ID   BGBP2_MANSE             Reviewed;         482 AA.
AC   Q8ISB6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Beta-1,3-glucan-binding protein 2;
DE            Short=BGBP-2;
DE   AltName: Full=Beta-1,3-glucan recognition protein 2;
DE            Short=BetaGRP-2;
DE   Flags: Precursor;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN10151.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-45, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION,
RP   GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   TISSUE=Cuticle {ECO:0000269|PubMed:14976985}, and
RC   Fat body {ECO:0000269|PubMed:14976985};
RX   PubMed=14976985; DOI=10.1016/j.ibmb.2003.09.006;
RA   Jiang H., Ma C., Lu Z.-Q., Kanost M.R.;
RT   "Beta-1,3-glucan recognition protein-2 (betaGRP-2) from Manduca sexta: an
RT   acute-phase protein that binds beta-1,3-glucan and lipoteichoic acid to
RT   aggregate fungi and bacteria and stimulate prophenoloxidase activation.";
RL   Insect Biochem. Mol. Biol. 34:89-100(2004).
CC   -!- FUNCTION: Involved in the recognition of invading microorganisms. Binds
CC       specifically to beta-1,3-glucan and lipoteichoic acid and causes
CC       aggregation of invading microorganisms. Binding to beta-1,3-glucan
CC       activates the phenoloxidase cascade. {ECO:0000269|PubMed:14976985}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14976985}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14976985}.
CC   -!- TISSUE SPECIFICITY: Cuticle and fat body.
CC       {ECO:0000269|PubMed:14976985}.
CC   -!- DEVELOPMENTAL STAGE: Expression levels are low during larval feeding
CC       stages and increase dramatically at the start of the wandering stage.
CC       {ECO:0000269|PubMed:14976985}.
CC   -!- INDUCTION: By bacterial and yeast infection.
CC       {ECO:0000269|PubMed:14976985}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14976985}.
CC   -!- MASS SPECTROMETRY: Mass=54920; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14976985};
CC   -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; AY135522; AAN10151.1; -; mRNA.
DR   AlphaFoldDB; Q8ISB6; -.
DR   BMRB; Q8ISB6; -.
DR   SMR; Q8ISB6; -.
DR   CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PRIDE; Q8ISB6; -.
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:0038187; F:pattern recognition 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   Direct protein sequencing; Glycoprotein; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:14976985"
FT   CHAIN           19..482
FT                   /note="Beta-1,3-glucan-binding protein 2"
FT                   /id="PRO_0000002822"
FT   DOMAIN          23..122
FT                   /note="CBM39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT   DOMAIN          128..482
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          127..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   482 AA;  54414 MW;  233755F7AD37E8A2 CRC64;
     MWIKSVCLFA TIAGCLGQRG GPYKVPDAKL EAIYPKGLRV SVPDDGYSLF AFHGKLNEEM
     EGLEAGHWSR DITKAKQGRW IFRDRNAELK LGDKIYFWTY VIKDGLGYRQ DNGEWTVTEF
     VNENGTVVDT STAPPPVAPA VSEEDQSPGP QWRPCERSLT ESLARERVCK GSLVFSEDFD
     GSSLADLGNW TAEVRFPGEP DYPYNLYTTD GTVGFESGSL VVRPVMTESK YHEGIIYDRL
     DLERCTGQLG TLECRRESSG GQIVPPVMTA KLATRRSFAF KFGRIDIKAK MPRGDWLIPE
     LNLEPLDNIY GNQRYASGLM RVAFVRGNDV YAKKLYGGPI MSDADPFRSM LLKDKQGLAN
     WNNDYHVYSL LWKPNGLELM VDGEVYGTID AGDGFYQIAK NNLVSHASQW LKGTVMAPFD
     EKFFITLGLR VAGIHDFTDG PGKPWENKGT KAMINFWNNR FRWFPTWHDT SLKVDYVRVY
     AL