ID   BGBP_HYPCU              Reviewed;         481 AA.
AC   O96363;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 76.
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   AltName: Full=Gram negative bacteria-binding protein;
DE   Flags: Precursor; Fragment;
GN   Name=gnbp1 {ECO:0000312|EMBL:AAD09290.1};
OS   Hyphantria cunea (Fall webworm moth) (Phalaena cunea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Erebidae; Arctiinae; Hyphantria.
OX   NCBI_TaxID=39466;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAD09290.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   TISSUE=Larva {ECO:0000269|PubMed:9818384};
RX   PubMed=9818384; DOI=10.1016/s0965-1748(98)00077-0;
RA   Shin S.W., Park S.-S., Park D.-S., Kim M.G., Kim S.C., Brey P.T.,
RA   Park H.-Y.;
RT   "Isolation and characterization of immune-related genes from the fall
RT   webworm, Hyphantria cunea, using PCR-based differential display and
RT   subtractive cloning.";
RL   Insect Biochem. Mol. Biol. 28:827-837(1998).
CC   -!- FUNCTION: Involved in the recognition of invading microorganisms. Binds
CC       specifically to beta-1,3-glucan and activates the phenoloxidase cascade
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q76DI2}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:9818384}.
CC   -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF023916; AAD09290.1; -; mRNA.
DR   AlphaFoldDB; O96363; -.
DR   CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GO; GO:0005576; C:extracellular region; ISS: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; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045088; P:regulation of innate immune response; ISS: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   2: Evidence at transcript level;
KW   Glycoprotein; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          <1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..481
FT                   /note="Beta-1,3-glucan-binding protein"
FT                   /id="PRO_0000002820"
FT   DOMAIN          20..120
FT                   /note="CBM39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT   DOMAIN          124..481
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAD09290.1"
SQ   SEQUENCE   481 AA;  53014 MW;  49B2AC8C406929F6 CRC64;
     RCARVCAVLF LFIQISYGQY QVPQVTVQAL KPRGFKASIP DSPSVSLFVF QGNINRAISK
     SDIGTISGEI LKAKDGRWTF EDPNVELKVG DVVNYYVVVV SNRGGYIKDN LSFTVSALED
     PSSTGTGTDP VPTPTTCRPT ATKLRSGVAC AGQTIFEENF NTFREDVWQI EQYIPVYSTE
     FPFVSYQHLS QDPTVAVTGG NLRITPKLQQ RMPGFTDSSI YSGSLNIFSG CTAPAEACMK
     DAWGASILPP VVSGRITSKA FAFTYGTVFV KAKLPQGDWI YPEILLEPFL KKYGSTHYSS
     GVIKIASARG NRELTSGYTD YSNKMLFGGP VMNLQCYDTL LESKASSNGR QWGDDFHEYV
     LRWAPERITL SVDGVEWARV EPTASGLSGR FPQTCSKLPR TFLAAGTKMA PFDDHFYLTL
     GVAAGSITEF PDGVQTSGSR PKPWTNTGSK AMLHFWEDMD SWFATWNQPQ LLVDYVKVVA
     L