PFD2_ARATH
ID PFD2_ARATH Reviewed; 148 AA.
AC Q9LJ98;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Prefoldin subunit 2 {ECO:0000303|PubMed:19825635};
DE AltName: Full=Gene involved in microtubule biogenesis 4 {ECO:0000303|PubMed:19825635};
GN Name=PFD2 {ECO:0000303|PubMed:19825635};
GN Synonyms=GIM4 {ECO:0000303|PubMed:19825635};
GN OrderedLocusNames=At3g22480 {ECO:0000312|Araport:AT3G22480};
GN ORFNames=F16J14.4 {ECO:0000312|EMBL:BAB01463.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, 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 [7]
RP INDUCTION BY COLD.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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 (PubMed:32396196). Required for microtubules (MTs)
CC organization and dynamicity (By similarity). Involved in the process
CC leading to microtubules dissociation in response to gibberellic acid
CC (GA) probably due to the DELLA proteins-mediated translocation of the
CC prefoldin co-chaperone complex from the cytoplasm to the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:P57742,
CC ECO:0000250|UniProtKB:Q2HIK4, ECO:0000269|PubMed:32396196,
CC ECO:0000303|PubMed:19825635}.
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 LSM8, a specific subunit of the LSM2-8 complex, which is
CC a core component of the spliceosome (PubMed:32396196).
CC {ECO:0000250|UniProtKB:P46988, ECO:0000269|PubMed:32396196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P57742}. Nucleus
CC {ECO:0000250|UniProtKB:P57742}. Note=In the presence of gibberellic
CC acid (GA) and at room temperature, the prefoldin complex stays in the
CC cytoplasm and is functional (By similarity). 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 (By similarity). This changing
CC subcellular localization follows a daily rhythm coordinated oscillation
CC (By similarity). {ECO:0000250|UniProtKB:P57742}.
CC -!- INDUCTION: Accumulates in response to cold.
CC {ECO:0000269|PubMed:28412546}.
CC -!- DISRUPTION PHENOTYPE: Smaller plants (PubMed:32396196). Lower pre-mRNA
CC splicing events and reduced production of U6 snRNA in plants lacking
CC PFD2, PFD4 and PFD6, probably due to a reduced activity of the LSM2-8
CC complex (PubMed:32396196). {ECO:0000269|PubMed:32396196}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
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DR EMBL; AP000731; BAB01463.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76644.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76645.1; -; Genomic_DNA.
DR EMBL; AY113920; AAM44968.1; -; mRNA.
DR EMBL; AY034920; AAK59427.1; -; mRNA.
DR EMBL; AY086635; AAM63693.1; -; mRNA.
DR RefSeq; NP_188887.1; NM_113147.4.
DR RefSeq; NP_850626.1; NM_180295.1.
DR AlphaFoldDB; Q9LJ98; -.
DR SMR; Q9LJ98; -.
DR BioGRID; 7151; 6.
DR IntAct; Q9LJ98; 1.
DR STRING; 3702.AT3G22480.1; -.
DR iPTMnet; Q9LJ98; -.
DR PaxDb; Q9LJ98; -.
DR PRIDE; Q9LJ98; -.
DR ProteomicsDB; 236310; -.
DR DNASU; 821819; -.
DR EnsemblPlants; AT3G22480.1; AT3G22480.1; AT3G22480.
DR EnsemblPlants; AT3G22480.2; AT3G22480.2; AT3G22480.
DR GeneID; 821819; -.
DR Gramene; AT3G22480.1; AT3G22480.1; AT3G22480.
DR Gramene; AT3G22480.2; AT3G22480.2; AT3G22480.
DR KEGG; ath:AT3G22480; -.
DR Araport; AT3G22480; -.
DR TAIR; locus:2077071; AT3G22480.
DR eggNOG; KOG4098; Eukaryota.
DR HOGENOM; CLU_113004_0_0_1; -.
DR InParanoid; Q9LJ98; -.
DR OMA; RKCFRQI; -.
DR OrthoDB; 1564069at2759; -.
DR PhylomeDB; Q9LJ98; -.
DR PRO; PR:Q9LJ98; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJ98; baseline and differential.
DR Genevisible; Q9LJ98; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016272; C:prefoldin complex; ISS:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0071370; P:cellular response to gibberellin stimulus; ISS:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR027235; PFD2.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR13303; PTHR13303; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..148
FT /note="Prefoldin subunit 2"
FT /id="PRO_0000124839"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000255"
SQ SEQUENCE 148 AA; 16526 MW; 2193233D3BE26475 CRC64;
MASKSGSGGL REPPNEQAVL NMYEGKRSEL SQIYSNITDL EMQVSEHSLV INAIQPLDQS
RKCFRMIGGV LVERTIKEVL PAVQRNKDGL EEVVRKLYET LEKKKKDLTE FEAKYKIRIT
KQEDNKEGGN KKEGNAQGVL VGAASSSQ
