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Prefoldin subunit 3 (Protein merry-go-round) (von Hippel-Lindau-binding protein 1)

 PFD3_DROME              Reviewed;         194 AA.
Q9VGP6; Q86PA8;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 3.
23-MAY-2018, entry version 113.
RecName: Full=Prefoldin subunit 3;
AltName: Full=Protein merry-go-round;
AltName: Full=von Hippel-Lindau-binding protein 1;
Name=mgr; ORFNames=CG6719;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SELF-ASSOCIATION,
INTERACTION WITH VHL; BETATUB56D AND TUBULIN ALPHA-BETA HETERODIMER,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=22451918; DOI=10.1073/pnas.1108537109;
Delgehyr N., Wieland U., Rangone H., Pinson X., Mao G.,
Dzhindzhev N.S., McLean D., Riparbelli M.G., Llamazares S.,
Callaini G., Gonzalez C., Glover D.M.;
"Drosophila Mgr, a Prefoldin subunit cooperating with von Hippel
Lindau to regulate tubulin stability.";
Proc. Natl. Acad. Sci. U.S.A. 109:5729-5734(2012).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
DISRUPTION PHENOTYPE.
PubMed=3138251;
Gonzalez C., Casal J., Ripoll P.;
"Functional monopolar spindles caused by mutation in mgr, a cell
division gene of Drosophila melanogaster.";
J. Cell Sci. 89:39-47(1988).
-!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
transfers target proteins to it. Binds to nascent polypeptide
chain and promotes folding in an environment in which there are
many competing pathways for nonnative proteins (By similarity).
Required for tubulin stability and spindle and centrosome
formation in cooperation with Vhl. {ECO:0000250,
ECO:0000269|PubMed:22451918}.
-!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
type subunits (By similarity). Interacts with itself. Interacts
with Vhl and betaTub56D/tubulin beta-1 chain. Interacts with
tubulin alpha-beta heterodimers by itself or in complex with Vhl.
Does not interact with microtubules (MTs). {ECO:0000250,
ECO:0000269|PubMed:22451918}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22451918}.
-!- TISSUE SPECIFICITY: Expressed in larval central nervous system
(CNS) and pupal testis (at protein level).
{ECO:0000269|PubMed:22451918}.
-!- DISRUPTION PHENOTYPE: Pupal lethal. Most mutants die just before
emergence from the pupal case. In mutant larval CNS, neuroblasts
show bipolar spindles that may lack one or both centrosomes or
monopolar spindles having one or two centrosomes at the single
pole. The mitotic index is elevated twofold over that in wild-type
larval brains and the ratio of metaphase:anaphase two- to
threefold over wild-type. Mutant neuroblasts also show a decrease
of 25% in betaTub56D/tubulin beta chain-1 expression. Mutant
mature primary spermatocytes show impaired MT network resulting in
meiotic spindles either absent or highly abnormal. In mutant
testis, decreased expression of betaTub85D/tubulin beta-2 chain is
observed. {ECO:0000269|PubMed:22451918,
ECO:0000269|PubMed:3138251}.
-!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
{ECO:0000305}.
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EMBL; AE014297; AAF54630.1; -; Genomic_DNA.
EMBL; BT003247; AAO25004.1; -; mRNA.
RefSeq; NP_650067.1; NM_141810.4.
UniGene; Dm.7197; -.
ProteinModelPortal; Q9VGP6; -.
SMR; Q9VGP6; -.
BioGrid; 66498; 20.
IntAct; Q9VGP6; 2.
STRING; 7227.FBpp0081882; -.
PaxDb; Q9VGP6; -.
PeptideAtlas; Q9VGP6; -.
PRIDE; Q9VGP6; -.
EnsemblMetazoa; FBtr0082406; FBpp0081882; FBgn0264694.
GeneID; 41365; -.
KEGG; dme:Dmel_CG6719; -.
UCSC; CG6719-RA; d. melanogaster.
CTD; 41365; -.
FlyBase; FBgn0264694; mgr.
eggNOG; KOG3313; Eukaryota.
eggNOG; ENOG410XRZ8; LUCA.
GeneTree; ENSGT00390000018904; -.
InParanoid; Q9VGP6; -.
OMA; QITVMEV; -.
OrthoDB; EOG091G0P5N; -.
PhylomeDB; Q9VGP6; -.
GenomeRNAi; 41365; -.
PRO; PR:Q9VGP6; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0264694; -.
Genevisible; Q9VGP6; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005844; C:polysome; IBA:GO_Central.
GO; GO:0016272; C:prefoldin complex; IDA:FlyBase.
GO; GO:0048487; F:beta-tubulin binding; IDA:FlyBase.
GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IMP:FlyBase.
GO; GO:0007017; P:microtubule-based process; IMP:FlyBase.
GO; GO:0090307; P:mitotic spindle assembly; IMP:FlyBase.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0090306; P:spindle assembly involved in meiosis; IMP:FlyBase.
GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
Gene3D; 1.10.287.370; -; 1.
InterPro; IPR016655; PFD3.
InterPro; IPR009053; Prefoldin.
InterPro; IPR004127; Prefoldin_subunit_alpha.
PANTHER; PTHR12409; PTHR12409; 1.
Pfam; PF02996; Prefoldin; 1.
PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Cytoplasm; Reference proteome.
CHAIN 1 194 Prefoldin subunit 3.
/FTId=PRO_0000153656.
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


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