Prefoldin subunit 3

{{Short description|Chaperone protein}}

{{infobox protein

|Name=Prefoldin subunit 3

|caption=

|image=

|width=

|HGNCid=12662

|Symbol=VBP1

|AltSymbols=

|EntrezGene=7411

|OMIM=300133

|RefSeq=NM_003372

|UniProt=P61758

|PDB=

|ECnumber=

|Chromosome=X

|Arm=q

|Band=28

|LocusSupplementaryData=

}}

Prefoldin subunit 3 (VBP-1),{{cite web |title=UniProt |url=https://beta.uniprot.org/uniprotkb/P61758/entry |website=beta.uniprot.org |access-date=27 March 2022}} also Von Hippel–Lindau binding protein 1, is a prefoldin chaperone protein that binds to von Hippel–Lindau protein and transports it from perinuclear granules to the nucleus or cytoplasm inside the cell.{{cite journal | vauthors = Tsuchiya H, Iseda T, Hino O | title = Identification of a novel protein (VBP-1) binding to the von Hippel–Lindau (VHL) tumor suppressor gene product | journal = Cancer Research | volume = 56 | year = 1996 | pages = 2881–5 | pmid = 8674032 | issue = 13}} It is also involved in transporting nascent polypeptides to cytosolic chaperonins for post-translational folding.{{cite web | title = GenAtlas report: VBP1 | url = http://www.dsi.univ-paris5.fr/genatlas/fiche.php?symbol=VBP1 | date = 2003-01-17 | accessdate = 2007-07-17}}

VBP-1 is a 197–amino acid heterohexamer comprising two prefoldin-α and four prefoldin-β subunits, and is a member of the prefoldin-α subunit family.{{cite web | title = NiceProt report: P61758 (Prefoldin 3, human) | url = http://www.expasy.org/cgi-bin/niceprot.pl?P61758 | date = 2007-07-10 | accessdate = 2007-07-17}} It is ubiquitously expressed in tissues, and is located in the cell nucleus and cytoplasm. The VBP1 gene is located at Xq28.{{cite journal | vauthors = Brinke A, Green PM, Giannelli F | title = Characterization of the gene (VBP1) and transcript for the von Hippel–Lindau binding protein and isolation of the highly conserved murine homologue | journal = Genomics | volume = 45 | pages = 105–12 | year = 1997 | pmid = 9339366 | doi = 10.1006/geno.1997.4902 | issue = 1}} Homologues are known to exist between human VBP-1 and proteins in mice, Drosophila and C. elegans.