RMP_BOVIN
ID RMP_BOVIN Reviewed; 524 AA.
AC Q3B7M7; A7E3X6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Unconventional prefoldin RPB5 interactor;
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=PPP1R19, RMP, URI;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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. Cytoplasm. Mitochondrion. Cell
CC projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2, PFDN4,
CC PPP1CC, RPS6KB1 and STAP1 in mitochondrion. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs essentially on serine
CC residues. 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-361 by RPS6KB1 in a growth factor- and
CC rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation
CC at Ser-361 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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase II subunit 5-mediating
CC protein family. {ECO:0000305}.
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DR EMBL; BT030747; ABS45063.1; -; mRNA.
DR EMBL; BC107540; AAI07541.1; -; mRNA.
DR RefSeq; NP_001030382.1; NM_001035305.2.
DR AlphaFoldDB; Q3B7M7; -.
DR SMR; Q3B7M7; -.
DR STRING; 9913.ENSBTAP00000009950; -.
DR PaxDb; Q3B7M7; -.
DR PRIDE; Q3B7M7; -.
DR GeneID; 515119; -.
DR KEGG; bta:515119; -.
DR CTD; 8725; -.
DR eggNOG; KOG3130; Eukaryota.
DR InParanoid; Q3B7M7; -.
DR OrthoDB; 964566at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR Pfam; PF02996; Prefoldin; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Mitochondrion; Nucleus; Oncogene;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..524
FT /note="Unconventional prefoldin RPB5 interactor"
FT /id="PRO_0000328597"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:O94763"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94763"
FT CONFLICT 123
FT /note="L -> F (in Ref. 1; ABS45063)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="I -> V (in Ref. 1; ABS45063)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="G -> D (in Ref. 1; ABS45063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 58994 MW; DF7BB113242A2F85 CRC64;
MEAPPDPRPH ASAAAPLRAP EVARLREEQE KVVTNCQEKI QHWKKVDNDY NALQERLSTL
PDKLSYNIMV PFGPFAFMPG KLVHTNEVTV LLGDNWFAKC SAKQAVGLVE HRKEHVRKTI
DDLKKVMKNF ESRVEFTEDL QKMSDAAGDI VDIREEIKTD FEFKAKHRIA HKPHSKPKTS
DIFEAEFAND LKSKDLLADK ELWDRLEELE RQEELLGEID IDSKPDTVIA NGEDVSSEEE
KEDQNINVNM MHQVTDSLAL SSCYNSLTNS ELFNGQVNSP LNYSVNGSSS YHSNEDDGDN
NDDGGDSEND HDTLGVEDNS IPTIYFSHTV EPKRVRINTG KNTTLKFSEK KEEAKRKRKN
SSGSGHSPQE LPMIRTPADI YRVFVDVVNG EYVPRKSILK SRSRENSVCS DTSESSAADF
DDRRGVLRSI SCEEATCSDA SESILEEEQE NHQKKLLPLS VTPEAFSGTV IEKEFLSPSL
TPHPAMAHPV LPTIPERKEV LSEVSEGTTK RVSKFKAARL QQKN
