Reviewed,
UniProtKB/Swiss-Prot P81943 (ALL5_APIGR)
Last modified
November 25, 2008.
Version 32.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Allergen Api g 5 Alternative name(s): Allergen=Api g 5 |
| Organism | Apium graveolens (Celery) |
| Taxonomic identifier | 4045 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apioideae › apioid superclade › Apium clade › Apium |
Protein attributes
| Sequence length | 86 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Cofactor | FAD By similarity. UniProtKB P93479 |
| Post-translational modification | Carries MUXF and MMXF, two complex N-linked glycans with alpha-1,3-fucose and beta-1,2-xylose residues in their structures. MMXF is added to Asn-62. Ref.2 |
| Allergenic properties | Causes an allergic reaction in human. Binds to IgE. The glycan moiety seems to constitute the relevant allergenic epitope. Ref.1 Ref.2 |
| Sequence similarities | Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
| Caution | The order of the peptides shown is unknown. Ref.2 |
Ontologies
| Keywords | |
|---|---|
| Disease | Allergen |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW type I hypersensitivity Ref.1Non-traceable author statement. Source: UniProtKB |
| Molecular function | oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›86 | ›86 | Allergen Api g 5 | PRO_0000128175 | |||||
Amino acid modifications | |||||||||
| Glycosylation | 62 | 1 | N-linked (GlcNAc...) Ref.2 | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 22 – 23 | 2 | |||||||
| Non-adjacent residues | 52 – 53 | 2 | |||||||
| Non-adjacent residues | 76 – 77 | 2 | |||||||
| Non-terminal residue | 86 | 1 | |||||||
Sequences
References
| [1] | "N-terminal sequences of high molecular weight allergens from celery tuber." Ganglberger E., Radauer C., Grimm R., Hoffmann-Sommergruber K., Breiteneder H., Scheiner O., Jensen-Jarolim E. Clin. Exp. Allergy 30:566-570(2000) [PubMed: 10718855] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18, ALLERGENICITY. Tissue: Tuber. |
| [2] | "Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients." Bublin M., Radauer C., Wilson I.B.H., Kraft D., Scheiner O., Breiteneder H., Hoffmann-Sommergruber K. FASEB J. 17:1697-1699(2003) [PubMed: 12958180] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-86, SEQUENCE REVISION, GLYCOSYLATION, ALLERGENICITY. Tissue: Tuber. |
Cross-references
Entry information
| Entry name | ALL5_APIGR | ||||||||
| Accession | Primary (citable) accession number: P81943 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Allergens Nomenclature of allergens and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


