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Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (PubMed:19825635). Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8 (By similarity). Required for the biogenesis of tubulins and for subsequent microtubules (MTs) organization and dynamicity (PubMed:19825635). Necessary for tolerance to NaCl salt stress (PubMed:19825635). Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (PubMed:23583555). Prevents cold acclimation (e.g. 7 days at 4 degrees Celsius) in a DELLA proteins-dependent manner by promoting nuclear proteasome-mediated HY5 degradation, thus modulating the expression of several genes and reducing anthocyanin biosynthesis, but seems not involved in constitutive freezing tolerance (PubMed:28412546). Contributes to the GA-dependent regulation of PIN2 trafficking at the plasma membrane, thus influencing auxin flux (PubMed:29463731)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19004800"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23583555"}],"value":"Heterohexamer of two PFD-alpha type and four PFD-beta type subunits forming prefoldin co-chaperone complex (By similarity). Interacts with PFD6 (PubMed:19004800). 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Interacts with LSM8, a specific subunit of the LSM2-8 complex, which is core components of the spliceosome (PubMed:32396196)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23583555"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23583555"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28412546"}],"value":"Accumulates in response to cold"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19825635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28412546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29463731"}],"value":"Reduced levels of alpha- and beta-tubulin (PubMed:19825635). Altered development patterns and disturbed microtubules (MTs) organization (PubMed:19825635). Hypersensitivity to high NaCl salt levels (PubMed:19825635). Increased capacity to tolerate freezing temperatures upon acclimation (e.g. 7 days at 4 degrees Celsius) associated with a continuous accumulation of HY5 in cold conditions (PubMed:28412546). The pfd5 pfd6 double mutant is less sensitive to gibberellic acid (GA)-mediated mobilization of PIN2 at the plasma membrane (PubMed:29463731)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the prefoldin subunit alpha family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"Prefoldin subunit 5","featureId":"PRO_0000153666"},{"type":"Coiled coil","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]}],"keywords":[{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"9501997","citationType":"journal article","authors":["Nakamura Y.","Sato S.","Kaneko T.","Kotani H.","Asamizu E.","Miyajima N.","Tabata S."],"citationCrossReferences":[{"database":"PubMed","id":"9501997"},{"database":"DOI","id":"10.1093/dnares/4.6.401"}],"title":"Structural analysis of Arabidopsis thaliana chromosome 5. 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