Prefoldin subunit 6 (PFDN6)

The protein contains 129 amino acids for an estimated molecular weight of 14583 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:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  2. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 0%
Model score: 47

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The reference OMIM entry for this protein is 605660

Prefoldin 6; pfdn6
Ke2, mouse, homolog of; hke2

DESCRIPTION

PFDN6 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

A number of diseases are influenced by genes at the centromeric end of the major histocompatibility complex (see 142800) on chromosome 6p21.3. Herberg et al. (1998) cloned and characterized genes, including HKE2, in the 70-kb, gene-dense segment flanking the tapasin (TAPBP; 601962) gene. The 129-amino acid HKE2 protein is identical to the mouse Ke2 sequence apart from the insertion of 2 residues at position 122. Vainberg et al. (1998) purified the prefoldin heterohexameric chaperone from bovine testis and, by database analysis, they identified Pfdn6 in several species, including mouse. The deduced mouse protein contains 127 amino acids.

GENE FUNCTION

Using a mouse antibody directed against PFDN6 to follow the prefoldin complex, 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.

GENE STRUCTURE

Herberg et al. (1998) determined that the PFDN6 gene contains 4 exons.

MAPPING

By genomic sequence analysis, Herberg et al. (1998) mapped the PFDN6 gene to chromosome 6p21.3. ... More on the omim web site

Subscribe to this protein entry history

Dec. 10, 2018: Protein entry updated
Automatic update: model status changed

Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 605660 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).