ID   PFD2_BOVIN              Reviewed;         154 AA.
AC   A1A4P5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Prefoldin subunit 2;
GN   Name=PFDN2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; BC126786; AAI26787.1; -; mRNA.
DR   RefSeq; NP_001073690.1; NM_001080221.2.
DR   AlphaFoldDB; A1A4P5; -.
DR   SMR; A1A4P5; -.
DR   STRING; 9913.ENSBTAP00000026841; -.
DR   PaxDb; A1A4P5; -.
DR   PeptideAtlas; A1A4P5; -.
DR   PRIDE; A1A4P5; -.
DR   Ensembl; ENSBTAT00000026841; ENSBTAP00000026841; ENSBTAG00000020152.
DR   GeneID; 404138; -.
DR   KEGG; bta:404138; -.
DR   CTD; 5202; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020152; -.
DR   VGNC; VGNC:59188; PFDN2.
DR   eggNOG; KOG4098; Eukaryota.
DR   GeneTree; ENSGT00390000009272; -.
DR   HOGENOM; CLU_113004_0_0_1; -.
DR   InParanoid; A1A4P5; -.
DR   OMA; RKCFRQI; -.
DR   OrthoDB; 1564069at2759; -.
DR   TreeFam; TF313252; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000020152; Expressed in pons and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; IEA:Ensembl.
DR   GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IEA:Ensembl.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR   GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
DR   GO; GO:0051495; P:positive regulation of cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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_0000282857"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  16648 MW;  95933161C41BBA16 CRC64;
     MAENGGRAGK SSGSGTGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
     LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE
     KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS