ID   BGBP1_MANSE             Reviewed;         487 AA.
AC   Q9NJ98;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Beta-1,3-glucan-binding protein 1;
DE            Short=BGBP-1;
DE   AltName: Full=Beta-1,3-glucan recognition protein 1;
DE            Short=BetaGRP-1;
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:AAF44011.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-42, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   GLYCOSYLATION.
RC   TISSUE=Fat body {ECO:0000312|EMBL:AAF44011.1}, and
RC   Larval hemolymph {ECO:0000269|PubMed:10713054};
RX   PubMed=10713054; DOI=10.1074/jbc.275.11.7505;
RA   Ma C., Kanost M.R.;
RT   "A beta1,3-glucan recognition protein from an insect, Manduca sexta,
RT   agglutinates microorganisms and activates the phenoloxidase cascade.";
RL   J. Biol. Chem. 275:7505-7514(2000).
RN   [2] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
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 activates the phenoloxidase
CC       cascade. Causes aggregation of invading microorganisms.
CC       {ECO:0000269|PubMed:10713054}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10713054}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10713054}.
CC   -!- TISSUE SPECIFICITY: Fat body and hemolymph.
CC       {ECO:0000269|PubMed:10713054}.
CC   -!- DEVELOPMENTAL STAGE: Expression is maintained at a moderate level
CC       during larval feeding and wandering stages.
CC       {ECO:0000269|PubMed:14976985}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10713054}.
CC   -!- MASS SPECTROMETRY: Mass=53583; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10713054};
CC   -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF177982; AAF44011.1; -; mRNA.
DR   AlphaFoldDB; Q9NJ98; -.
DR   SMR; Q9NJ98; -.
DR   CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   iPTMnet; Q9NJ98; -.
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..19
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:10713054"
FT   CHAIN           20..487
FT                   /note="Beta-1,3-glucan-binding protein 1"
FT                   /id="PRO_0000002821"
FT   DOMAIN          20..119
FT                   /note="CBM39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT   DOMAIN          157..487
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          123..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:10713054"
SQ   SEQUENCE   487 AA;  54567 MW;  3BA4869C5ADE934A CRC64;
     MLKSVFVLFL VNYLNSVRCL EVPDAKLEAI YPKGLRVSIP DDGYTLFAFH GKLNEEMEGL
     EAGHWSRDIT KAKNGRWIFR DRNAKLKIGD KIYFWTYILK DGLGYRQDNG EWTVTGYVNE
     DGEPLDANFE PRSTASTAAP PQAGAGQAPG PSYPCELSVS EVSVPGFVCK GQMLFEDNFN
     KPLADGRIWT PEIMFPGEPD YPFNVYMKET DNLHVGNGNL VIKPMPLVTA FGEDAIWKTL
     DLSDRCTGLL GTAQCKRDPS DAIIVPPIVT AKINTKKTFA FKYGRVEISA KMPRGDWLVP
     LIQLEPVNKN YGIRNYVSGL LRVACVKGNT EYIKTLVGGP IMSEAEPYRT ANLKEFISNE
     PWTNEFHNYT LEWSPDAITM AVDGIVYGRV TAPAGGFYKE ANEQNVEAAA RWIQGSNIAP
     FDDMFYISLG MDVGGVHEFP DEAINKPWKN TATKAMVNFW NARSQWNPTW LESEKALLVD
     YVRVYAL