UTP25_CHICK
ID UTP25_CHICK Reviewed; 772 AA.
AC Q5ZLG3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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; ORFNames=RCJMB04_6f17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719771; CAG31430.1; -; mRNA.
DR RefSeq; NP_001026222.1; NM_001031051.1.
DR AlphaFoldDB; Q5ZLG3; -.
DR STRING; 9031.ENSGALP00000016054; -.
DR PaxDb; Q5ZLG3; -.
DR GeneID; 421384; -.
DR KEGG; gga:421384; -.
DR CTD; 421384; -.
DR VEuPathDB; HostDB:geneid_421384; -.
DR eggNOG; KOG2340; Eukaryota.
DR InParanoid; Q5ZLG3; -.
DR OrthoDB; 257318at2759; -.
DR PhylomeDB; Q5ZLG3; -.
DR PRO; PR:Q5ZLG3; -.
DR Proteomes; UP000000539; Unplaced.
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..772
FT /note="U3 small nucleolar RNA-associated protein 25
FT homolog"
FT /id="PRO_0000254152"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..200
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 588..650
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 651..712
FT /note="Represses p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
SQ SEQUENCE 772 AA; 88950 MW; 11A18A4E8B795C17 CRC64;
MGKRRGGREL ARGLSKRQRK HLRQFGEQHP VCDRVSGRPE ATQICELSDN SDKSSAESDS
ETEVEQVSVY HKLLATLKAS PESESEEEED ESESEEAGES EAELDSEGSQ EPKEAVGGEE
EQNDVPEQEE EVAAKDPPEQ AFGQEEADGV ETSCDPNRGA IEEFTDVKHE AEFSLETNFM
EEESGDCDAD KRESNSSQAF SEDPFKQHMD KELEEKEVEK ISTLSKTSSQ SKWPRLGQLT
FSSTLEKHTT LKPDKEFSVK QLYLHKPLES TWPKVNKHYL SSASKPSDSF FTPLQRELFC
IMNTYRDLFY PERNALTNGE EIRHAYCLHA LNHILKANAQ VLSNNAKKRD QKPGTDSDDY
RDQGLTRPKV LMIVPFRECA LRIVHIFISL LEVNEKRKID VSNKKRFKGE FGSDPDEKPP
NLKRPEDYEA VFAGNIDDHF RIGVAILQKS MRLYAPFYSS DIIIASPLGM RTIIGTEGEK
KRDFDFLSSI EMLIIDQADI YLMQNWEHVL HLMRHINLLP LDSHGVDFSR VRMPNLNNWS
KYYRQTLLFS ALQDPQINAI FNKHCFNYVG QVAVRNVPLS GSISRVVVQL PHVFRRIEAE
NLTSVIDTRF QFFIDKVLPE YRDAIMSHTL IYVPSYFDYV RLRNYFKKEE LNFTHICEYT
KKAGICRARR SFLKGEKQFL LLTERFHFYK RYTIKGIRNL IFYELPTYSH FYSEICNMMK
ATDSGVDATW TCTVLYSKYD AQKLAAVVGI DRTAQMLQSK KNVHLFVTGE NE
