Detail Information for IndEnz0014000001
IED ID IndEnz0014000001
Enzyme Type ID pancreatin000001
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