ID   PFD2_CAEEL              Reviewed;         141 AA.
AC   Q9N5M2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Prefoldin subunit 2;
GN   Name=pfd-2 {ECO:0000312|WormBase:H20J04.5};
GN   Synonyms=tag-355 {ECO:0000312|WormBase:H20J04.5};
GN   ORFNames=H20J04.5 {ECO:0000312|WormBase:H20J04.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; FO080156; CCD61681.1; -; Genomic_DNA.
DR   RefSeq; NP_494764.1; NM_062363.5.
DR   AlphaFoldDB; Q9N5M2; -.
DR   SMR; Q9N5M2; -.
DR   BioGRID; 39124; 17.
DR   IntAct; Q9N5M2; 5.
DR   STRING; 6239.H20J04.5; -.
DR   iPTMnet; Q9N5M2; -.
DR   EPD; Q9N5M2; -.
DR   PaxDb; Q9N5M2; -.
DR   PeptideAtlas; Q9N5M2; -.
DR   EnsemblMetazoa; H20J04.5.1; H20J04.5.1; WBGene00019220.
DR   GeneID; 173768; -.
DR   KEGG; cel:CELE_H20J04.5; -.
DR   CTD; 173768; -.
DR   WormBase; H20J04.5; CE23815; WBGene00019220; pfd-2.
DR   eggNOG; KOG4098; Eukaryota.
DR   GeneTree; ENSGT00390000009272; -.
DR   HOGENOM; CLU_113004_0_1_1; -.
DR   InParanoid; Q9N5M2; -.
DR   OMA; RKCFRQI; -.
DR   OrthoDB; 1564069at2759; -.
DR   PhylomeDB; Q9N5M2; -.
DR   SignaLink; Q9N5M2; -.
DR   PRO; PR:Q9N5M2; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00019220; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR   GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR   GO; GO:0030017; C:sarcomere; HDA:WormBase.
DR   GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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   3: Inferred from homology;
KW   Chaperone; Reference proteome.
FT   CHAIN           1..141
FT                   /note="Prefoldin subunit 2"
FT                   /id="PRO_0000124837"
SQ   SEQUENCE   141 AA;  16050 MW;  5608014D515665E6 CRC64;
     MSAAQTAAAT PAEQEEQRKV VEKFKALRDQ QQDIAAEVTR IEEERREFGR VLEVIKDLEP
     DQKCFRLISD TLVEYTVKDV IPDLQNNIAN LTIVSKQLND QLVEKGKELN THKTTHNIRL
     LTEKESAELR KAEALGQLPK A