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Reviewed, UniProtKB/Swiss-Prot Q9NHB0 (BGBP1_DROME)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Gram-negative bacteria-binding protein 1
Gene names
Name: GNBP1
ORF Names: CG6895
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in the recognition of invading micro-organisms. Binds specifically to beta-1,3-glucan and lipopolysaccharide and induces expression of the antimicrobial peptides drosomycin, cecropin and attacin. Ref.1

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor. Note: Secreted and attached to the membrane by a GPI-anchor. Ref.1

Developmental stage

Expressed at moderate levels throughout the life cycle. Ref.1

Sequence similarities

Belongs to the insect beta-1,3-glucan binding protein family.

Sequence caution

The sequence AAF33849.1 differs from that shown. Reason: Frameshift at positions 457 and 468.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 494475Gram-negative bacteria-binding protein 1
PRO_0000002817

Amino acid modifications

Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2301P → R in AAF33849. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NHB0-1 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 95172030E5E61FAB

FASTA49455,531
        10         20         30         40         50         60 
MPGLCIGILL LIGFGCTTAY KIPTPTVELL ETGFSVSIPD EEGVKVVAFN VNRNRNFTSF 

        70         80         90        100        110        120 
INEGQYNVRL TEPQNGRWTT NFSSVPLRSQ DVLYLWTSVQ HQKAVYQDLA QPLPVCNLGG 

       130        140        150        160        170        180 
EYRPRGCSPG DDDFTDDNQL STEDSALEPT APSVCEPSES QVSPQIGVSI CKGQLLFEET 

       190        200        210        220        230        240 
FDQLNESLWI HDVRLPLDSK DAEFVLYDGK AKVHDGNLVI EPLLWSSYRP DLSIANSRLD 

       250        260        270        280        290        300 
LSERCTGTHN RIKECILHST GSGPSGIMPP IVTPRISTKE TFAFQYGRIE IRAKLPKGDW 

       310        320        330        340        350        360 
IVPLLLLEPL TEWYGQSGYE SGQLRVALAR GNSVLRMPRG KLVDGRSLYG GPVLSTDAHQ 

       370        380        390        400        410        420 
REDLWLSKRK ISHFGDDFHT YSLDWSSNRL LFSVDGQVYG EMLNGFTELD ENPRWKQGGP 

       430        440        450        460        470        480 
MAPFDKMFYI SLGVSVGGFG DFVDHLRTAT YEKPWANYHP QAKLQFHQAQ DQWLPTWKQP 

       490 
ALKIDYVRVF ATDN 

« Hide

References

« Hide 'large scale' references
[1]"Gram-negative bacteria-binding protein, a pattern recognition receptor for lipopolysaccharide and beta-1,3-glucan that mediates the signaling for the induction of innate immune genes in Drosophila melanogaster cells."
Kim Y.-S., Ryu J.-H., Han S.-J., Choi K.-H., Nam K.-B., Jang I.-H., Lemaitre B., Brey P.T., Lee W.-J.
J. Biol. Chem. 275:32721-32727(2000) [PubMed: 10827089] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF228472 mRNA. Translation: AAF33849.1. Frameshift.
AE014296 Genomic DNA. Translation: AAF49244.1.
RefSeqNP_524142.2.
UniGeneDm.2810

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyCBM39. Carbohydrate-Binding Module Family 39.
GH16. Glycoside Hydrolase Family 16.

Genome annotation databases

EnsemblFBgn0040323. Drosophila melanogaster. [Contig view]
GeneID40034.
KEGGdme:Dmel_CG6895.

Organism-specific databases

FlyBaseFBgn0040323. GNBP1.

Phylogenomic databases

HOGENOMQ9NHB0.

Gene expression databases

ArrayExpressQ9NHB0.
GermOnlineCG6895. Drosophila melanogaster.

Family and domain databases

InterProIPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio816659.

Entry information

Entry nameBGBP1_DROME
AccessionPrimary (citable) accession number: Q9NHB0
Secondary accession number(s): Q9VVR5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: June 16, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents