PFD3_ARATH
ID PFD3_ARATH Reviewed; 195 AA.
AC P57741;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Prefoldin subunit 3 {ECO:0000303|PubMed:19825635};
DE AltName: Full=Gene involved in microtubule biogenesis 2 {ECO:0000303|PubMed:19825635};
GN Name=PFD3 {ECO:0000303|PubMed:19825635};
GN Synonyms=GIM2 {ECO:0000303|PubMed:19825635};
GN OrderedLocusNames=At5g49510 {ECO:0000312|Araport:AT5G49510};
GN ORFNames=K6M13.5 {ECO:0000312|EMBL:BAB10764.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INTERACTION WITH PFD6.
RC STRAIN=cv. Columbia;
RX PubMed=19004800; DOI=10.1073/pnas.0808652105;
RA Gu Y., Deng Z., Paredez A.R., DeBolt S., Wang Z.-Y., Somerville C.;
RT "Prefoldin 6 is required for normal microtubule dynamics and organization
RT in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18064-18069(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825635; DOI=10.1093/mp/ssp016;
RA Rodriguez-Milla M.A., Salinas J.;
RT "Prefoldins 3 and 5 play an essential role in Arabidopsis tolerance to salt
RT stress.";
RL Mol. Plant 2:526-534(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP INTERACTION WITH GAI.
RX PubMed=23583555; DOI=10.1016/j.cub.2013.03.053;
RA Locascio A., Blazquez M.A., Alabadi D.;
RT "Dynamic regulation of cortical microtubule organization through prefoldin-
RT DELLA interaction.";
RL Curr. Biol. 23:804-809(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY COLD, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28412546; DOI=10.1016/j.molp.2017.03.012;
RA Perea-Resa C., Rodriguez-Milla M.A., Iniesto E., Rubio V., Salinas J.;
RT "Prefoldins negatively regulate cold acclimation in Arabidopsis thaliana by
RT promoting nuclear proteasome-mediated HY5 degradation.";
RL Mol. Plant 10:791-804(2017).
RN [9]
RP INTERACTION WITH LSM8.
RC STRAIN=cv. Columbia;
RX PubMed=32396196; DOI=10.1093/nar/gkaa354;
RA Esteve-Bruna D., Carrasco-Lopez C., Blanco-Tourinan N., Iserte J.,
RA Calleja-Cabrera J., Perea-Resa C., Urbez C., Carrasco P., Yanovsky M.J.,
RA Blazquez M.A., Salinas J., Alabadi D.;
RT "Prefoldins contribute to maintaining the levels of the spliceosome LSM2-8
RT complex through Hsp90 in Arabidopsis.";
RL Nucleic Acids Res. 48:6280-6293(2020).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it (PubMed:19825635). Binds to nascent
CC polypeptide chain and promotes folding in an environment in which there
CC are many competing pathways for nonnative proteins (PubMed:19825635).
CC Together with other chaperonins, contribute to the regulation of gene
CC expression by modulating the spliceosome function on pre-mRNA splicing
CC post-transcriptionally by acting as a co-chaperone of Hsp90 to control
CC levels of LSM8 (By similarity). Required for the biogenesis of tubulins
CC and for subsequent microtubules (MTs) organization and dynamicity
CC (PubMed:19825635). Necessary for tolerance to NaCl salt stress
CC (PubMed:19825635). Involved in the process leading to microtubules
CC dissociation in response to gibberellic acid (GA) probably due to the
CC DELLA proteins-mediated translocation of the prefoldin co-chaperone
CC complex from the cytoplasm to the nucleus (By similarity). Prevents
CC cold acclimation (e.g. 7 days at 4 degrees Celsius) in a DELLA
CC proteins-dependent manner by promoting nuclear proteasome-mediated HY5
CC degradation, thus modulating the expression of several genes and
CC reducing anthocyanin biosynthesis, but seems not involved in
CC constitutive freezing tolerance (PubMed:28412546).
CC {ECO:0000250|UniProtKB:P57742, ECO:0000250|UniProtKB:Q2HIK4,
CC ECO:0000269|PubMed:19825635, ECO:0000269|PubMed:28412546}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits forming prefoldin co-chaperone complex (By similarity).
CC Interacts with PFD6 (PubMed:19004800). Binds to the DELLA protein GAI
CC (PubMed:23583555). Interacts with LSM8, a specific subunit of the LSM2-
CC 8 complex, which is a core component of the spliceosome
CC (PubMed:32396196). {ECO:0000250|UniProtKB:P46988,
CC ECO:0000269|PubMed:19004800, ECO:0000269|PubMed:23583555,
CC ECO:0000269|PubMed:32396196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28412546}. Nucleus
CC {ECO:0000269|PubMed:28412546}. Note=In the presence of gibberellic acid
CC (GA) and at room temperature, the prefoldin complex stays in the
CC cytoplasm and is functional (PubMed:28412546). But in the absence of GA
CC or in response to cold, the prefoldin complex is localized to the
CC nucleus in the presence of DELLA proteins, which severely compromises
CC alpha/beta-tubulin heterodimer availability, thus affecting
CC microtubules (MTs) organization (PubMed:28412546). This changing
CC subcellular localization follows a daily rhythm coordinated oscillation
CC (By similarity). {ECO:0000250|UniProtKB:P57742,
CC ECO:0000269|PubMed:28412546}.
CC -!- INDUCTION: Accumulates in response to cold.
CC {ECO:0000269|PubMed:28412546}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of alpha- and beta-tubulin
CC (PubMed:19825635). Altered development patterns and disturbed
CC microtubules (MTs) organization (PubMed:19825635). Hypersensitivity to
CC high NaCl salt levels (PubMed:19825635). Increased capacity to tolerate
CC freezing temperatures upon acclimation (e.g. 7 days at 4 degrees
CC Celsius) associated with a continuous accumulation of HY5 in cold
CC conditions (PubMed:28412546). {ECO:0000269|PubMed:19825635,
CC ECO:0000269|PubMed:28412546}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; AB023033; BAB10764.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95822.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95823.1; -; Genomic_DNA.
DR EMBL; AF370354; AAK44169.1; -; mRNA.
DR EMBL; AY059071; AAL15177.1; -; mRNA.
DR RefSeq; NP_001032045.1; NM_001036968.2.
DR RefSeq; NP_199762.1; NM_124328.3.
DR AlphaFoldDB; P57741; -.
DR SMR; P57741; -.
DR BioGRID; 20257; 10.
DR IntAct; P57741; 2.
DR STRING; 3702.AT5G49510.1; -.
DR iPTMnet; P57741; -.
DR PaxDb; P57741; -.
DR PRIDE; P57741; -.
DR ProteomicsDB; 236462; -.
DR DNASU; 835011; -.
DR EnsemblPlants; AT5G49510.1; AT5G49510.1; AT5G49510.
DR EnsemblPlants; AT5G49510.2; AT5G49510.2; AT5G49510.
DR GeneID; 835011; -.
DR Gramene; AT5G49510.1; AT5G49510.1; AT5G49510.
DR Gramene; AT5G49510.2; AT5G49510.2; AT5G49510.
DR KEGG; ath:AT5G49510; -.
DR Araport; AT5G49510; -.
DR TAIR; locus:2157819; AT5G49510.
DR eggNOG; KOG3313; Eukaryota.
DR HOGENOM; CLU_083737_1_0_1; -.
DR InParanoid; P57741; -.
DR OMA; WIGANVM; -.
DR OrthoDB; 1567796at2759; -.
DR PhylomeDB; P57741; -.
DR PRO; PR:P57741; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P57741; baseline and differential.
DR Genevisible; P57741; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0016272; C:prefoldin complex; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0071370; P:cellular response to gibberellin stimulus; ISS:UniProtKB.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR016655; PFD3.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12409; PTHR12409; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Coiled coil; Cytoplasm; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..195
FT /note="Prefoldin subunit 3"
FT /id="PRO_0000153657"
FT COILED 134..161
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 195 AA; 21465 MW; C1F018964AA6758E CRC64;
MSSSSPSGSG SDLTERRGIP AAKFIQDVET YLSQSGLDPN SALAFHQERL QQYKVVEMKL
LAQQRDLQAK IPDIEKCLEV VATLEAKKGT GEALLADFEV SEGIYSRACI EDTDSVCLWL
GANVMLEYSC EEASALLKNN LENAKASLEV LVADLQFLRD QVTVTQVTIA RVYNWDVHQR
RVKQVTPTAI AVADS
