ID   PFD3_PONAB              Reviewed;         197 AA.
AC   Q5RCG9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Prefoldin subunit 3;
DE   AltName: Full=von Hippel-Lindau-binding protein 1;
DE            Short=VBP-1;
DE            Short=VHL-binding protein 1;
GN   Name=VBP1; Synonyms=PFDN3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits. Binds to the C-terminal part of VHL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=In complex with VHL can translocate to the nucleus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC       {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; CR858301; CAH90538.1; -; mRNA.
DR   RefSeq; NP_001129019.1; NM_001135547.1.
DR   AlphaFoldDB; Q5RCG9; -.
DR   SMR; Q5RCG9; -.
DR   STRING; 9601.ENSPPYP00000023400; -.
DR   Ensembl; ENSPPYT00000024378; ENSPPYP00000023400; ENSPPYG00000020900.
DR   GeneID; 100190860; -.
DR   KEGG; pon:100190860; -.
DR   CTD; 7411; -.
DR   eggNOG; KOG3313; Eukaryota.
DR   GeneTree; ENSGT00390000018904; -.
DR   HOGENOM; CLU_083737_1_0_1; -.
DR   InParanoid; Q5RCG9; -.
DR   OMA; DEQHSKY; -.
DR   OrthoDB; 1567796at2759; -.
DR   TreeFam; TF313706; -.
DR   Proteomes; UP000001595; Chromosome X.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; IEA:Ensembl.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
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:0006457; P:protein folding; IEA:Ensembl.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR016655; PFD3.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12409; PTHR12409; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61758"
FT   CHAIN           2..197
FT                   /note="Prefoldin subunit 3"
FT                   /id="PRO_0000153654"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P61758"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61758"
SQ   SEQUENCE   197 AA;  22626 MW;  973BA048048D948E CRC64;
     MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY
     KFMELNLAQK KRRLKGQIPE IKQTLEILKY MQKKKESTNS METRFLLADN LYCKASVPPT
     DKVCLWLGAN VMLEYDIDEA QALLEKNLST ATKNLDSLEE DLDFLRDQFT TTEVNMARVY
     NWDVKRRNKD DSTKNKA