URI_DROME
ID URI_DROME Reviewed; 731 AA.
AC Q9W148; Q8T044;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Unconventional prefoldin RPB5 interactor-like protein {ECO:0000305};
GN Name=uri {ECO:0000312|FlyBase:FBgn0035025};
GN Synonyms=ori {ECO:0000312|FlyBase:FBgn0035025};
GN ORFNames=CG11416 {ECO:0000312|FlyBase:FBgn0035025};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL39712.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39712.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39712.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:AAV36993.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAV36993.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAV36993.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FLW AND PP1-87B, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18412953; DOI=10.1186/1471-2199-9-36;
RA Kirchner J., Vissi E., Gross S., Szoor B., Rudenko A., Alphey L.,
RA White-Cooper H.;
RT "Drosophila Uri, a PP1alpha binding protein, is essential for viability,
RT maintenance of DNA integrity and normal transcriptional activity.";
RL BMC Mol. Biol. 9:36-36(2008).
CC -!- FUNCTION: Inhibits the activity of serine/threonine-protein
CC phosphatases flw/PP1beta9C and Pp1-87B. Required for germ line cell
CC viability and differentiation, normal transcriptional activity and
CC maintenance of DNA integrity. {ECO:0000269|PubMed:18412953}.
CC -!- SUBUNIT: Interacts with serine/threonine-protein phosphatases
CC flw/PP1beta9C and Pp1-87B with higher affinity for Pp1-87B.
CC {ECO:0000269|PubMed:18412953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18412953}.
CC Chromosome {ECO:0000269|PubMed:18412953}. Nucleus
CC {ECO:0000269|PubMed:18412953}. Note=In primary spermatocytes and
CC maturing spermatids, found throughout the cytoplasm with a distinctive
CC concentration in speckles. In the embryo, primarily cytoplasmic with
CC some protein in speckles in both the nucleus and cytoplasm. In salivary
CC glands, predominantly cytoplasmic with a mild perinuclear accumulation.
CC Also detected on salivary gland polytene chromosomes where it is
CC associated with regions of active transcription.
CC {ECO:0000269|PubMed:18412953}.
CC -!- DEVELOPMENTAL STAGE: Most abundant in early embryo, pupa and adult
CC gonads (at protein level). In testis, expressed in mitotically
CC proliferating spermatogonia and early primary spermatocytes with levels
CC decreasing as spermatocytes mature and no expression in postmitotic
CC stages. {ECO:0000269|PubMed:18412953}.
CC -!- DISRUPTION PHENOTYPE: Embryos hatch normally but first instar larvae
CC show very little locomotion or feeding and die soon after hatching.
CC Embryos show transcriptional defects with reduced expression of ebony
CC and Ass. Somatically-rescued mutant larvae show defective germ line
CC cell viability and differentiation with damaged DNA.
CC {ECO:0000269|PubMed:18412953}.
CC -!- SIMILARITY: Belongs to the RNA polymerase II subunit 5-mediating
CC protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39712.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF47229.1; -; Genomic_DNA.
DR EMBL; AY069567; AAL39712.1; ALT_FRAME; mRNA.
DR EMBL; BT016108; AAV36993.1; -; mRNA.
DR RefSeq; NP_611933.1; NM_138089.4.
DR AlphaFoldDB; Q9W148; -.
DR SMR; Q9W148; -.
DR IntAct; Q9W148; 1.
DR STRING; 7227.FBpp0072215; -.
DR PaxDb; Q9W148; -.
DR PRIDE; Q9W148; -.
DR EnsemblMetazoa; FBtr0072308; FBpp0072215; FBgn0035025.
DR GeneID; 37924; -.
DR KEGG; dme:Dmel_CG11416; -.
DR UCSC; CG11416-RA; d. melanogaster.
DR CTD; 37924; -.
DR FlyBase; FBgn0035025; uri.
DR VEuPathDB; VectorBase:FBgn0035025; -.
DR eggNOG; KOG3130; Eukaryota.
DR GeneTree; ENSGT00390000002362; -.
DR HOGENOM; CLU_025757_0_0_1; -.
DR InParanoid; Q9W148; -.
DR OMA; GHYQGYF; -.
DR OrthoDB; 811607at2759; -.
DR PhylomeDB; Q9W148; -.
DR BioGRID-ORCS; 37924; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37924; -.
DR PRO; PR:Q9W148; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0035025; Expressed in egg cell and 25 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0019212; F:phosphatase inhibitor activity; IDA:FlyBase.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:FlyBase.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR Pfam; PF02996; Prefoldin; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Cytoplasm; Nucleus; Protein phosphatase inhibitor;
KW Reference proteome.
FT CHAIN 1..731
FT /note="Unconventional prefoldin RPB5 interactor-like
FT protein"
FT /id="PRO_0000436525"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..115
FT /evidence="ECO:0000255"
FT COILED 143..176
FT /evidence="ECO:0000255"
FT COILED 220..258
FT /evidence="ECO:0000255"
FT COILED 357..379
FT /evidence="ECO:0000255"
FT COILED 452..477
FT /evidence="ECO:0000255"
FT COMPBIAS 259..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 83924 MW; D924359687FCB1A4 CRC64;
MDRREDALLQ ALQTNASETE RWEAFKRDNE STIRNLDKFA KNLSVEVMVP IGRKALMPGE
LIHTNELLVG HYEGYFSACS SHKAKEICQY RLKLAEEQLK KLAVENDLWQ KKLHTPFAEG
AVPSGDQVEI VEDFNEESHN KWLAEHRKRM RQQKQKERLE REAEPVKKDN EVLRKLEERE
MMEELGLDPD NIDEDQLHDM LNQEPLKSTN ESSPKSLTQE EEDELWKKLE AEEQNEADEL
SSEAEESLKT TDNLVRQLMS GETETPSSKK RTAGTNRNVE IQDPISEDDG DDDDEGDQEE
EVRTIREQMS LLPNEDREPF LRAQLHVLKA KMRKIQKVNF ISDELIHLMN VVVMLEDDLQ
DLVFEQELEA SEEEEEVVEN NHLPDEPSKE LSTVSESSTN KRRISFALDD EKLEFRREET
VAEMLPNAKK NSRDIIKLNA PLKPAGDPQP ASIKTKRQTT QDILQKVERN IEFVKENQSV
QDFDLLNRIM EESTGLINTL HISFTHSGAI PSPSSDQSDG IPGKPSDFYV RYEKDRARPN
DSFPIYVNGF EGEEHVKVPI MSEAARGSAY EDPRSQFSKP NSSEICFTHS GSITPTSNDQ
SDDIPGNPFD FYEKYEKDRA KFSKSNSSEG DATDPESATK SILRNKSAVD LEPHNVNQQP
KKGRKVRNQK KKERTLDDDL RDMSAYQKVM HDLVEKEPTA PEPLPPGKFI DSHAPKKRVS
RFKEQRALNK T
