UTP25_XENTR
ID UTP25_XENTR Reviewed; 765 AA.
AC Q642T7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
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; Synonyms=def, diexf;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC080917; AAH80917.1; -; mRNA.
DR RefSeq; NP_001008035.1; NM_001008034.1.
DR AlphaFoldDB; Q642T7; -.
DR STRING; 8364.ENSXETP00000000454; -.
DR GeneID; 493397; -.
DR KEGG; xtr:493397; -.
DR CTD; 27042; -.
DR Xenbase; XB-GENE-1002187; utp25.
DR InParanoid; Q642T7; -.
DR OrthoDB; 257318at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000216; Expressed in gastrula and 12 other tissues.
DR ExpressionAtlas; Q642T7; differential.
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:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR GO; GO:0048568; P:embryonic organ development; ISS:UniProtKB.
DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
DR GO; GO:0090594; P:inflammatory response to wounding; IEA:Ensembl.
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:0035265; P:organ growth; IEA:Ensembl.
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 GO; GO:0048485; P:sympathetic nervous system development; IEA:Ensembl.
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..765
FT /note="U3 small nucleolar RNA-associated protein 25
FT homolog"
FT /id="PRO_0000254154"
FT REGION 1..198
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..643
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 644..705
FT /note="Represses p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
SQ SEQUENCE 765 AA; 88101 MW; F143F8704BDC1375 CRC64;
MGKRRKPRRE EAGSALSKKQ KKHLKEFGEQ HPFYDAVSKK QETTQVVQLP ESSEDESRSE
SEAESDPEPV NMYHKLLATL NTVSDEEEEE SDDEEEEALE EAEEEDEAEE VGEESEAEDE
DNEDESDGEG HGQMDELPVE AEKAGDNEEE ERAGDPAAEE AGEFTDAKHE SKFSLETNFM
DEDNEDSKDE SVPCPTVATE DPFVQHVGRE LEEQDISKIG TNPKKASLKW PALGQLGVSS
SLPQLQPLKV EKETDLQKLY LHKPLFSTWP KVNSPFLSVD KEQNFTPLQR ELFSIMNSYR
DLFFPARSPT AQGEEIRHVY CLHALNHVLK ANAQVLNNNS QKRDQKPGLD EEDLRDQGLT
RPKVLIVVPF RESALRIVQI LISLMEVGGR KVDVSNKKRF KEEFGSEPED RPPNLKRPED
YEAVFAGNID DHFRIGVAIL QKSMRLYSPF YSSDIIIASP VGLRTIIGSE GEKKRDFDFL
SSIEVLILDQ ADLYLMQNWE HVLHLMAHLN LQPTDSHGVD FSRVRMWNLS NWAKYYRQTL
LFSSLQEPQI NSIFNKHCFN YCGQVAVRNM PVTGSISHVV VQLPHVFQRL EADSLLTVID
ARFEFFTSKI LPQYRDAIMS HTLIYIPSYF DYVRLRNYFK KEELNFTHIC EYTNRSGVSR
ARQFFLKGER QFLLVTERFH FYKRYTLKGI RNLIFYELPT YPHFYSEVCN MMKAWHRGEE
ATWTCTVLYS KYDAQRLAAV VGAERAAQML QSKKNVHLFV TGENG
