PFD6_ARATH
ID PFD6_ARATH Reviewed; 129 AA.
AC Q2HIK4; Q8GYJ1; Q9C8S0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Prefoldin subunit 6 {ECO:0000303|PubMed:19825635};
DE AltName: Full=Gene involved in microtubule biogenesis 1 {ECO:0000303|PubMed:19825635};
GN Name=PFD6 {ECO:0000303|PubMed:19825635};
GN Synonyms=GIM1 {ECO:0000303|PubMed:19825635};
GN OrderedLocusNames=At1g29990 {ECO:0000312|Araport:AT1G29990};
GN ORFNames=T1P2.3 {ECO:0000312|EMBL:AAG52059.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PFD2; PFD3; PFD4 AND PFD5.
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 FUNCTION, AND SUBCELLULAR LOCATION.
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 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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=29463731; DOI=10.1073/pnas.1721760115;
RA Salanenka Y., Verstraeten I., Loefke C., Tabata K., Naramoto S., Glanc M.,
RA Friml J.;
RT "Gibberellin DELLA signaling targets the retromer complex to redirect
RT protein trafficking to the plasma membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3716-3721(2018).
RN [10]
RP FUNCTION, MUTAGENESIS OF ARG-83, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP LSM8 AND HSP90.
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 the biogenesis of
CC tubulins and for subsequent microtubules (MTs) organization and
CC dynamicity, but unable to associate with microtubules
CC (PubMed:19004800). 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 (PubMed:23583555).
CC Contributes to the GA-dependent regulation of PIN2 trafficking at the
CC plasma membrane, thus influencing auxin flux (PubMed:29463731).
CC {ECO:0000269|PubMed:19004800, ECO:0000269|PubMed:19825635,
CC ECO:0000269|PubMed:23583555, ECO:0000269|PubMed:29463731,
CC ECO:0000269|PubMed:32396196}.
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 PFD2, PFD3, PFD4 and PFD5 (PubMed:19004800). Interacts
CC with LSM8, a specific subunit of the LSM2-8 complex, which is a core
CC component of the spliceosome (PubMed:32396196). Binds to HSP90 to
CC facilitate the formation of a larger complex made at least of HSP90,
CC PFD6 and LSM8 (PubMed:32396196). {ECO:0000250|UniProtKB:P46988,
CC ECO:0000269|PubMed:19004800, ECO:0000269|PubMed:32396196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19004800,
CC ECO:0000269|PubMed:23583555}. Nucleus {ECO:0000269|PubMed:23583555}.
CC Note=In the presence of gibberellic acid (GA) and at room temperature,
CC the prefoldin complex stays in the cytoplasm and is functional
CC (PubMed:23583555). But in the absence of GA or in response to cold, the
CC prefoldin complex is localized to the nucleus in the presence of DELLA
CC proteins, which severely compromises alpha/beta-tubulin heterodimer
CC availability, thus affecting microtubules (MTs) organization
CC (PubMed:23583555). This changing subcellular localization follows a
CC daily rhythm coordinated oscillation (PubMed:23583555).
CC {ECO:0000269|PubMed:23583555}.
CC -!- INDUCTION: Accumulates in response to cold.
CC {ECO:0000269|PubMed:28412546}.
CC -!- DISRUPTION PHENOTYPE: Several microtubules (MTs) defects, including
CC hypersensitivity to oryzalin (a microtubule inhibitor), defects in cell
CC division, abnormal cortical array organization, and impaired
CC microtubule dynamicity, due to reduced tubulins levels
CC (PubMed:19004800). Reduced levels of PIN2 at the plasma membrane
CC (PubMed:29463731). The pfd5 pfd6 double mutant is less sensitive to
CC gibberellic acid (GA)-mediated mobilization of PIN2 at the plasma
CC membrane (PubMed:29463731). Lower pre-mRNA splicing events and reduced
CC production of U6 snRNA in plants lacking PFD2, PFD4 and PFD6, probably
CC due to a reduced activity of the LSM2-8 complex (PubMed:32396196).
CC {ECO:0000269|PubMed:19004800, ECO:0000269|PubMed:29463731,
CC ECO:0000269|PubMed:32396196}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52059.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022455; AAG52059.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31165.1; -; Genomic_DNA.
DR EMBL; AK117588; BAC42245.1; -; mRNA.
DR EMBL; BT024577; ABD38916.1; -; mRNA.
DR PIR; G86423; G86423.
DR RefSeq; NP_174292.2; NM_102739.4.
DR SMR; Q2HIK4; -.
DR IntAct; Q2HIK4; 6.
DR STRING; 3702.AT1G29990.1; -.
DR PRIDE; Q2HIK4; -.
DR ProteomicsDB; 187933; -.
DR EnsemblPlants; AT1G29990.1; AT1G29990.1; AT1G29990.
DR GeneID; 839878; -.
DR Gramene; AT1G29990.1; AT1G29990.1; AT1G29990.
DR KEGG; ath:AT1G29990; -.
DR Araport; AT1G29990; -.
DR TAIR; locus:2198289; AT1G29990.
DR eggNOG; KOG3478; Eukaryota.
DR HOGENOM; CLU_125172_0_0_1; -.
DR OMA; ETQYQEN; -.
DR OrthoDB; 1559044at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2HIK4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016272; C:prefoldin complex; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0071370; P:cellular response to gibberellin stimulus; IDA:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:1901703; P:protein localization involved in auxin polar transport; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR Pfam; PF01920; Prefoldin_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..129
FT /note="Prefoldin subunit 6"
FT /id="PRO_0000455729"
FT COILED 6..26
FT /evidence="ECO:0000255"
FT COILED 84..118
FT /evidence="ECO:0000255"
FT MUTAGEN 83
FT /note="R->Q: In pfd6-1; smaller plants and reduced levels
FT of LSM8 via a post-transcriptional process (at protein
FT level). Reduced production of U6 snRNA."
FT /evidence="ECO:0000269|PubMed:32396196"
FT CONFLICT 96
FT /note="A -> V (in Ref. 3; BAC42245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14856 MW; CAC8E95FD2A36873 CRC64;
MSSSTVRDLQ RDLENKANDL GKIQKDIGKN HQLRKKYTIQ LGENELVLKE LDLLEEDANV
YKLIGPVLVK QDLAEANANV RKRIEYISAE LKRLDAILQD MEEKQNNKRE TIMKLQQRLQ
TIQAGKAKA
