ID   BGBP_TENMO              Reviewed;         481 AA.
AC   Q76DI2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Beta-1,3-glucan-binding protein;
DE            Short=BGBP;
DE   AltName: Full=Beta-1,3-glucan recognition protein;
DE            Short=BetaGRP;
DE   Flags: Precursor;
GN   Name=GRP;
OS   Tenebrio molitor (Yellow mealworm beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrio.
OX   NCBI_TaxID=7067;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC99308.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 88-103; 159-173; 188-202;
RP   235-249; 290-301; 364-378 AND 419-430, FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Larva {ECO:0000269|PubMed:12923175}, and
RC   Larval hemolymph {ECO:0000269|PubMed:12923175};
RX   PubMed=12923175; DOI=10.1074/jbc.m307475200;
RA   Zhang R., Cho H.Y., Kim H.S., Ma Y.G., Osaki T., Kawbata S.,
RA   Soederhaell K., Lee B.L.;
RT   "Characterization and properties of a 1,3-beta-D-glucan pattern recognition
RT   protein of Tenebrio molitor larvae that is specifically degraded by serine
RT   protease during prophenoloxidase activation.";
RL   J. Biol. Chem. 278:42072-42079(2003).
CC   -!- FUNCTION: Involved in the recognition of invading microorganisms. Binds
CC       specifically to beta-1,3-glucan and activates the phenoloxidase
CC       cascade. {ECO:0000269|PubMed:12923175}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12923175}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:12923175}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12923175}.
CC   -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; AB108841; BAC99308.1; -; mRNA.
DR   AlphaFoldDB; Q76DI2; -.
DR   SMR; Q76DI2; -.
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:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; 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   Direct protein sequencing; Glycoprotein; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..481
FT                   /note="Beta-1,3-glucan-binding protein"
FT                   /id="PRO_0000002824"
FT   DOMAIN          19..123
FT                   /note="CBM39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT   DOMAIN          211..481
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   481 AA;  54075 MW;  AAA2CC8B623AECE3 CRC64;
     MKVLVVFIFC LVRSTFGQFE VPDALVEVFR PRGLRVSIPD QEGIKLFAFH GKINEEMNGR
     EGGTFSRDIL KAKNGRWTFY DANARLKEGD ILYYWTYVDY FDGKNKLGYP NDDQKFVVKQ
     LLDKDGAAPS VTPPTVTKAP PQEHTTLESG CKASVTTKVN ERVCAGEQIF HEDFTTFETN
     IWRPEVKFAD KPDYEFVFYR AGPPNLQVKH HRLTIRPVPS DAVFGEGFVS RREKVNLAPA
     CTGVHGSIEC VQTPGAFLIL PPVTSAQIST KGKWSFKYGK VEIRAKLPKG DWIYPELYLN
     PVNEEYGPGY ASGQIRIAFS GGNEDLCRDL RGGCILGSRP AARNYAVKNI VKNSGSWSDD
     FHKFIVIWKP DQITMMVDDQ VYGNIYPPEG GFVSEAYNLD LVNVERWRGG TSFAPFDKEM
     YLVLGVGVGG HCFEDRSDAT KPWTNNDPKS QKKFYQAAAQ WGATWSNASR LEVDYVKVSA
     L