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Q9NL89 (BGBP_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-1,3-glucan-binding protein

Short name=BGBP
Alternative name(s):
Beta-1,3-glucan recognition protein
Short name=BetaGRP
OrganismBombyx mori (Silk moth)
Taxonomic identifier7091 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.1 Ref.2

Subunit structure

Monomer. Ref.2

Subcellular location

Secreted By similarity UniProtKB Q76DI2.

Tissue specificity

Hemocytes, fat body and epidermal cells. Ref.1

Induction

By bacterial and yeast infection. Ref.1

Post-translational modification

Glycosylated Probable. Ref.1

Sequence similarities

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

Mass spectrometry

Molecular mass is 54594 Da from positions 17 - 495. Determined by MALDI. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.1
Chain17 – 495479Beta-1,3-glucan-binding protein Ref.1
PRO_0000002816

Amino acid modifications

Glycosylation3781N-linked (GlcNAc...) Probable

Secondary structure

......... 495
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NL89 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 09249039F7456BF2

FASTA49555,802
        10         20         30         40         50         60 
MYKTCVWVLL FKIVLCYEAP PATLEAIHPK GLRVSVPDEG FSLFAFHGKL NEEMEGLEAG 

        70         80         90        100        110        120 
HWSRDITKPK NGRWIFRDRN AALKIGDKIY FWTFVIKDGL GYRQDNGEWT VEGFVDEAGN 

       130        140        150        160        170        180 
PVNTEGSEIT PGVEFTSTSL NPESPQSIPN QPPDNLPAKP PSEGYPCELS LSTVSVPGFV 

       190        200        210        220        230        240 
CKGQLLFEDQ FNIPIHRGKI WVPEVKFPGE PDFPFNVYLS DNAEVNDGKL IIKPATLESK 

       250        260        270        280        290        300 
YGEDFVRQSL DLSERCTGTV GTAQCLREAS GPLILPPIIT AKISTRHQFA FKYGRVEIRA 

       310        320        330        340        350        360 
KMPKGDWLYP EILLEPRDNI YGVRNYASGI LKIASVKGNA EFSKKLYAGP IMTGSDPYRS 

       370        380        390        400        410        420 
FYLKENIGYE SWNNDFHNYT LEWRPDGITL LVDGESYGEI KPGEGFYNVA NSYKVEAAPQ 

       430        440        450        460        470        480 
WLKGTIMAPF DELFYVSIGL NVAGIREFSE DISNKPWKNS ATKAMLKFWD ARSQWFPTWD 

       490 
EDSALQVDYV KVFAI 

« Hide

References

[1]"A pattern-recognition protein for beta-1,3-glucan. The binding domain and the cDNA cloning of beta-1,3-glucan recognition protein from the silkworm, Bombyx mori."
Ochiai M., Ashida M.
J. Biol. Chem. 275:4995-5002(2000) [PubMed: 10671539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-84; 98-159; 183-199; 241-274; 305-332; 346-389; 415-423 AND 464-495, FUNCTION, TISSUE SPECIFICITY, INDUCTION, MASS SPECTROMETRY.
Strain: Kinshu X Showa.
Tissue: Hemocyte and Larval hemolymph.
[2]"Purification of a beta-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori."
Ochiai M., Ashida M.
J. Biol. Chem. 263:12056-12062(1988) [PubMed: 3136171] [Abstract]
Cited for: FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026441 mRNA. Translation: BAA92243.1.
RefSeqNP_001036840.1. NM_001043375.1.
UniGeneBmo.370.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQENMR-A17-118[»]
3AQXX-ray2.05A/B17-118[»]
ProteinModelPortalQ9NL89.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID692379.

Organism-specific databases

CTD692379.

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. 1 hit.
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGBP_BOMMO
AccessionPrimary (citable) accession number: Q9NL89
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2000
Last modified: September 21, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families