{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P57741","uniProtkbId":"PFD3_ARATH","entryAudit":{"firstPublicDate":"2001-01-11","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-01-11","entryVersion":135,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Arabidopsis thaliana","commonName":"Mouse-ear cress","taxonId":3702,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19825635"}],"value":"Prefoldin subunit 3"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19825635"}],"value":"Gene involved in microtubule biogenesis 2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19825635"}],"value":"PFD3"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19825635"}],"value":"GIM2"}],"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"Araport","id":"AT5G49510"}],"value":"At5g49510"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"BAB10764.1"}],"value":"K6M13.5"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P57742"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q2HIK4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19825635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28412546"}],"value":"Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it (PubMed:19825635). 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 (By similarity). 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)"}],"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"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32396196"}],"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). Binds to the DELLA protein GAI (PubMed:23583555). Interacts with LSM8, a specific subunit of the LSM2-8 complex, which is a core component of the spliceosome (PubMed:32396196)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P57742"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28412546"}],"value":"In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (PubMed:28412546). But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (PubMed:28412546). This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28412546"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28412546"}],"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"}],"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)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the prefoldin subunit alpha family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"22223895"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"Prefoldin subunit 3","featureId":"PRO_0000153657"},{"type":"Coiled coil","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"22223895"}]}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"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":"10718197","citationType":"journal article","authors":["Sato S.","Nakamura Y.","Kaneko T.","Katoh T.","Asamizu E.","Kotani H.","Tabata S."],"citationCrossReferences":[{"database":"PubMed","id":"10718197"},{"database":"DOI","id":"10.1093/dnares/7.1.31"}],"title":"Structural analysis of Arabidopsis thaliana chromosome 5. 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