BGBP3_DROME
ID BGBP3_DROME Reviewed; 490 AA.
AC Q9NHA8; A0ZX55; A0ZX56; A0ZX59; A0ZX64; Q9VSR4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Gram-negative bacteria-binding protein 3;
DE Flags: Precursor;
GN Name=GNBP3 {ECO:0000312|FlyBase:FBgn0040321}; ORFNames=CG5008;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF33851.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=10827089; DOI=10.1074/jbc.m003934200;
RA Kim Y.-S., Ryu J.-H., Han S.-J., Choi K.-H., Nam K.-B., Jang I.-H.,
RA Lemaitre B., Brey P.T., Lee W.-J.;
RT "Gram-negative bacteria-binding protein, a pattern recognition receptor for
RT lipopolysaccharide and beta-1,3-glucan that mediates the signaling for the
RT induction of innate immune genes in Drosophila melanogaster cells.";
RL J. Biol. Chem. 275:32721-32727(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Netherlands line N01, Netherlands line N02, Netherlands line N03,
RC Netherlands line N06, Netherlands line N07, Netherlands line N14,
RC Netherlands line N15, Netherlands line N16, Netherlands line N17,
RC Netherlands line N22, Netherlands line N29, and Netherlands line N30;
RX PubMed=17103056; DOI=10.1007/s00239-006-0005-2;
RA Jiggins F.M., Kim K.W.;
RT "Contrasting evolutionary patterns in Drosophila immune receptors.";
RL J. Mol. Evol. 63:769-780(2006).
RN [3] {ECO:0000312|EMBL:AAF50349.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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:Q8MU95}.
CC -!- DEVELOPMENTAL STAGE: Expressed at very low levels during embryonic
CC development. Expression increases during the larva stages and peaks at
CC a moderate level during the late larval, prepupal and pupal stages,
CC before decreasing in the adult. {ECO:0000269|PubMed:10827089}.
CC -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC family. {ECO:0000305}.
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DR EMBL; AF228474; AAF33851.1; -; mRNA.
DR EMBL; AM050231; CAJ18903.1; -; Genomic_DNA.
DR EMBL; AM050232; CAJ18904.1; -; Genomic_DNA.
DR EMBL; AM050233; CAJ18905.1; -; Genomic_DNA.
DR EMBL; AM050234; CAJ18906.1; -; Genomic_DNA.
DR EMBL; AM050235; CAJ18907.1; -; Genomic_DNA.
DR EMBL; AM050236; CAJ18908.1; -; Genomic_DNA.
DR EMBL; AM050237; CAJ18909.1; -; Genomic_DNA.
DR EMBL; AM050238; CAJ18910.1; -; Genomic_DNA.
DR EMBL; AM050239; CAJ18911.1; -; Genomic_DNA.
DR EMBL; AM050240; CAJ18912.1; -; Genomic_DNA.
DR EMBL; AM050241; CAJ18913.1; -; Genomic_DNA.
DR EMBL; AM050242; CAJ18914.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50349.1; -; Genomic_DNA.
DR RefSeq; NP_523986.2; NM_079262.3.
DR PDB; 3IE4; X-ray; 1.45 A; A/B=26-132.
DR PDBsum; 3IE4; -.
DR AlphaFoldDB; Q9NHA8; -.
DR SMR; Q9NHA8; -.
DR BioGRID; 64425; 3.
DR IntAct; Q9NHA8; 1.
DR STRING; 7227.FBpp0076237; -.
DR CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GlyGen; Q9NHA8; 2 sites.
DR PaxDb; Q9NHA8; -.
DR PRIDE; Q9NHA8; -.
DR EnsemblMetazoa; FBtr0076510; FBpp0076237; FBgn0040321.
DR GeneID; 39020; -.
DR KEGG; dme:Dmel_CG5008; -.
DR CTD; 39020; -.
DR FlyBase; FBgn0040321; GNBP3.
DR VEuPathDB; VectorBase:FBgn0040321; -.
DR eggNOG; ENOG502RVCU; Eukaryota.
DR GeneTree; ENSGT00940000165988; -.
DR HOGENOM; CLU_019533_2_0_1; -.
DR InParanoid; Q9NHA8; -.
DR OMA; HNYTLEW; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q9NHA8; -.
DR SignaLink; Q9NHA8; -.
DR BioGRID-ORCS; 39020; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q9NHA8; -.
DR GenomeRNAi; 39020; -.
DR PRO; PR:Q9NHA8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040321; Expressed in eye disc (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q9NHA8; baseline and differential.
DR Genevisible; Q9NHA8; DM.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:FlyBase.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:FlyBase.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:FlyBase.
DR GO; GO:0019732; P:antifungal humoral response; IMP:FlyBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0032491; P:detection of molecule of fungal origin; IDA:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; ISS:FlyBase.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035008; P:positive regulation of melanization defense response; IMP:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IGI:FlyBase.
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 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Immunity; Innate immunity; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..490
FT /note="Gram-negative bacteria-binding protein 3"
FT /id="PRO_0000002819"
FT DOMAIN 26..126
FT /note="CBM39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT DOMAIN 162..490
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 16
FT /note="L -> Q (in strain: Netherlands line N22)"
FT VARIANT 142
FT /note="P -> T (in strain: Netherlands line N02 and
FT Netherlands line N30)"
FT VARIANT 213
FT /note="P -> L (in strain: Netherlands line N02, Netherlands
FT line N07, Netherlands line N17 and Netherlands line N30)"
FT VARIANT 292
FT /note="A -> V (in strain: Netherlands line N02 and
FT Netherlands line N30)"
FT VARIANT 399
FT /note="K -> I (in strain: Netherlands line N22)"
FT VARIANT 404
FT /note="E -> G (in strain: Netherlands line N02 and
FT Netherlands line N30)"
FT VARIANT 408
FT /note="A -> G (in strain: Netherlands line N22)"
FT VARIANT 479
FT /note="H -> N (in strain: Netherlands line N22)"
FT CONFLICT 196
FT /note="R -> K (in Ref. 1; AAF33851)"
FT /evidence="ECO:0000305"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:3IE4"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3IE4"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:3IE4"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3IE4"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:3IE4"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:3IE4"
FT STRAND 110..120
FT /evidence="ECO:0007829|PDB:3IE4"
SQ SEQUENCE 490 AA; 55211 MW; B442E16CC027D849 CRC64;
MADALRFVAW SCCLQLLFLL LGVQGYEVPK AKIDVFYPKG FEVSIPDEEG ITLFAFHGKL
NEEMEGLEAG TWARDIVKAK NGRWTFRDRI TALKPGDTLY YWTYVIYNGL GYREDDGSFV
VNGYSGNNAS PHPPVVPVST TPWTPPADPD IDIRLGCTTP KTEVNGAPTR CAGQLVFVDE
FNAAKLDPNK WKAERRFSGQ PDYEFNVYVD DAPETLCLAN GHVVLSTNTM KKQFKKGSGE
SLDLGEKCTG QANTHDCVRN GRTLNDGLPP MVTAQFSSKD FSFKYGRVEV RAKMPRAQWV
TPQIWLQPRR PIYGVDDYRS GQLRIAYTRP NGGNLDLYGA AVLFADEPLR SVKNCLKPGT
GNNSEDWSDS FHNYTLEWTP RELRWLVDGK EWCVQGSAKG SFSETTAAGK SLPQAQKLEE
GTGLAPFDQE FYLTFGLSVG GFNEYQHEIK PWNERAPQAQ KAFWKEVKKI RDHWLDEGHM
KIDYVKVYSL
