ID   PFD1_ARATH              Reviewed;         128 AA.
AC   Q94AF7; Q9ZQK7; Q9ZQK8;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Prefoldin subunit 1 {ECO:0000303|PubMed:19825635};
DE   AltName: Full=Gene involved in microtubule biogenesis 6 {ECO:0000303|PubMed:19825635};
GN   Name=PFD1 {ECO:0000303|PubMed:19825635};
GN   Synonyms=GIM6 {ECO:0000303|PubMed:19825635};
GN   OrderedLocusNames=At2g07340 {ECO:0000312|Araport:AT2G07340};
GN   ORFNames=T13E11.11 {ECO:0000312|EMBL:AAD15526.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   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   [6]
RP   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   [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   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 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: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   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD15526.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAD15527.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC006217; AAD15526.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC006217; AAD15527.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06048.1; -; Genomic_DNA.
DR   EMBL; AY048212; AAK82475.1; -; mRNA.
DR   EMBL; AY094019; AAM16175.1; -; mRNA.
DR   EMBL; AY087310; AAM64861.1; -; mRNA.
DR   PIR; F84484; F84484.
DR   PIR; G84484; G84484.
DR   RefSeq; NP_850990.1; NM_180659.3.
DR   SMR; Q94AF7; -.
DR   IntAct; Q94AF7; 2.
DR   STRING; 3702.AT2G07340.1; -.
DR   PRIDE; Q94AF7; -.
DR   ProteomicsDB; 176753; -.
DR   EnsemblPlants; AT2G07340.1; AT2G07340.1; AT2G07340.
DR   GeneID; 815304; -.
DR   Gramene; AT2G07340.1; AT2G07340.1; AT2G07340.
DR   Araport; AT2G07340; -.
DR   TAIR; locus:2054845; AT2G07340.
DR   eggNOG; KOG3501; Eukaryota.
DR   HOGENOM; CLU_122140_2_1_1; -.
DR   OMA; MAQMDME; -.
DR   OrthoDB; 1492856at2759; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q94AF7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; IBA:GO_Central.
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; ISS: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; 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..128
FT                   /note="Prefoldin subunit 1"
FT                   /id="PRO_0000455728"
FT   COILED          17..37
FT                   /evidence="ECO:0000255"
FT   COILED          81..115
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   128 AA;  14605 MW;  2A0227EB0215BA09 CRC64;
     MADEATRAAF MEIQASMIEL TGKLKQVQNQ MRNKEGDRKR AFLTLEELRP LPEETNTYKS
     IGRTFVLEPK TVLEGEQEQK LKDSEAAVAS LQTSKEYLEK QVAEVENNLR ELLQQEPGIA
     QQIMSMSM