Q8MU95 (BGBP_PLOIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 36.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-1,3-glucan-binding protein Short name=BGBP Alternative name(s): Beta-1,3-glucan recognition protein Short name=BetaGRP |
| Organism | Plodia interpunctella (Indianmeal moth) |
| Taxonomic identifier | 58824 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Pyraloidea › Pyralidae › Phycitinae › Plodia |
Protein attributes
| Sequence length | 488 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in the recognition of invading micro-organisms. Binds specifically to beta-1,3-glucan, causing aggregation of invading micro-organisms and activation of the phenoloxidase cascade. Ref.1 |
| Subunit structure | Monomer. Ref.1 |
| Subcellular location | |
| Tissue specificity | Fat body and hemolymph. Ref.1 |
| Developmental stage | Expression is maintained at a moderate level throughout development from embryo to adult. Ref.1 |
| Post-translational modification | The N-terminus is blocked. Ref.1 |
| Sequence similarities | Belongs to the insect beta-1,3-glucan binding protein family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Immunity Innate immunity |
| Cellular component | Secreted |
| Domain | Signal |
| PTM | Glycoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro innate immune responseInferred from electronic annotation. Source: UniProtKB-KW regulation of innate immune responseInferred from direct assay Ref.1. Source: UniProtKB |
| Cellular component | extracellular region Inferred from direct assay Ref.1. Source: UniProtKB |
| Molecular function | bacterial cell surface binding Inferred from direct assay Ref.1. Source: UniProtKB hydrolase activity, hydrolyzing O-glycosyl compoundsInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||
Molecule processing | |||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Potential | ||||||||||||||||||||
| Chain | 18 – 488 | 471 | Beta-1,3-glucan-binding protein | PRO_0000002823 | |||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||
| Glycosylation | 373 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||
| Glycosylation | 453 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||
| Beta strand | 30 – 32 | 3 | |||||||||||||||||||||
| Beta strand | 40 – 43 | 4 | |||||||||||||||||||||
| Beta strand | 50 – 54 | 5 | |||||||||||||||||||||
| Beta strand | 56 – 58 | 3 | |||||||||||||||||||||
| Beta strand | 71 – 73 | 3 | |||||||||||||||||||||
| Beta strand | 81 – 84 | 4 | |||||||||||||||||||||
| Beta strand | 95 – 103 | 9 | |||||||||||||||||||||
Sequences
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References
| [1] | "cDNA cloning, purification, properties and function of a beta-1,3-glucan recognition protein from a pyralid moth, Plodia interpunctella." Fabrick J.A., Baker J.E., Kanost M.R. Insect Biochem. Mol. Biol. 33:579-594(2003) [PubMed: 12770576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-30, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: HD198. Tissue: Larva and Larval plasma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF532603 mRNA. Translation: AAM95970.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| ProteinModelPortal | Q8MU95. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||
| CAZy | CBM39. Carbohydrate-Binding Module Family 39. GH16. Glycoside Hydrolase Family 16. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. IPR000757. Glyco_hydro_16. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00722. Glyco_hydro_16. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| SUPFAM | SSF49899. ConA_like_lec_gl. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | BGBP_PLOIN | ||||||||
| Accession | Primary (citable) accession number: Q8MU95 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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