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Q9VVR4 (BGBP2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gram-negative bacteria-binding protein 2
Gene names
Name:GNBP2
ORF Names:CG4144
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length461 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 activates the phenoloxidase cascade By similarity. UniProtKB Q9NHB0

Subcellular location

Secreted By similarity UniProtKB Q9NHB0.

Developmental stage

Expressed at very low levels during embryonic development and at moderate levels in the larva, prepupal, pupal and adult stages. Ref.1

Sequence similarities

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform B Ref.1 (identifier: Q9VVR4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: Q9VVR4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
Isoform C (identifier: Q9VVR4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
     291-292: YL → CE
     293-461: Missing.
Isoform D (identifier: Q9VVR4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 461441Gram-negative bacteria-binding protein 2
PRO_0000002818

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 5151Missing in isoform C and isoform D.
VSP_051600
Alternative sequence1 – 2929Missing in isoform A.
VSP_026674
Alternative sequence291 – 2922YL → CE in isoform C.
VSP_051601
Alternative sequence293 – 461169Missing in isoform C.
VSP_051602
Natural variant751V → G in strain: Netherlands line N30.
Natural variant4001I → M in strain: Netherlands line N07 and Netherlands line N14.

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified October 1, 2002. Version 3.
Checksum: F62524B64CBE150D

FASTA46152,856
        10         20         30         40         50         60 
MRWEFLPCLL LLISNNKIFG FKVPSINFEM LKDEGFEVSI PDEPGIQRVF YMFQIDDTCP 

        70         80         90        100        110        120 
ALMDYITEAV NGSWVSKQKM SLQNNDKLQI SMLVQFNEEI FEKSETRVII NTRLLTTKDS 

       130        140        150        160        170        180 
SSRGITFLTG EGECQAYLAP AQQAKRCKAA QTIVSNGRHT CQGELIFEDN FSEAQLNKTT 

       190        200        210        220        230        240 
WKHDIRQRMY HVEEELVAFD DAARNCFVKE GELHIVPTIA TEVTDGSFKL GDRCTAVESP 

       250        260        270        280        290        300 
EQECNIAHGI FYSIKPPVFS AQIHTRNSFS FKFGKIVVRA KLPKGDWLFP YLMLQPVSTY 

       310        320        330        340        350        360 
AETHYAKQLR IAYARGNANL RTKQGDDISG NHLYGGGVVW HHGNAVQFLK DKISNSHYGD 

       370        380        390        400        410        420 
DFHNYTMIWQ RDKITLMVDD EVYGELYDGL PFFNEKCFII FGVTVGGFLN FDDSLLAKDV 

       430        440        450        460 
KPYKNREPRA ALSFWQHRDA WAPTWGRHSA MVIDYVRVYA E

« Hide

Isoform A [UniParc].

Checksum: D0ED6EA819F4E2C8
Show »

FASTA43249,404
Isoform C [UniParc].

Checksum: B5F544D12C9C5567
Show »

FASTA24127,313
Isoform D [UniParc].

Checksum: B97E75D2348B65E3
Show »

FASTA41046,852

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] (ISOFORM B), DEVELOPMENTAL STAGE.
[2]"Contrasting evolutionary patterns in Drosophila immune receptors."
Jiggins F.M., Kim K.W.
J. Mol. Evol. 63:769-780(2006) [PubMed: 17103056] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
Strain: Netherlands line N01, Netherlands line N02, Netherlands line N03, Netherlands line N06, Netherlands line N07, Netherlands line N14, Netherlands line N15, Netherlands line N16, Netherlands line N17, Netherlands line N22, Netherlands line N29 and Netherlands line N30.
[3]"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.
[4]"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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF228473 mRNA. Translation: AAF33850.1.
AM050207 Genomic DNA. Translation: CAJ19007.1.
AM050207 Genomic DNA. Translation: CAJ19008.1.
AM050207 Genomic DNA. Translation: CAJ19009.1.
AM050207 Genomic DNA. Translation: CAJ19010.1.
AM050208 Genomic DNA. Translation: CAJ19011.1.
AM050208 Genomic DNA. Translation: CAJ19012.1.
AM050208 Genomic DNA. Translation: CAJ19013.1.
AM050208 Genomic DNA. Translation: CAJ19014.1.
AM050209 Genomic DNA. Translation: CAJ19015.1.
AM050209 Genomic DNA. Translation: CAJ19016.1.
AM050209 Genomic DNA. Translation: CAJ19017.1.
AM050209 Genomic DNA. Translation: CAJ19018.1.
AM050210 Genomic DNA. Translation: CAJ19019.1.
AM050210 Genomic DNA. Translation: CAJ19020.1.
AM050210 Genomic DNA. Translation: CAJ19021.1.
AM050210 Genomic DNA. Translation: CAJ19022.1.
AM050211 Genomic DNA. Translation: CAJ19023.1.
AM050211 Genomic DNA. Translation: CAJ19024.1.
AM050211 Genomic DNA. Translation: CAJ19025.1.
AM050211 Genomic DNA. Translation: CAJ19026.1.
AM050212 Genomic DNA. Translation: CAJ19027.1.
AM050212 Genomic DNA. Translation: CAJ19028.1.
AM050212 Genomic DNA. Translation: CAJ19029.1.
AM050212 Genomic DNA. Translation: CAJ19030.1.
AM050213 Genomic DNA. Translation: CAJ19031.1.
AM050213 Genomic DNA. Translation: CAJ19032.1.
AM050213 Genomic DNA. Translation: CAJ19033.1.
AM050213 Genomic DNA. Translation: CAJ19034.1.
AM050214 Genomic DNA. Translation: CAJ19035.1.
AM050214 Genomic DNA. Translation: CAJ19036.1.
AM050214 Genomic DNA. Translation: CAJ19037.1.
AM050214 Genomic DNA. Translation: CAJ19038.1.
AM050215 Genomic DNA. Translation: CAJ19039.1.
AM050215 Genomic DNA. Translation: CAJ19040.1.
AM050215 Genomic DNA. Translation: CAJ19041.1.
AM050215 Genomic DNA. Translation: CAJ19042.1.
AM050216 Genomic DNA. Translation: CAJ19043.1.
AM050216 Genomic DNA. Translation: CAJ19044.1.
AM050216 Genomic DNA. Translation: CAJ19045.1.
AM050216 Genomic DNA. Translation: CAJ19046.1.
AM050217 Genomic DNA. Translation: CAJ19047.1.
AM050217 Genomic DNA. Translation: CAJ19048.1.
AM050217 Genomic DNA. Translation: CAJ19049.1.
AM050217 Genomic DNA. Translation: CAJ19050.1.
AM050218 Genomic DNA. Translation: CAJ19051.1.
AM050218 Genomic DNA. Translation: CAJ19052.1.
AM050218 Genomic DNA. Translation: CAJ19053.1.
AM050218 Genomic DNA. Translation: CAJ19054.1.
AE014296 Genomic DNA. Translation: AAF49245.3.
AE014296 Genomic DNA. Translation: AAF49246.3.
AE014296 Genomic DNA. Translation: AAN11665.1.
AE014296 Genomic DNA. Translation: AAN11666.1.
AY058277 mRNA. Translation: AAL13506.1.
RefSeqNP_524141.1. NM_079417.2.
NP_730350.1. NM_168771.1.
NP_730351.1. NM_168772.1.
NP_730352.1. NM_168773.1.
UniGeneDm.1608.

3D structure databases

ProteinModelPortalQ9VVR4.
SMRQ9VVR4. Positions 21-114.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9VVR4.

Protein family/group databases

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

Proteomic databases

PRIDEQ9VVR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075094; FBpp0074861; FBgn0040322.
GeneID40033.
KEGGdme:Dmel_CG4144.

Organism-specific databases

CTD40033.
FlyBaseFBgn0040322. GNBP2.

Phylogenomic databases

eggNOGinNOG09068.
GeneTreeEMGT00050000015300.
InParanoidQ9VVR4.
OMAFNEKCFI.
OrthoDBEOG4FN2ZZ.
PhylomeDBQ9VVR4.

Gene expression databases

BgeeQ9VVR4.
GermOnlineCG4144. Drosophila melanogaster.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 2 hits.
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Other

NextBio816648.

Entry information

Entry nameBGBP2_DROME
AccessionPrimary (citable) accession number: Q9VVR4
Secondary accession number(s): A0ZWZ5 expand/collapse secondary AC list , A0ZWZ8, A0ZX11, A0ZX12, A0ZX13, A0ZX39, A0ZX40, A0ZX41, A0ZX42, Q8IQT6, Q8IQT7, Q95U68, Q9NHA9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents