Search by BoMiProt ID - Bomi8200


Primary Information

BoMiProt ID Bomi8200
Protein Name Prefoldin subunit 2
Organism Bos taurus
Uniprot IdA1A4P5
Milk FractionExosomes
Ref Sequence Id NP_001073690.1
Aminoacid Length 154
Molecular Weight 16648
Fasta Sequence https://www.uniprot.org/uniprot/A1A4P5.fasta
Gene Name PFDN2
Gene Id 404138
Protein Existence Status reviewed

Secondary Information

Protein Function It is a subunit of Prefoldin complex which is a chaperone protein that regulates the correct folding of proteins.The prefoldin complex specifically binds to the cytoplasmic chaperone protein of TCP-1 (CCT), a loop complex, forming actin molecules and acting as a transport molecule that directs protein accurately, thereby promoting actin and tubulin to be protected from aggregation and folded correctly.
Biochemical Properties Eukaryotic prefoldin complex is a heterohexameric complex like a jellyfish-like structure, consisting of six different subunits (PFDN1–6): two α subunits (PFDN3 and PFDN5) and four β subunits (PFDN1, PFDN2, PFDN4, and PFDN6.Contains a clamp-like structure that holds the substrate proteins. The clamp-like structure has a multivalent binding surface and can protect the protein conformers of unnatural proteins until they reach natural state or transfer to another component of the folding machine.
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
NA
Predicted Disorder Regions 1-39, 43-49, 113-154
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments Prefoldin complex was discovered 20 years ago in the domains of eukaryotes and archaea as the property of promoting the assembly of cytoskeletal proteins (actin and tubulin) into corresponding polymers, also known as Gim complex (Genes involved in microtubule biogenesis. The prefoldin complex helps protein fold correctly and prevents aggregation by providing class II chaperones (Hsp60 molecular chaperones found in archaebacteria and eukaryotic cytoplasm) with a linear, unnatural substrate in the cytoplasm.Studies have shown that the prefoldin complex is involved in the pathogenesis of neurodegenerative diseases, especially Alzheimer’s disease (AD) and Parkinson’s disease (PD).
Bibliography 1.Liang, J., Xia, L., Oyang, L. et al. The functions and mechanisms of prefoldin complex and prefoldin-subunits. Cell Biosci 10, 87 (2020). https://doi.org/10.1186/s13578-020-00446-8