BGBP2_DROME
ID BGBP2_DROME Reviewed; 461 AA.
AC Q9VVR4; A0ZWZ5; A0ZWZ8; A0ZX11; A0ZX12; A0ZX13; A0ZX39; A0ZX40; A0ZX41;
AC A0ZX42; Q8IQT6; Q8IQT7; Q95U68; Q9NHA9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Gram-negative bacteria-binding protein 2;
DE Flags: Precursor;
GN Name=GNBP2 {ECO:0000312|EMBL:AAF49245.3}; ORFNames=CG4144;
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:AAF33850.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), 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], AND ALTERNATIVE SPLICING.
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:AAF49245.3}
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, AND ALTERNATIVE SPLICING.
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).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAL13506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(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:Q9NHB0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B {ECO:0000269|PubMed:10827089};
CC IsoId=Q9VVR4-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9VVR4-3; Sequence=VSP_026674;
CC Name=C {ECO:0000305};
CC IsoId=Q9VVR4-2; Sequence=VSP_051600, VSP_051601, VSP_051602;
CC Name=D;
CC IsoId=Q9VVR4-4; Sequence=VSP_051600;
CC -!- DEVELOPMENTAL STAGE: Expressed at very low levels during embryonic
CC development and at moderate levels in the larva, prepupal, pupal and
CC adult stages. {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; AF228473; AAF33850.1; -; mRNA.
DR EMBL; AM050207; CAJ19007.1; -; Genomic_DNA.
DR EMBL; AM050207; CAJ19008.1; -; Genomic_DNA.
DR EMBL; AM050207; CAJ19009.1; -; Genomic_DNA.
DR EMBL; AM050207; CAJ19010.1; -; Genomic_DNA.
DR EMBL; AM050208; CAJ19011.1; -; Genomic_DNA.
DR EMBL; AM050208; CAJ19012.1; -; Genomic_DNA.
DR EMBL; AM050208; CAJ19013.1; -; Genomic_DNA.
DR EMBL; AM050208; CAJ19014.1; -; Genomic_DNA.
DR EMBL; AM050209; CAJ19015.1; -; Genomic_DNA.
DR EMBL; AM050209; CAJ19016.1; -; Genomic_DNA.
DR EMBL; AM050209; CAJ19017.1; -; Genomic_DNA.
DR EMBL; AM050209; CAJ19018.1; -; Genomic_DNA.
DR EMBL; AM050210; CAJ19019.1; -; Genomic_DNA.
DR EMBL; AM050210; CAJ19020.1; -; Genomic_DNA.
DR EMBL; AM050210; CAJ19021.1; -; Genomic_DNA.
DR EMBL; AM050210; CAJ19022.1; -; Genomic_DNA.
DR EMBL; AM050211; CAJ19023.1; -; Genomic_DNA.
DR EMBL; AM050211; CAJ19024.1; -; Genomic_DNA.
DR EMBL; AM050211; CAJ19025.1; -; Genomic_DNA.
DR EMBL; AM050211; CAJ19026.1; -; Genomic_DNA.
DR EMBL; AM050212; CAJ19027.1; -; Genomic_DNA.
DR EMBL; AM050212; CAJ19028.1; -; Genomic_DNA.
DR EMBL; AM050212; CAJ19029.1; -; Genomic_DNA.
DR EMBL; AM050212; CAJ19030.1; -; Genomic_DNA.
DR EMBL; AM050213; CAJ19031.1; -; Genomic_DNA.
DR EMBL; AM050213; CAJ19032.1; -; Genomic_DNA.
DR EMBL; AM050213; CAJ19033.1; -; Genomic_DNA.
DR EMBL; AM050213; CAJ19034.1; -; Genomic_DNA.
DR EMBL; AM050214; CAJ19035.1; -; Genomic_DNA.
DR EMBL; AM050214; CAJ19036.1; -; Genomic_DNA.
DR EMBL; AM050214; CAJ19037.1; -; Genomic_DNA.
DR EMBL; AM050214; CAJ19038.1; -; Genomic_DNA.
DR EMBL; AM050215; CAJ19039.1; -; Genomic_DNA.
DR EMBL; AM050215; CAJ19040.1; -; Genomic_DNA.
DR EMBL; AM050215; CAJ19041.1; -; Genomic_DNA.
DR EMBL; AM050215; CAJ19042.1; -; Genomic_DNA.
DR EMBL; AM050216; CAJ19043.1; -; Genomic_DNA.
DR EMBL; AM050216; CAJ19044.1; -; Genomic_DNA.
DR EMBL; AM050216; CAJ19045.1; -; Genomic_DNA.
DR EMBL; AM050216; CAJ19046.1; -; Genomic_DNA.
DR EMBL; AM050217; CAJ19047.1; -; Genomic_DNA.
DR EMBL; AM050217; CAJ19048.1; -; Genomic_DNA.
DR EMBL; AM050217; CAJ19049.1; -; Genomic_DNA.
DR EMBL; AM050217; CAJ19050.1; -; Genomic_DNA.
DR EMBL; AM050218; CAJ19051.1; -; Genomic_DNA.
DR EMBL; AM050218; CAJ19052.1; -; Genomic_DNA.
DR EMBL; AM050218; CAJ19053.1; -; Genomic_DNA.
DR EMBL; AM050218; CAJ19054.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49245.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF49246.3; -; Genomic_DNA.
DR EMBL; AE014296; AAN11665.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11666.1; -; Genomic_DNA.
DR EMBL; AY058277; AAL13506.1; -; mRNA.
DR RefSeq; NP_524141.1; NM_079417.3. [Q9VVR4-1]
DR RefSeq; NP_730350.1; NM_168771.2. [Q9VVR4-3]
DR RefSeq; NP_730351.1; NM_168772.2. [Q9VVR4-4]
DR AlphaFoldDB; Q9VVR4; -.
DR SMR; Q9VVR4; -.
DR BioGRID; 65314; 1.
DR STRING; 7227.FBpp0074861; -.
DR CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GlyGen; Q9VVR4; 4 sites.
DR PaxDb; Q9VVR4; -.
DR PRIDE; Q9VVR4; -.
DR DNASU; 40033; -.
DR EnsemblMetazoa; FBtr0075094; FBpp0074861; FBgn0040322. [Q9VVR4-1]
DR EnsemblMetazoa; FBtr0075095; FBpp0074862; FBgn0040322. [Q9VVR4-3]
DR EnsemblMetazoa; FBtr0075096; FBpp0074863; FBgn0040322. [Q9VVR4-4]
DR GeneID; 40033; -.
DR KEGG; dme:Dmel_CG4144; -.
DR CTD; 40033; -.
DR FlyBase; FBgn0040322; GNBP2.
DR VEuPathDB; VectorBase:FBgn0040322; -.
DR eggNOG; ENOG502RTM3; Eukaryota.
DR GeneTree; ENSGT00940000173596; -.
DR InParanoid; Q9VVR4; -.
DR OMA; DTWAPTW; -.
DR PhylomeDB; Q9VVR4; -.
DR BioGRID-ORCS; 40033; 0 hits in 1 CRISPR screen.
DR ChiTaRS; GNBP2; fly.
DR GenomeRNAi; 40033; -.
DR PRO; PR:Q9VVR4; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040322; Expressed in second segment of antenna (Drosophila) and 16 other tissues.
DR ExpressionAtlas; Q9VVR4; baseline and differential.
DR Genevisible; Q9VVR4; DM.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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: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 Alternative splicing; Glycoprotein; Immunity; Innate immunity;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..461
FT /note="Gram-negative bacteria-binding protein 2"
FT /id="PRO_0000002818"
FT DOMAIN 21..115
FT /note="CBM39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT DOMAIN 179..461
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_051600"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_026674"
FT VAR_SEQ 291..292
FT /note="YL -> CE (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_051601"
FT VAR_SEQ 293..461
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_051602"
FT VARIANT 75
FT /note="V -> G (in strain: Netherlands line N30)"
FT VARIANT 400
FT /note="I -> M (in strain: Netherlands line N07 and
FT Netherlands line N14)"
SQ SEQUENCE 461 AA; 52856 MW; F62524B64CBE150D CRC64;
MRWEFLPCLL LLISNNKIFG FKVPSINFEM LKDEGFEVSI PDEPGIQRVF YMFQIDDTCP
ALMDYITEAV NGSWVSKQKM SLQNNDKLQI SMLVQFNEEI FEKSETRVII NTRLLTTKDS
SSRGITFLTG EGECQAYLAP AQQAKRCKAA QTIVSNGRHT CQGELIFEDN FSEAQLNKTT
WKHDIRQRMY HVEEELVAFD DAARNCFVKE GELHIVPTIA TEVTDGSFKL GDRCTAVESP
EQECNIAHGI FYSIKPPVFS AQIHTRNSFS FKFGKIVVRA KLPKGDWLFP YLMLQPVSTY
AETHYAKQLR IAYARGNANL RTKQGDDISG NHLYGGGVVW HHGNAVQFLK DKISNSHYGD
DFHNYTMIWQ RDKITLMVDD EVYGELYDGL PFFNEKCFII FGVTVGGFLN FDDSLLAKDV
KPYKNREPRA ALSFWQHRDA WAPTWGRHSA MVIDYVRVYA E
