UTP25_MOUSE
ID UTP25_MOUSE Reviewed; 772 AA.
AC Q8BTT6; Q8BWJ1; Q8VEC2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=U3 small nucleolar RNA-associated protein 25 homolog;
DE AltName: Full=Digestive organ expansion factor homolog;
DE AltName: Full=UTP25 small subunit processor component;
GN Name=Utp25 {ECO:0000312|MGI:MGI:2138080}; Synonyms=Def, Diexf;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=29262616; DOI=10.18632/oncotarget.22087;
RA Aryal N.K., Wasylishen A.R., Pant V., Riley-Croce M., Lozano G.;
RT "Loss of digestive organ expansion factor (Diexf) reveals an essential role
RT during murine embryonic development that is independent of p53.";
RL Oncotarget 8:103996-104006(2017).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=32303961; DOI=10.1007/s11427-019-1635-2;
RA Huang W., Chen F., Ma Q., Xin J., Li J., Chen J., Zhou B., Chen M., Li J.,
RA Peng J.;
RT "Ribosome biogenesis gene DEF/UTP25 is essential for liver homeostasis and
RT regeneration.";
RL Sci. China Life Sci. 63:1651-1664(2020).
CC -!- FUNCTION: Component of the ribosomal small subunit processome for the
CC biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA)
CC processing (By similarity). Essential for embryonic development in part
CC through the regulation of p53 pathway. Controls the expansion growth of
CC digestive organs and liver (PubMed:29262616, PubMed:32303961). Also
CC involved in the sympathetic neuronal development (By similarity).
CC Mediates, with CAPN3, the proteasome-independent degradation of
CC p53/TP53 (By similarity). {ECO:0000250|UniProtKB:Q68CQ4,
CC ECO:0000250|UniProtKB:Q6PEH4, ECO:0000269|PubMed:29262616,
CC ECO:0000269|PubMed:32303961}.
CC -!- SUBUNIT: Interacts with CAPN3; the interaction is required for CAPN3
CC translocation to the nucleolus. {ECO:0000250|UniProtKB:Q68CQ4}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q68CQ4}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested: brain, small
CC intestine, large intestine, stomach, liver, spleen, thymus, lung,
CC kidney and testes (at protein level). {ECO:0000269|PubMed:29262616}.
CC -!- PTM: Phosphorylated. Phosphorylation is required to promote p53/TP53
CC degradation in the nucleolus which promotes cell cycle progression and
CC liver development. {ECO:0000250|UniProtKB:Q68CQ4}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos are peri-implantation lethal at
CC E4.5-E5.5 stages (PubMed:29262616, PubMed:32303961). Conditional
CC knockouts in hepatocytes do not show overall differences in liver
CC growth but suffer from liver chronic inflammation (PubMed:32303961).
CC Hepatocytes show nuclei enlargement with nuclear vacuolization
CC (PubMed:32303961). Animals have bile duct hyperplasia and polycystic
CC liver (PubMed:32303961). Males die suddenly after hepatectomy due to
CC overactive inflammatory response (PubMed:32303961).
CC {ECO:0000269|PubMed:29262616, ECO:0000269|PubMed:32303961}.
CC -!- SIMILARITY: Belongs to the UTP25 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK052355; BAC34954.1; -; mRNA.
DR EMBL; AK088756; BAC40549.1; -; mRNA.
DR EMBL; BC019218; AAH19218.1; -; mRNA.
DR RefSeq; NP_663390.2; NM_145415.2.
DR AlphaFoldDB; Q8BTT6; -.
DR BioGRID; 229602; 25.
DR IntAct; Q8BTT6; 1.
DR MINT; Q8BTT6; -.
DR STRING; 10090.ENSMUSP00000082691; -.
DR iPTMnet; Q8BTT6; -.
DR PhosphoSitePlus; Q8BTT6; -.
DR EPD; Q8BTT6; -.
DR jPOST; Q8BTT6; -.
DR MaxQB; Q8BTT6; -.
DR PaxDb; Q8BTT6; -.
DR PeptideAtlas; Q8BTT6; -.
DR PRIDE; Q8BTT6; -.
DR ProteomicsDB; 279868; -.
DR GeneID; 215193; -.
DR KEGG; mmu:215193; -.
DR UCSC; uc007edw.1; mouse.
DR CTD; 27042; -.
DR MGI; MGI:2138080; Utp25.
DR eggNOG; KOG2340; Eukaryota.
DR InParanoid; Q8BTT6; -.
DR OrthoDB; 257318at2759; -.
DR PhylomeDB; Q8BTT6; -.
DR TreeFam; TF105930; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 215193; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Diexf; mouse.
DR PRO; PR:Q8BTT6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BTT6; protein.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; ISS:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010678; UTP25.
DR PANTHER; PTHR12933; PTHR12933; 1.
DR Pfam; PF06862; UTP25; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..772
FT /note="U3 small nucleolar RNA-associated protein 25
FT homolog"
FT /id="PRO_0000254150"
FT REGION 1..201
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..651
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 652..713
FT /note="Represses p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT COMPBIAS 19..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CQ4"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT CONFLICT 84..94
FT /note="Missing (in Ref. 2; AAH19218)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..87
FT /note="Missing (in Ref. 1; BAC34954)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="V -> A (in Ref. 1; BAC40549)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> M (in Ref. 2; AAH19218)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="L -> S (in Ref. 2; AAH19218)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> P (in Ref. 2; AAH19218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 88818 MW; 79BA30E31B757CF3 CRC64;
MGKRRNRGRS QMLSTMTKKQ KKHLRDFGEE HPFYDRVSKK EAKPQICQLP ESSDSSHSES
ESESEQEHVS GYHRLLATLK NVSEEEEEEE EEEEEEEEEE EEEEEEEEDD SAVGDAEMNE
EAGSEDGSVG EAAVSEAAEE AAETQEHMSL ADNSKEKDGE EPPGVSQKSS EEFTDVKHES
LFSLETNFLE EDSGGSCSQR PSQDPFQQHV NKELKEKEIQ AAASSPPATQ QLKWPVLGHL
VFSSKFQKTE TFKPPKDIDL KLLHLQKPLE STWAKTNSQF LSGPQKSNSS FTPLQKELFL
IMNSYRDLFY PERTALKNGE EVRHVYCLHA INHVLKANAQ VLANNSRRRS QKLGVGEDDD
FRDQGLTRPK VLIVVPFREA ALRVVQLFIS LLEGDSKKKI IVSNKKRFQG EYGSDPEERP
PNLKRPEDYE AVFVGNIDDH FRIGVAILQR SIRLYAPFYS SDILIASPLG LRTIIGGEGE
KKRDFDFLSS VELLIIDQAD IYLMQNWEHV LHLMNHMNLL PLDSHGVDFS RVRMWSLNNW
SKYYRQTLLF GALQDAQINS VFNKHCINAQ GQVAVRNVPM TGSISHVLVQ LPHVFQRMEA
QDLSSVIDAR FHFFINKILP QYRDAVMSHT LIYVPSYFDF VRLRNYFKKE ELNFTHICEY
TQKSGISRAR HFFLQGEKQF LLLTERFHFY KRYTIKGIRN LIFYELPTYP HFYSEVCNML
RATSRGEEAT WTCTVLYSKY DAQRLAAVVG VERAAQMLQS PKNVHLFVTG EK