: Decreased binding affinity to curdlan to less
FT than 80% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 70
FT /note="K->A: Decreased binding affinity to curdlan to less
FT than 80% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 75
FT /note="I->A: Slightly decreased binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 76
FT /note="F->A: Decreased binding affinity to curdlan to less
FT than 60% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 77
FT /note="R->A: Decreased binding affinity to curdlan to less
FT than 60% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 78
FT /note="D->A: Decreased binding affinity to curdlan to less
FT than 60% of the wild-type. Loss of ability to fully
FT initiate the activation of the phenoloxidase cascade by
FT beta-1,3-glucan."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 79
FT /note="R->A: Decreased binding affinity to curdlan to less
FT than 60% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 81
FT /note="A->Q: Decreased binding affinity to curdlan to less
FT than 60% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 82
FT /note="A->Q: Decreased binding affinity to curdlan to less
FT than 80% of the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 94
FT /note="F->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 100
FT /note="L->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 102
FT /note="Y->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 109
FT /note="W->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 114
FT /note="F->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT MUTAGEN 115
FT /note="V->A: No effect in binding affinity to curdlan
FT compared to the wild-type."
FT /evidence="ECO:0000269|PubMed:19561300"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:3AQX"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3AQX"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:3AQX"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2RQE"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3AQX"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3AQX"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3AQX"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:3AQX"
SQ SEQUENCE 495 AA; 55802 MW; 09249039F7456BF2 CRC64;
MYKTCVWVLL FKIVLCYEAP PATLEAIHPK GLRVSVPDEG FSLFAFHGKL NEEMEGLEAG
HWSRDITKPK NGRWIFRDRN AALKIGDKIY FWTFVIKDGL GYRQDNGEWT VEGFVDEAGN
PVNTEGSEIT PGVEFTSTSL NPESPQSIPN QPPDNLPAKP PSEGYPCELS LSTVSVPGFV
CKGQLLFEDQ FNIPIHRGKI WVPEVKFPGE PDFPFNVYLS DNAEVNDGKL IIKPATLESK
YGEDFVRQSL DLSERCTGTV GTAQCLREAS GPLILPPIIT AKISTRHQFA FKYGRVEIRA
KMPKGDWLYP EILLEPRDNI YGVRNYASGI LKIASVKGNA EFSKKLYAGP IMTGSDPYRS
FYLKENIGYE SWNNDFHNYT LEWRPDGITL LVDGESYGEI KPGEGFYNVA NSYKVEAAPQ
WLKGTIMAPF DELFYVSIGL NVAGIREFSE DISNKPWKNS ATKAMLKFWD ARSQWFPTWD
EDSALQVDYV KVFAI
