ID   PFD2_RAT                Reviewed;         154 AA.
AC   B0BN18;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Prefoldin subunit 2;
GN   Name=Pfdn2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC       transfers target proteins to it. Binds to nascent polypeptide chain and
CC       promotes folding in an environment in which there are many competing
CC       pathways for nonnative proteins. {ECO:0000250|UniProtKB:Q9UHV9}.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits. Component of the PAQosome complex which is responsible for
CC       the biogenesis of several protein complexes and which consists of R2TP
CC       complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members
CC       PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and
CC       DNAAF10/WDR92. Interacts with URI1; the interaction is phosphorylation-
CC       dependent and occurs in a growth-dependent manner.
CC       {ECO:0000250|UniProtKB:P40005, ECO:0000250|UniProtKB:Q9UHV9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UHV9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9UHV9}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9UHV9}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; BC158649; AAI58650.1; -; mRNA.
DR   RefSeq; NP_001102946.1; NM_001109476.1.
DR   AlphaFoldDB; B0BN18; -.
DR   SMR; B0BN18; -.
DR   BioGRID; 600470; 1.
DR   STRING; 10116.ENSRNOP00000005346; -.
DR   iPTMnet; B0BN18; -.
DR   PhosphoSitePlus; B0BN18; -.
DR   jPOST; B0BN18; -.
DR   PaxDb; B0BN18; -.
DR   PeptideAtlas; B0BN18; -.
DR   PRIDE; B0BN18; -.
DR   Ensembl; ENSRNOT00000005346; ENSRNOP00000005346; ENSRNOG00000066932.
DR   GeneID; 685607; -.
DR   KEGG; rno:685607; -.
DR   UCSC; RGD:1591406; rat.
DR   CTD; 5202; -.
DR   RGD; 1591406; Pfdn2.
DR   eggNOG; KOG4098; Eukaryota.
DR   GeneTree; ENSGT00390000009272; -.
DR   HOGENOM; CLU_113004_0_0_1; -.
DR   InParanoid; B0BN18; -.
DR   OMA; RKCFRQI; -.
DR   OrthoDB; 1564069at2759; -.
DR   PhylomeDB; B0BN18; -.
DR   TreeFam; TF313252; -.
DR   ChiTaRS; Pfdn2; rat.
DR   PRO; PR:B0BN18; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003983; Expressed in frontal cortex and 20 other tissues.
DR   Genevisible; B0BN18; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0016272; C:prefoldin complex; ISO:RGD.
DR   GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:RGD.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR   GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR   GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR   GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:RGD.
DR   GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; ISO:RGD.
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   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Mitochondrion; Nucleus; Reference proteome.
FT   CHAIN           1..154
FT                   /note="Prefoldin subunit 2"
FT                   /id="PRO_0000330360"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  16580 MW;  AE949993A9AD6715 CRC64;
     MADSSGRVGK SGGSGTGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
     LKEVDETRKC YRMVGGVLVE RTVKEVLPAL EGNKEQIQKI IETLSQQLQA KGKELNEFRE
     KHNIRLMGED EKPAAKENSE GAGAKSSSAG VLVS