P81182 · BGBP_PENVA

Function

function

Involved in the recognition of invading microorganisms. Binds specifically to beta-1,3-glucan and activates the prophenoloxidase cascade.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functionpattern recognition receptor activity
Biological Processcell surface pattern recognition receptor signaling pathway
Biological Processinnate immune response
Biological Processlipid transport
Biological Processregulation of innate immune response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Beta-1,3-glucan-binding protein
  • Short names
    BGBP
  • Alternative names
    • Beta-1,3-glucan recognition protein (BetaGRP)
    • BetaGBP-HDL
    • High density lipoprotein

Organism names

Accessions

  • Primary accession
    P81182
  • Secondary accessions
    • Q86G48

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for propeptide, glycosylation, chain.

Type
IDPosition(s)Description
PropeptidePRO_00000028251-197
Glycosylation33N-linked (GlcNAc...) asparagine
Glycosylation55N-linked (GlcNAc...) asparagine
Glycosylation185N-linked (GlcNAc...) asparagine
ChainPRO_0000002826198-1454Beta-1,3-glucan-binding protein
Glycosylation571N-linked (GlcNAc...) asparagine
Glycosylation592N-linked (GlcNAc...) asparagine
Glycosylation825N-linked (GlcNAc...) asparagine
Glycosylation882N-linked (GlcNAc...) asparagine
Glycosylation1153N-linked (GlcNAc...) asparagine

Keywords

Expression

Tissue specificity

Expressed in the hepatopancreas and secreted into the hemolymph. Expressed at lower levels in muscle, pleopod and gill tissue.

Interaction

Subunit

Monomer.

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 16 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,454
  • Mass (Da)
    164,013
  • Last updated
    2004-09-27 v2
  • Checksum
    03076021A5D6465F
MSFDLTTPFDVIKTVSLSARYSWTTSQKGATLNITYNDKNFVLSSSLQLSTRASNITFQATTPFEGFQNSFIEIKYDIDNREELLASRVSVDDHSYSFVVGGYIEDKLAVFKWNLNSPLTGWTDAKFVAKIDLSSENKNLEISLEKEGDLKAIAVSGKFIGSTLDFNLRTPFRGLNNFNVFGSLNRSKRSLEMRMMNDAGQASLAGNFNSLRFNMKTPFERAEQISWEVTKTGEGSYKAEWRRNDNYATFTIEKDVSKQSFDLNIKSEFRGWEILALTGRLDQETKQAYLSGAINEQKITVTGSGSITNKIKFSMTIETPYENYRQVKAQLNYAKRKNAIKLEASSSSSDFHLLWSRSGSGLEAHLIVPNSRQNTEISINLTPTQGKITITSRFEPIRDYLQEYHVNLGQNEITADHIIKLNGHEVFKMDFERNAPEQKVHLEIHTHVAERHTTIHFHREGFSKLNFLFKREVPQYGEKHFKVDITGSGALPQKGALDIVVENTFREPAKTINARVEVDRTGARKKIMLEVSPRQSRVYIFNLEYIADLESPQHGDFTLKITTPNNSPWQNISGNWNVEDPNDATITFTVGNVTYNAKGKLTLRESTMILSSTDPSAENIYLQWKFERNGDTKDYFLKLGRKSRYGMLKLTGTITDIAHVDIEGGFKAGPFMPNEFLFTSMWGKSNGVVTGEGTFDYGNYHGSHRLVKFERNAERKSASFEWSATSNIPQYNSVSVSGNYDFNHKVVIFVVINADGRESKIDINIADINPTSSRNTAMISIPLLGPTFKRTELTVSHDFSHPNRKSISAVAKFGRSESFINAKWNRSDGFDTLEGNIEAKSRFLGDFLINVRYDMSNIADAHAEVDYLRTTTDGDKKEFKLNWTRKSTDDHLENEMVFDSNFETLSHARAYANADYGGIFKLLSGLDWDDKKISLTLEVRKNKISGILTTPFEGFETLEIDLQYKLTGKDKSVKATYQRGDRKASFNMEMSTKGKKGGSFKVDLTTPFEVVKNLHIDGQYENKVAQINYQRNDIQMNFNGKANIKSSKASFDISFTPPSGQNIRIAASYDVQDFIDGTGDEEKELASLSLEFEGNSMDFSLHGFRNDDRLYVMIHGTSSFAVLKMFHLKLDSELNTEARDGTFELTFNDFKFNVSNHFERRANNGYYFRSKIESTLTPLPALIIGLGREGQERIITIGYGEDKEITFSVKGKNNFLSGFSGKVDIPSIGYEGVEYDVDYSFPGDNHLQIKVEIDLNENGQEVEATFFLDSEGIKARLSSAVLGDHSLRVRRSVAPDGFYAEAGLDDYNLKLRGGFKNEDTARGVQLEGEVFGKRFLIDTLFQSEGKRYSEGKLIIHTPFHGMEKMGGLFTWSNQNKKIMAHAELHLPSYTTPTITGEISLDLKKKINGYVTLDVAGEEFTLKCNLAGSSISQGYTGSLEFYTTIPCCITCCGDR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict220-221in Ref. 2; AA sequence
Sequence conflict831in Ref. 1; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY249858
EMBL· GenBank· DDBJ
AAO92933.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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