RMP_MOUSE
ID RMP_MOUSE Reviewed; 531 AA.
AC Q3TLD5; Q3V078; Q8R5C4; Q9Z243;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Unconventional prefoldin RPB5 interactor;
DE AltName: Full=Protein NNX3;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 19;
DE AltName: Full=RNA polymerase II subunit 5-mediating protein;
DE Short=RPB5-mediating protein;
GN Name=Uri1; Synonyms=Nnx3, Ppp1r19, Rmp, Uri;
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] (ISOFORM 2), PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9878255; DOI=10.1006/geno.1998.5609;
RA Van Leuven F., Torrekens S., Moechars D., Hilliker C., Buellens M.,
RA Bollen M., Delabie J.;
RT "Molecular cloning of a gene on chromosome 19q12 coding for a novel
RT intracellular protein: analysis of expression in human and mouse tissues
RT and in human tumor cells, particularly Reed-Sternberg cells in Hodgkin
RT disease.";
RL Genomics 54:511-520(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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: Involved in gene transcription regulation. Acts as a
CC transcriptional repressor in concert with the corepressor UXT to
CC regulate androgen receptor (AR) transcription. May act as a tumor
CC suppressor to repress AR-mediated gene transcription and to inhibit
CC anchorage-independent growth in prostate cancer cells. Required for
CC cell survival in ovarian cancer cells. Together with UXT, associates
CC with chromatin to the NKX3-1 promoter region (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD
CC phosphorylation under normal growth conditions thereby protecting cells
CC from potential deleterious effects of sustained S6K1 signaling. The
CC URI1-PPP1CC complex acts as a central component of a negative feedback
CC mechanism that counteracts excessive S6K1 survival signaling to BAD in
CC response to growth factors. Mediates inhibition of PPP1CC phosphatase
CC activity in mitochondria. Coordinates the regulation of nutrient-
CC sensitive gene expression availability in a mTOR-dependent manner.
CC Seems to be a scaffolding protein able to assemble a prefoldin-like
CC complex that contains PFDs and proteins with roles in transcription and
CC ubiquitination (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. 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. Interacts with POLR2E/RPB5, RUVBL2 and
CC RUVBL1. Interacts with PFDN2, PFDN4 and STAP1; the interactions are
CC phosphorylation-dependent and occur in a growth-dependent manner in the
CC mitochondrion. Interacts with UXT. Interacts with PPP1CC; the
CC interaction is phosphorylation-dependent and occurs in a growth factor-
CC dependent manner. Interacts (via the middle C-terminal region) with
CC GTF2F1 and GTF2F2. Interacts with DMAP1. Interacts with TSC1 and TSC2.
CC Interacts with PRPF8 and EFTUD2 in a ZNHIT2-dependent manner.
CC {ECO:0000250|UniProtKB:O94763}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9878255}. Cytoplasm
CC {ECO:0000269|PubMed:9878255}. Mitochondrion
CC {ECO:0000269|PubMed:9878255}. Cell projection, dendrite {ECO:0000250}.
CC Note=Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 in
CC mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TLD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TLD5-2; Sequence=VSP_032774;
CC -!- TISSUE SPECIFICITY: Expressed in the spinal cord, ganglia, choroid
CC plexus and olfactors epithelium of the developing brain. Expressed in
CC skin, lung, kidney, testis and muscles (at protein level). Expressed
CC strongly in brain and kidney. Expressed weakly in skeletal muscle, lung
CC and liver. {ECO:0000269|PubMed:9878255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 6 dpc, onward.
CC {ECO:0000269|PubMed:9878255}.
CC -!- PTM: Phosphorylation occurs in response to androgen treatment in
CC prostate cancer cells in a mTOR-dependent manner. Phosphorylated;
CC hyperhosphorylated in mitochondria in a mTORC-dependent signaling
CC pathway. Phosphorylated at Ser-369 by RPS6KB1 in a growth factor- and
CC rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation
CC at Ser-369 disrupts the URI1-PPP1CC complex in the mitochondrion,
CC relieves PPP1CC phosphatase inhibition activity and hence engages a
CC negative feedback diminishing RPS6KB1 kinase activity, preventing
CC sustained S6K1-dependent signaling (By similarity). Phosphorylated.
CC Phosphorylation occurs essentially on serine residues. {ECO:0000250,
CC ECO:0000269|PubMed:9878255}.
CC -!- SIMILARITY: Belongs to the RNA polymerase II subunit 5-mediating
CC protein family. {ECO:0000305}.
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DR EMBL; AF091096; AAD08680.1; -; mRNA.
DR EMBL; AK133383; BAE21626.1; -; mRNA.
DR EMBL; AK166566; BAE38857.1; -; mRNA.
DR EMBL; BC023029; AAH23029.1; -; mRNA.
DR CCDS; CCDS21157.1; -. [Q3TLD5-1]
DR RefSeq; NP_035404.4; NM_011274.5. [Q3TLD5-1]
DR RefSeq; XP_006539741.1; XM_006539678.3. [Q3TLD5-2]
DR AlphaFoldDB; Q3TLD5; -.
DR SMR; Q3TLD5; -.
DR BioGRID; 202902; 7.
DR IntAct; Q3TLD5; 2.
DR MINT; Q3TLD5; -.
DR STRING; 10090.ENSMUSP00000082646; -.
DR iPTMnet; Q3TLD5; -.
DR PhosphoSitePlus; Q3TLD5; -.
DR EPD; Q3TLD5; -.
DR jPOST; Q3TLD5; -.
DR MaxQB; Q3TLD5; -.
DR PaxDb; Q3TLD5; -.
DR PeptideAtlas; Q3TLD5; -.
DR PRIDE; Q3TLD5; -.
DR ProteomicsDB; 300410; -. [Q3TLD5-1]
DR ProteomicsDB; 300411; -. [Q3TLD5-2]
DR Antibodypedia; 28848; 230 antibodies from 32 providers.
DR DNASU; 19777; -.
DR Ensembl; ENSMUST00000085513; ENSMUSP00000082646; ENSMUSG00000030421. [Q3TLD5-1]
DR GeneID; 19777; -.
DR KEGG; mmu:19777; -.
DR UCSC; uc009gkp.2; mouse. [Q3TLD5-1]
DR CTD; 8725; -.
DR MGI; MGI:1342294; Uri1.
DR VEuPathDB; HostDB:ENSMUSG00000030421; -.
DR eggNOG; KOG3130; Eukaryota.
DR GeneTree; ENSGT00390000002362; -.
DR HOGENOM; CLU_029262_0_0_1; -.
DR InParanoid; Q3TLD5; -.
DR OMA; VEKDPMP; -.
DR OrthoDB; 964566at2759; -.
DR PhylomeDB; Q3TLD5; -.
DR TreeFam; TF332816; -.
DR BioGRID-ORCS; 19777; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Uri1; mouse.
DR PRO; PR:Q3TLD5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3TLD5; protein.
DR Bgee; ENSMUSG00000030421; Expressed in optic fissure and 254 other tissues.
DR ExpressionAtlas; Q3TLD5; baseline and differential.
DR Genevisible; Q3TLD5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0019212; F:phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
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 Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Mitochondrion; Nucleus; Oncogene; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..531
FT /note="Unconventional prefoldin RPB5 interactor"
FT /id="PRO_0000328753"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O94763"
FT MOD_RES 369
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000250"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94763"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9878255"
FT /id="VSP_032774"
FT CONFLICT 143
FT /note="T -> A (in Ref. 1; BAE38857)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="N -> D (in Ref. 3; AAH23029)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="E -> D (in Ref. 3; AAH23029)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="D -> E (in Ref. 1; AAD08680)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="R -> H (in Ref. 3; AAH23029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 59084 MW; 47624F5450813693 CRC64;
MEPPSEPEPE PQPLAEASAA APLRAPEVAR LREEQEKVVT NCQEKIQHWE KVDNDYSALQ
ERLRTLPDKL SYDVMVPFGP LAFMPGKLVH TNEVTVLLGD NWFAKCSAKQ AVGLVEHRKE
HVRKTIDDFK KVLKNFESRV EFTEDLQKMS DAAGDFVDIR EEIKSDFEFK GKQRIAHKPH
SKPKTSDIFE ADFENGVKPK NTFDADELWA RLEELERQEE LLGELESKPD TVIANGEDRV
SSEEEKEGAD TGVNVVSPVT DSSAASSCKR RAGNAGLPNG QVNSLNYSVN GSNSYHSNKD
DDEEEEDDDD DDDEDDDNES DHAISADNSI PTIYFSHTVE PKRVRINTGK NTTLKFSEKK
EEAKRKRKSG AGSHATHELP AIKSPADIYR VFVDVVNGEY VPRKSILKSR SRENSVCSDT
SESSAADVED RRGLLRSTSS EEAVATEAGG SSLDELQENH PKKPLPSGVS EAFSGTVIEK
EFLSPSLAPY SAIAHHALPT IPERKEVPSE VSEEPTKRVS KFRAARLQQR S
