| IED ID | IndEnz0004000037 |
| Enzyme Type ID | xylanase000037 |
| Protein Name |
Gamma conglutin 1 Conglutin gamma allergen Lup an gamma-conglutin Cleaved into: Gamma conglutin 1 beta subunit Gamma conglutin 1 small subunit ; Gamma conglutin 1 alpha subunit Gamma conglutin 1 large subunit |
| Gene Name | LOC109345795 TanjilG_29300 |
| Organism | Lupinus angustifolius (Narrow-leaved blue lupine) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade genistoids sensu lato core genistoids Genisteae Lupinus Lupinus angustifolius (Narrow-leaved blue lupine) |
| Enzyme Sequence | MARNMAHILHILVISLSYSFLFVSSSSQDSQSLYHNSQPTSSKPNLLVLPVQEDASTGLHWANIHKRTPLMQVPLLLDLNGKHLWVTCSQHYSSSTYQAPFCHSTQCSRANTHQCFTCTDSTTTRPGCHNNTCGLLSSNPVTQESGLGELAQDVLAIHSTHGSKLGPMVKVPQFLFSCAPSFLAQKGLPNNVQGALGLGQAPISLQNQLFSHFGLKRQFSVCLSRYSTSNGAILFGDINDPNNNNYIHNSLDVLHDLVYTPLTISKQGEYFIQVNAIRVNKHLVIPTKNPFISPSSTSYHGSGEIGGALITTTHPYTVLSHSIFEVFTQVFANNMPKQAQVKAVGPFGLCYDSRKISGGAPSVDLILDKNDAVWRISSENFMVQAQDGVSCLGFVDGGVHARAGIALGAHHLEENLVVFDLERSRVGFNSNSLKSYGKTCSNLFDLNNP |
| Enzyme Length | 449 |
| Uniprot Accession Number | Q42369 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Sulfur-rich seed storage protein that remains undegraded at germination. {ECO:0000250|UniProtKB:Q9FSH9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (29); Chain (3); Disulfide bond (7); Domain (1); Erroneous initiation (1); Glycosylation (1); Helix (13); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Allergen;Direct protein sequencing;Disulfide bond;Glycoprotein;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By sulfur deficiency. {ECO:0000269|Ref.2}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q9FEX1}. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes very complex post-translational maturation; the proteolytic processing leading to the formation of two alpha and beta subunits is incomplete, leaving a certain amount of the protein in an uncut form. {ECO:0000269|PubMed:25664733, ECO:0000269|PubMed:29635768}.; PTM: Glycosylated on alpha chain. {ECO:0000269|PubMed:22264085, ECO:0000269|PubMed:29635768}. |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000269|PubMed:29635768 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4PPH; |
| Mapped Pubmed ID | 21457461; 21733318; 23872149; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,916 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |