Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth B]PF09259e7wdlB1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Fungal immunomodulatory protein, FIP (From Topology)T: Fungal immunomodulatory protein, FIPF: PF09259ECOD (1.6)
B [auth A]PF09259e7wdlA1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Fungal immunomodulatory protein, FIP (From Topology)T: Fungal immunomodulatory protein, FIPF: PF09259ECOD (1.6)
CPF09259e7wdlC1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Fungal immunomodulatory protein, FIP (From Topology)T: Fungal immunomodulatory protein, FIPF: PF09259ECOD (1.6)
DPF09259e7wdlD1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Fungal immunomodulatory protein, FIP (From Topology)T: Fungal immunomodulatory protein, FIPF: PF09259ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth B],
B [auth A],
C,
D
PF09259Fungal immunomodulatory protein Fve (Fve)Fungal immunomodulatory protein FveFve is a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity. It stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and oedema, enhances transcription of IL-2, IFN-gamma and ...Fve is a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity. It stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and oedema, enhances transcription of IL-2, IFN-gamma and TNF-alpha, and haemagglutinates red blood cells. It appears to be a lectin with specificity for complex cell-surface carbohydrates. Fve adopts a tertiary structure consisting of an immunoglobulin-like beta-sandwich, with seven strands arranged in two beta sheets, in a Greek-key topology. It forms a non-covalently linked homodimer containing no Cys, His or Met residues; dimerisation occurs by 3-D domain swapping of the N-terminal helices and is stabilised predominantly by hydrophobic interactions [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage