Prefoldin subunit 1 (PFDN1)
The protein contains 122 amino acids for an estimated molecular weight of 14210 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. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
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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The reference OMIM entry for this protein is 604897
Prefoldin 1; pfdn1
DESCRIPTION
PFDN1 is a subunit of the heteromeric prefoldin complex that chaperones nascent actin (see 102560) and alpha- and beta-tubulin (see 602529 and 191130, respectively) chains pending their transfer to the cytosolic chaperonin containing TCP1 (186980) (CCT) complex (Hansen et al., 1999).CLONING
Molecular chaperones are proteins that assist in the correct folding of other proteins in the crowded molecular environment that exists in living cells. Vainberg et al. (1998) described the biochemical purification of a heterohexameric chaperone that they termed prefoldin. By analysis of prefoldin by reverse-phase HPLC, they identified 6 prefoldin polypeptides, and they identified the corresponding mammalian cDNA sequences, of which 4 were human, by sequence analysis. These 4 included PFDN1, which encodes a 122-amino acid protein. PFDN3 is identical to VBP1 (300133), whereas PFDN4 (604898) and PFDN5 (604899) encode a possible transcription factor and a MYC (190080)-binding protein, respectively.GENE FUNCTION
Hansen et al. (1999) showed that prefoldin is involved in chaperoning nascent chains of the cytoskeletal proteins actin, alpha-tubulin, and beta-tubulin in HeLa cells and rabbit reticulocyte lysates. Prefoldin bound to actin chains after synthesis of the N-terminal 130 to 140 amino acids and to beta-tubulin after synthesis of about 250 amino acids. Prefoldin remained bound to the relatively unfolded actin and tubulin polypeptides until delivery of the full-length proteins to CCT for folding to their native states.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PFDN1 gene to chromosome 5 (TMAP WI-20399). ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 604897 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).