PFD2_HUMAN
ID PFD2_HUMAN Reviewed; 154 AA.
AC Q9UHV9; Q9P0P7; Q9UN05;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Prefoldin subunit 2;
GN Name=PFDN2; Synonyms=PFD2; ORFNames=HSPC231;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Xu Y., Yu Y., Fang C., Zhang H., Ying H., Yan J., Chang Y.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Skin;
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 [5]
RP FUNCTION.
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 [6]
RP INTERACTION WITH URI1, AND SUBCELLULAR LOCATION.
RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
RA Aebersold R., Hess D., Krek W.;
RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
RT activates a negative feedback program that counters S6K1 survival
RT signaling.";
RL Mol. Cell 28:28-40(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION IN THE PAQOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599;
RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M.,
RA Gauthier M.S., Coulombe B.;
RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the
RT PAQosome.";
RL J. Proteome Res. 19:18-27(2020).
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:0000269|PubMed:9630229}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits (By similarity). Component of the PAQosome complex which is
CC responsible for the biogenesis of several protein complexes and which
CC consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI
CC complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF,
CC POLR2E and DNAAF10/WDR92 (PubMed:31738558). Interacts with URI1; the
CC interaction is phosphorylation-dependent and occurs in a growth-
CC dependent manner (PubMed:17936702). {ECO:0000250|UniProtKB:P40005,
CC ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:31738558}.
CC -!- INTERACTION:
CC Q9UHV9; P07108-2: DBI; NbExp=3; IntAct=EBI-359873, EBI-12847580;
CC Q9UHV9; Q9NUG6: PDRG1; NbExp=2; IntAct=EBI-359873, EBI-307050;
CC Q9UHV9; O60925: PFDN1; NbExp=3; IntAct=EBI-359873, EBI-356919;
CC Q9UHV9; Q99471: PFDN5; NbExp=5; IntAct=EBI-359873, EBI-357275;
CC Q9UHV9; P63000: RAC1; NbExp=3; IntAct=EBI-359873, EBI-413628;
CC Q9UHV9; Q9H6T3: RPAP3; NbExp=2; IntAct=EBI-359873, EBI-356928;
CC Q9UHV9; P31930: UQCRC1; NbExp=3; IntAct=EBI-359873, EBI-1052596;
CC Q9UHV9; O94763: URI1; NbExp=2; IntAct=EBI-359873, EBI-357067;
CC Q9UHV9; Q9UBK9: UXT; NbExp=2; IntAct=EBI-359873, EBI-357355;
CC Q9UHV9; P61758: VBP1; NbExp=7; IntAct=EBI-359873, EBI-357430;
CC Q9UHV9; A6NNF4-2: ZNF726; NbExp=3; IntAct=EBI-359873, EBI-18338284;
CC Q9UHV9; P0C045; Xeno; NbExp=4; IntAct=EBI-359873, EBI-9351969;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17936702}. Cytoplasm
CC {ECO:0000269|PubMed:17936702}. Mitochondrion
CC {ECO:0000269|PubMed:17936702}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36151.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF117237; AAF17218.1; -; mRNA.
DR EMBL; AF165883; AAD47084.1; -; mRNA.
DR EMBL; AF151065; AAF36151.1; ALT_FRAME; mRNA.
DR EMBL; BC012464; AAH12464.1; -; mRNA.
DR EMBL; BC047042; AAH47042.1; -; mRNA.
DR CCDS; CCDS1217.1; -.
DR RefSeq; NP_036526.2; NM_012394.3.
DR RefSeq; XP_011507926.1; XM_011509624.2.
DR PDB; 6NR8; EM; 7.80 A; 2=22-124.
DR PDB; 6NR9; EM; 8.50 A; 2=22-124.
DR PDB; 6NRB; EM; 8.70 A; 2=22-124.
DR PDB; 6NRC; EM; 8.30 A; 2=22-124.
DR PDB; 6NRD; EM; 8.20 A; 2=22-124.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR AlphaFoldDB; Q9UHV9; -.
DR SMR; Q9UHV9; -.
DR BioGRID; 111224; 196.
DR ComplexPortal; CPX-6144; URI1 prefoldin co-chaperone complex.
DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex.
DR CORUM; Q9UHV9; -.
DR DIP; DIP-27557N; -.
DR IntAct; Q9UHV9; 91.
DR MINT; Q9UHV9; -.
DR STRING; 9606.ENSP00000356989; -.
DR ChEMBL; CHEMBL4295976; -.
DR GlyGen; Q9UHV9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHV9; -.
DR MetOSite; Q9UHV9; -.
DR PhosphoSitePlus; Q9UHV9; -.
DR SwissPalm; Q9UHV9; -.
DR BioMuta; PFDN2; -.
DR DMDM; 12643887; -.
DR EPD; Q9UHV9; -.
DR jPOST; Q9UHV9; -.
DR MassIVE; Q9UHV9; -.
DR MaxQB; Q9UHV9; -.
DR PaxDb; Q9UHV9; -.
DR PeptideAtlas; Q9UHV9; -.
DR PRIDE; Q9UHV9; -.
DR ProteomicsDB; 84419; -.
DR TopDownProteomics; Q9UHV9; -.
DR Antibodypedia; 34290; 181 antibodies from 28 providers.
DR DNASU; 5202; -.
DR Ensembl; ENST00000368010.4; ENSP00000356989.3; ENSG00000143256.5.
DR GeneID; 5202; -.
DR KEGG; hsa:5202; -.
DR MANE-Select; ENST00000368010.4; ENSP00000356989.3; NM_012394.4; NP_036526.2.
DR UCSC; uc001fxu.4; human.
DR CTD; 5202; -.
DR DisGeNET; 5202; -.
DR GeneCards; PFDN2; -.
DR HGNC; HGNC:8867; PFDN2.
DR HPA; ENSG00000143256; Low tissue specificity.
DR MIM; 613466; gene.
DR neXtProt; NX_Q9UHV9; -.
DR OpenTargets; ENSG00000143256; -.
DR PharmGKB; PA33208; -.
DR VEuPathDB; HostDB:ENSG00000143256; -.
DR eggNOG; KOG4098; Eukaryota.
DR GeneTree; ENSGT00390000009272; -.
DR HOGENOM; CLU_113004_0_0_1; -.
DR InParanoid; Q9UHV9; -.
DR OMA; RKCFRQI; -.
DR OrthoDB; 1564069at2759; -.
DR PhylomeDB; Q9UHV9; -.
DR TreeFam; TF313252; -.
DR PathwayCommons; Q9UHV9; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR SignaLink; Q9UHV9; -.
DR BioGRID-ORCS; 5202; 790 hits in 1081 CRISPR screens.
DR ChiTaRS; PFDN2; human.
DR GeneWiki; PFDN2; -.
DR GenomeRNAi; 5202; -.
DR Pharos; Q9UHV9; Tbio.
DR PRO; PR:Q9UHV9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UHV9; protein.
DR Bgee; ENSG00000143256; Expressed in C1 segment of cervical spinal cord and 202 other tissues.
DR ExpressionAtlas; Q9UHV9; baseline and differential.
DR Genevisible; Q9UHV9; HS.
DR GO; GO:0101031; C:chaperone complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016272; C:prefoldin complex; IDA:FlyBase.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:FlyBase.
DR GO; GO:0044183; F:protein folding chaperone; IPI:AgBase.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:FlyBase.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IDA:AgBase.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
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 3D-structure; Chaperone; Cytoplasm; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1..154
FT /note="Prefoldin subunit 2"
FT /id="PRO_0000124835"
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"
FT CONFLICT 14..22
FT /note="SGAGKGAVS -> TPRRGRGRCP (in Ref. 2; AAD47084)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="Missing (in Ref. 3; AAF36151)"
FT /evidence="ECO:0000305"
FT CONFLICT 29..34
FT /note="GFNRLR -> SFNAF (in Ref. 3; AAF36151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 16648 MW; 2FC68A7425412198 CRC64;
MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE
KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS
