GNBP1_DROME
ID GNBP1_DROME Reviewed; 494 AA.
AC Q9NHB0; Q9VVR5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Gram-negative bacteria-binding protein 1;
DE Flags: Precursor;
GN Name=GNBP1 {ECO:0000312|FlyBase:FBgn0040323}; ORFNames=CG6895;
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:AAF33849.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP 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] {ECO:0000312|EMBL:AAF49244.1}
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 [3]
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).
RN [4]
RP FUNCTION.
RX PubMed=16399077; DOI=10.1016/j.devcel.2005.11.013;
RA Jang I.H., Chosa N., Kim S.H., Nam H.J., Lemaitre B., Ochiai M.,
RA Kambris Z., Brun S., Hashimoto C., Ashida M., Brey P.T., Lee W.J.;
RT "A Spatzle-processing enzyme required for toll signaling activation in
RT Drosophila innate immunity.";
RL Dev. Cell 10:45-55(2006).
CC -!- FUNCTION: Plays a key role in innate immunity by acting as a pattern
CC recognition receptor for beta-1,3-glucan from fungi and
CC lipopolysaccharide from Gram-negative bacteria (PubMed:10827089). Upon
CC recognition of invading microorganism-derived products, acts upstream
CC of protease spz processing enzyme SPE to activate the Toll pathway and
CC to induce the expression of antimicrobial peptides drosomycin, cecropin
CC and attacin (PubMed:10827089, PubMed:16399077).
CC {ECO:0000269|PubMed:10827089, ECO:0000269|PubMed:16399077}.
CC -!- INTERACTION:
CC Q9NHB0; Q9VYX7: PGRP-SA; NbExp=4; IntAct=EBI-15721168, EBI-15721239;
CC Q9NHB0; Q9VS97: PGRP-SD; NbExp=4; IntAct=EBI-15721168, EBI-15721196;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827089};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10827089}. Note=Secreted
CC and attached to the membrane by a GPI-anchor.
CC -!- DEVELOPMENTAL STAGE: Expressed at moderate levels throughout the life
CC cycle. {ECO:0000269|PubMed:10827089}.
CC -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF33849.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF228472; AAF33849.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAF49244.1; -; Genomic_DNA.
DR RefSeq; NP_524142.2; NM_079418.3.
DR AlphaFoldDB; Q9NHB0; -.
DR SMR; Q9NHB0; -.
DR BioGRID; 65315; 3.
DR DIP; DIP-60776N; -.
DR IntAct; Q9NHB0; 2.
DR STRING; 7227.FBpp0074817; -.
DR CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GlyGen; Q9NHB0; 3 sites.
DR PaxDb; Q9NHB0; -.
DR DNASU; 40034; -.
DR EnsemblMetazoa; FBtr0075050; FBpp0074817; FBgn0040323.
DR GeneID; 40034; -.
DR KEGG; dme:Dmel_CG6895; -.
DR CTD; 40034; -.
DR FlyBase; FBgn0040323; GNBP1.
DR VEuPathDB; VectorBase:FBgn0040323; -.
DR eggNOG; ENOG502RY3C; Eukaryota.
DR GeneTree; ENSGT00940000173596; -.
DR HOGENOM; CLU_019533_2_0_1; -.
DR InParanoid; Q9NHB0; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q9NHB0; -.
DR BioGRID-ORCS; 40034; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40034; -.
DR PRO; PR:Q9NHB0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040323; Expressed in eye disc (Drosophila) and 19 other tissues.
DR ExpressionAtlas; Q9NHB0; baseline and differential.
DR Genevisible; Q9NHB0; DM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:FlyBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:FlyBase.
DR GO; GO:0006955; P:immune response; IEP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IDA:FlyBase.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
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 Cell membrane; Glycoprotein; GPI-anchor; Immunity; Innate immunity;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..494
FT /note="Gram-negative bacteria-binding protein 1"
FT /id="PRO_0000002817"
FT DOMAIN 20..120
FT /note="CBM39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT DOMAIN 135..494
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 126..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 230
FT /note="P -> R (in Ref. 1; AAF33849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55531 MW; 95172030E5E61FAB CRC64;
MPGLCIGILL LIGFGCTTAY KIPTPTVELL ETGFSVSIPD EEGVKVVAFN VNRNRNFTSF
INEGQYNVRL TEPQNGRWTT NFSSVPLRSQ DVLYLWTSVQ HQKAVYQDLA QPLPVCNLGG
EYRPRGCSPG DDDFTDDNQL STEDSALEPT APSVCEPSES QVSPQIGVSI CKGQLLFEET
FDQLNESLWI HDVRLPLDSK DAEFVLYDGK AKVHDGNLVI EPLLWSSYRP DLSIANSRLD
LSERCTGTHN RIKECILHST GSGPSGIMPP IVTPRISTKE TFAFQYGRIE IRAKLPKGDW
IVPLLLLEPL TEWYGQSGYE SGQLRVALAR GNSVLRMPRG KLVDGRSLYG GPVLSTDAHQ
REDLWLSKRK ISHFGDDFHT YSLDWSSNRL LFSVDGQVYG EMLNGFTELD ENPRWKQGGP
MAPFDKMFYI SLGVSVGGFG DFVDHLRTAT YEKPWANYHP QAKLQFHQAQ DQWLPTWKQP
ALKIDYVRVF ATDN
