ID   PFD3_BOVIN              Reviewed;         197 AA.
AC   Q2TBX2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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   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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) 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}.
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DR   EMBL; BC109526; AAI09527.1; -; mRNA.
DR   RefSeq; NP_001033605.1; NM_001038516.2.
DR   AlphaFoldDB; Q2TBX2; -.
DR   SMR; Q2TBX2; -.
DR   STRING; 9913.ENSBTAP00000022946; -.
DR   PaxDb; Q2TBX2; -.
DR   PRIDE; Q2TBX2; -.
DR   GeneID; 508727; -.
DR   KEGG; bta:508727; -.
DR   CTD; 7411; -.
DR   eggNOG; KOG3313; Eukaryota.
DR   InParanoid; Q2TBX2; -.
DR   OrthoDB; 1567796at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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_0000282856"
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;  22483 MW;  B5B74277D1ECA4BC CRC64;
     MAASKDGCGV GEVAAGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADIVL KKLDEQYQKY
     KFMELNLAQK KRRLKGQIPE IKQTLEILKY KQKKKESTSS LETRFLLADN LYCKASVPPT
     DKVCLWLGAN VMLEYDIDEA QALLEKNLLT ATKNLDSLEE DLDFLRDQFT TTEVNMARVY
     NWDVKRRNKD DSTKNKA