UTP25_RAT
ID UTP25_RAT Reviewed; 763 AA.
AC Q5M9G7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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|RGD:1359148}; Synonyms=Def, Diexf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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 (By similarity). Also involved in the
CC sympathetic neuronal development (By similarity). Mediates, with CAPN3,
CC the proteasome-independent degradation of p53/TP53 (By similarity).
CC {ECO:0000250|UniProtKB:Q68CQ4, ECO:0000250|UniProtKB:Q6PEH4}.
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 -!- 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 -!- SIMILARITY: Belongs to the UTP25 family. {ECO:0000305}.
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DR EMBL; BC087114; AAH87114.1; -; mRNA.
DR RefSeq; NP_001014008.1; NM_001013986.2.
DR AlphaFoldDB; Q5M9G7; -.
DR STRING; 10116.ENSRNOP00000006395; -.
DR PaxDb; Q5M9G7; -.
DR PRIDE; Q5M9G7; -.
DR Ensembl; ENSRNOT00000006395; ENSRNOP00000006395; ENSRNOG00000004789.
DR GeneID; 305076; -.
DR KEGG; rno:305076; -.
DR CTD; 27042; -.
DR RGD; 1359148; Utp25.
DR eggNOG; KOG2340; Eukaryota.
DR GeneTree; ENSGT00390000000709; -.
DR HOGENOM; CLU_018705_1_1_1; -.
DR InParanoid; Q5M9G7; -.
DR OMA; KYFRQTI; -.
DR OrthoDB; 257318at2759; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q5M9G7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004789; Expressed in spleen and 19 other tissues.
DR Genevisible; Q5M9G7; RN.
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; ISS: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 2: Evidence at transcript level;
KW Developmental protein; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..763
FT /note="U3 small nucleolar RNA-associated protein 25
FT homolog"
FT /id="PRO_0000254151"
FT REGION 1..190
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..642
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 643..704
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..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..164
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"
SQ SEQUENCE 763 AA; 87825 MW; 5E00F6DE232C2010 CRC64;
MGKRRSRGRS QLLSTMTKKQ KKHLRDFGEE HPFYDRVSKK EVKPQICQLS ESSDSSHSES
ESESEQEHVS GYHRLLATLK NISEEEEEEE EEEEEEEEDK EEVDDSAVGD SEMNGEDGGE
DVRVEETAES SETQDHMSLA DNSKGKDGEE PPGVSQKSSE EFTDVKHESL FSLETNFLEE
ESGGSYSQRT SQDPFQHHIN KELQEKEIQA AASSPAATQQ LKWPVLGHLV FSSKFQKMET
FKPPKDIDLK SLHLQKPLES TWAKTNSQFL SGPGPQKSSS CFTPLQKELF LIMNSYRDLF
YPERTALKNG EEVRHVYCLH AINHVLKANA QVLANNSRRR TQKLGVGDDD DFRDQGLTRP
KVLIVVPFRE AALRVVQLFI SLLEGDSKKK IIVSNKKRFQ GEYGSDPEER PPNLKRPEDY
EAVFVGNIDD HFRIGVAILQ RSIRLYAPFY SSDILIASPL GLRTIIGGEG EKKRDFDFLS
SIELLIIDQA DIYLMQNWEH VLHLMNHMNL LPLDSHGVNF SRVRMWSLNN WSKYYRQTLL
FGALQDAQIN SVFNKHCVNA QGQVAVRNVP MTGSISHVLV QLPHVFQRME AQDLASVIDA
RFHFFINKIL PQYRDAVMSH TLIYVPSYFD FVRLRNYFKK EELNFTHICE YTQRSGVSRA
RHFFLQGEKQ FLLLTERFHF YKRYTIKGIR NLIFYELPTY AHFYSEVCNM LRATSRGEEA
TWTCTVLYSK YDAQRLAAVV GVERAAQMLQ SPKSVHLFIT GEK
