Prefoldin subunit 5 (PFDN5)
The protein contains 154 amino acids for an estimated molecular weight of 17328 Da.
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
'de novo' posttranslational protein folding
Cellular protein metabolic process
Negative regulation of amyloid fibril formation
Negative regulation of canonical Wnt signaling pathway
Negative regulation of transcription, DNA-templated
Protein folding
Regulation of transcription, DNA-templated
Retina development in camera-type eye
The reference OMIM entry for this protein is 604899
Prefoldin 5; pfdn5
Mm1
DESCRIPTION
Prefoldin-5 is a subunit of the heterohexameric chaperone protein prefoldin, which binds specifically to cytosolic chaperonin and transfers target proteins to it (Vainberg et al., 1998). See also 604897.CLONING
Using a yeast 2-hybrid screen of a HeLa cell cDNA library with c-myc as bait, Mori et al. (1998) isolated a cDNA that they designated MM1 (for myc modulator-1). The MM1 cDNA encodes a deduced 167-amino acid protein with a putative leucine zipper motif in the N terminus. Northern blot analysis revealed expression of 4 distinct bands (0.7, 1.15, 2.9 and 4.4 kb); there was strong ubiquitous expression of the 0.7-kb transcript as well as strong expression of the 1.15-kb transcript in pancreas, weak expression in kidney, skeletal muscle, and placenta, and faint expression in liver and lung. Fluorescent microscopy showed MM1 expression primarily in the nucleus, with lower intensity in nucleoli and cytoplasm. Binding analyses indicated that MM1 and c-myc bind directly and that all but the N-terminal 13 amino acids of MM1 are required for binding. MM1 interacts with the myc box-2, a transcription-activating domain of c-myc.GENE FUNCTION
Vainberg et al. (1998) described the biochemical purification of a heterohexameric chaperone protein, which they called prefoldin. One of its subunits, prefoldin-5, is identical to MM1. Vainberg et al. (1998) found that deletion of PFDN5 from yeast resulted in impaired functions of the actin and tubulin-based cytoskeleton.BIOCHEMICAL FEATURES
- Crystal Structure Prefoldin is a hexameric molecular chaperone complex built from 2 related classes of subunits, alpha and beta, and present in all eukaryotes and archaea. Whereas eukaryotes have 2 related PFD-alpha subunits and 4 related PFD-beta subunits, archaea have only 1 member of each class, a PFD-alpha subunit whose closest human homolog is PFD5, and a PFD-beta subunit whose closest human homolog is PFD6. Prefoldin interacts with nascent polypeptide chains and, in vitro, can functionally substitute for the Hsp70 chaperone system in stabilizing nonnative proteins for subsequent folding in the central cavity of a chaperonin. Siegert et al. (2000) presented the crystal structure and characterization of the prefoldin hexamer from the archaeum Methanobacterium thermoautotrophicum. Prefoldin has the appearance of a jellyfish: its body consists of a double beta-barrel assembly with 6 long tentacle-like coiled coils protruding from it. The distal regions of the coiled coils expose hydrophobic patches and are required for multivalent binding of nonnative proteins.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PFDN5 gene to chromosome 12 (TMAP SHGC-31943). ... More on the omim web site
Dec. 10, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604899 was added.