PFD2_MOUSE
ID PFD2_MOUSE Reviewed; 154 AA.
AC O70591; Q8R0H2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Prefoldin subunit 2;
GN Name=Pfdn2; Synonyms=Pfd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9630229; DOI=10.1016/s0092-8674(00)81446-4;
RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
RA Klein H.L., Cowan N.J.;
RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
RT chaperonin.";
RL Cell 93:863-873(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Colon;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
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; Y17393; CAA76760.1; -; mRNA.
DR EMBL; BC026839; AAH26839.1; -; mRNA.
DR EMBL; BC049606; AAH49606.1; -; mRNA.
DR CCDS; CCDS15491.1; -.
DR RefSeq; NP_035200.2; NM_011070.3.
DR AlphaFoldDB; O70591; -.
DR SMR; O70591; -.
DR BioGRID; 202121; 48.
DR IntAct; O70591; 29.
DR MINT; O70591; -.
DR STRING; 10090.ENSMUSP00000120106; -.
DR iPTMnet; O70591; -.
DR PhosphoSitePlus; O70591; -.
DR REPRODUCTION-2DPAGE; IPI00119545; -.
DR REPRODUCTION-2DPAGE; O70591; -.
DR EPD; O70591; -.
DR jPOST; O70591; -.
DR MaxQB; O70591; -.
DR PaxDb; O70591; -.
DR PeptideAtlas; O70591; -.
DR PRIDE; O70591; -.
DR ProteomicsDB; 289474; -.
DR Antibodypedia; 34290; 181 antibodies from 28 providers.
DR DNASU; 18637; -.
DR Ensembl; ENSMUST00000135941; ENSMUSP00000120106; ENSMUSG00000006412.
DR GeneID; 18637; -.
DR KEGG; mmu:18637; -.
DR UCSC; uc007doc.1; mouse.
DR CTD; 5202; -.
DR MGI; MGI:1276111; Pfdn2.
DR VEuPathDB; HostDB:ENSMUSG00000006412; -.
DR eggNOG; KOG4098; Eukaryota.
DR GeneTree; ENSGT00390000009272; -.
DR HOGENOM; CLU_113004_0_0_1; -.
DR InParanoid; O70591; -.
DR OMA; RKCFRQI; -.
DR OrthoDB; 1564069at2759; -.
DR PhylomeDB; O70591; -.
DR TreeFam; TF313252; -.
DR BioGRID-ORCS; 18637; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Pfdn2; mouse.
DR PRO; PR:O70591; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O70591; protein.
DR Bgee; ENSMUSG00000006412; Expressed in embryonic brain and 255 other tissues.
DR ExpressionAtlas; O70591; baseline and differential.
DR Genevisible; O70591; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016272; C:prefoldin complex; ISO:MGI.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:MGI.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IDA:MGI.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..154
FT /note="Prefoldin subunit 2"
FT /id="PRO_0000124836"
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"
FT CONFLICT 14..17
FT /note="SGAG -> TARW (in Ref. 1; CAA76760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 16534 MW; A34F229309AC6715 CRC64;
MADSSGRVGK SGGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
LKEVDETRKC YRMVGGVLVE RTVKEVLPAL EGNKEQIQKI IETLSQQLQA KGKELNEFRE
KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS
