PFD3_DROME
ID PFD3_DROME Reviewed; 194 AA.
AC Q9VGP6; Q86PA8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Prefoldin subunit 3;
DE AltName: Full=Protein merry-go-round;
DE AltName: Full=von Hippel-Lindau-binding protein 1;
GN Name=mgr; ORFNames=CG6719;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SELF-ASSOCIATION, INTERACTION
RP WITH VHL; BETATUB56D AND TUBULIN ALPHA-BETA HETERODIMER, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22451918; DOI=10.1073/pnas.1108537109;
RA Delgehyr N., Wieland U., Rangone H., Pinson X., Mao G., Dzhindzhev N.S.,
RA McLean D., Riparbelli M.G., Llamazares S., Callaini G., Gonzalez C.,
RA Glover D.M.;
RT "Drosophila Mgr, a Prefoldin subunit cooperating with von Hippel Lindau to
RT regulate tubulin stability.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5729-5734(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=3138251; DOI=10.1242/jcs.89.1.39;
RA Gonzalez C., Casal J., Ripoll P.;
RT "Functional monopolar spindles caused by mutation in mgr, a cell division
RT gene of Drosophila melanogaster.";
RL J. Cell Sci. 89:39-47(1988).
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). Required for tubulin
CC stability and spindle and centrosome formation in cooperation with Vhl.
CC {ECO:0000250, ECO:0000269|PubMed:22451918}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits (By similarity). Interacts with itself. Interacts with Vhl and
CC betaTub56D/tubulin beta-1 chain. Interacts with tubulin alpha-beta
CC heterodimers by itself or in complex with Vhl. Does not interact with
CC microtubules (MTs). {ECO:0000250, ECO:0000269|PubMed:22451918}.
CC -!- INTERACTION:
CC Q9VGP6; Q9VCZ8: Pfdn5; NbExp=4; IntAct=EBI-186707, EBI-100243;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22451918}.
CC -!- TISSUE SPECIFICITY: Expressed in larval central nervous system (CNS)
CC and pupal testis (at protein level). {ECO:0000269|PubMed:22451918}.
CC -!- DISRUPTION PHENOTYPE: Pupal lethal. Most mutants die just before
CC emergence from the pupal case. In mutant larval CNS, neuroblasts show
CC bipolar spindles that may lack one or both centrosomes or monopolar
CC spindles having one or two centrosomes at the single pole. The mitotic
CC index is elevated twofold over that in wild-type larval brains and the
CC ratio of metaphase:anaphase two- to threefold over wild-type. Mutant
CC neuroblasts also show a decrease of 25% in betaTub56D/tubulin beta
CC chain-1 expression. Mutant mature primary spermatocytes show impaired
CC MT network resulting in meiotic spindles either absent or highly
CC abnormal. In mutant testis, decreased expression of betaTub85D/tubulin
CC beta-2 chain is observed. {ECO:0000269|PubMed:22451918,
CC ECO:0000269|PubMed:3138251}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF54630.1; -; Genomic_DNA.
DR EMBL; BT003247; AAO25004.1; -; mRNA.
DR RefSeq; NP_650067.1; NM_141810.4.
DR AlphaFoldDB; Q9VGP6; -.
DR SMR; Q9VGP6; -.
DR BioGRID; 66498; 20.
DR IntAct; Q9VGP6; 5.
DR STRING; 7227.FBpp0081882; -.
DR PaxDb; Q9VGP6; -.
DR PeptideAtlas; Q9VGP6; -.
DR PRIDE; Q9VGP6; -.
DR DNASU; 41365; -.
DR EnsemblMetazoa; FBtr0082406; FBpp0081882; FBgn0264694.
DR GeneID; 41365; -.
DR KEGG; dme:Dmel_CG6719; -.
DR UCSC; CG6719-RA; d. melanogaster.
DR CTD; 41365; -.
DR FlyBase; FBgn0264694; mgr.
DR VEuPathDB; VectorBase:FBgn0264694; -.
DR eggNOG; KOG3313; Eukaryota.
DR GeneTree; ENSGT00390000018904; -.
DR HOGENOM; CLU_083737_1_0_1; -.
DR InParanoid; Q9VGP6; -.
DR OMA; DEQHSKY; -.
DR OrthoDB; 1567796at2759; -.
DR PhylomeDB; Q9VGP6; -.
DR SignaLink; Q9VGP6; -.
DR BioGRID-ORCS; 41365; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41365; -.
DR PRO; PR:Q9VGP6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0264694; Expressed in secondary oocyte and 25 other tissues.
DR Genevisible; Q9VGP6; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0016272; C:prefoldin complex; IDA:FlyBase.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:FlyBase.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IMP:FlyBase.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:FlyBase.
DR GO; GO:0007017; P:microtubule-based process; IMP:FlyBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:FlyBase.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..194
FT /note="Prefoldin subunit 3"
FT /id="PRO_0000153656"
SQ SEQUENCE 194 AA; 22314 MW; 928F29B114A05DAF CRC64;
MTGIMDSVEM PKLPENQKTF AGIPEAVFLE EIDTFMSQPE NENCEKVLQR LDEQHGKYRF
MACNLEARRR KLKSQIPDLE RSLEMVNVLR KEDEERETQF LLSDQVFIKT LVPPTKTVYL
WLGASVMLEY PLDEAEALLN QNITSAVGNL KSVEHDQDFL RDQITTTEVN MARVYNWGVK
KRQAATKTTA TTPS
