PESC_RAT
ID PESC_RAT Reviewed; 586 AA.
AC Q3B8N8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN Name=Pes1;
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=Thymus;
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 PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12. The complex is held together by BOP1, which interacts with PES1
CC via its N-terminal domain and with WDR12 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The PeBoW complex associates with the 66S pre-ribosome. The
CC PeBoW complex also associates with DDX27, PES1 interacts directly with
CC DDX27. Interacts with IRS1 and UBTF. May interact with MAP1B.
CC {ECO:0000255|HAMAP-Rule:MF_03028}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03028}.
CC Chromosome {ECO:0000255|HAMAP-Rule:MF_03028}. Note=Appears to localize
CC to the periphery of metaphase chromosomes during mitosis and to the
CC prenucleolar bodies that form in mitotic cells prior to the actual
CC nucleoli.
CC -!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC Rule:MF_03028}.
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DR EMBL; BC105910; AAI05911.1; -; mRNA.
DR RefSeq; NP_001037693.1; NM_001044228.1.
DR AlphaFoldDB; Q3B8N8; -.
DR SMR; Q3B8N8; -.
DR STRING; 10116.ENSRNOP00000005996; -.
DR iPTMnet; Q3B8N8; -.
DR PhosphoSitePlus; Q3B8N8; -.
DR jPOST; Q3B8N8; -.
DR PaxDb; Q3B8N8; -.
DR PRIDE; Q3B8N8; -.
DR Ensembl; ENSRNOT00000005996; ENSRNOP00000005996; ENSRNOG00000004515.
DR GeneID; 289740; -.
DR KEGG; rno:289740; -.
DR UCSC; RGD:1559814; rat.
DR CTD; 23481; -.
DR RGD; 1559814; Pes1.
DR eggNOG; KOG2481; Eukaryota.
DR GeneTree; ENSGT00390000002626; -.
DR HOGENOM; CLU_019619_0_0_1; -.
DR InParanoid; Q3B8N8; -.
DR OMA; TWIVPHY; -.
DR OrthoDB; 777920at2759; -.
DR PhylomeDB; Q3B8N8; -.
DR TreeFam; TF300671; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q3B8N8; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000004515; Expressed in spleen and 20 other tissues.
DR Genevisible; Q3B8N8; RN.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0007000; P:nucleolus organization; ISO:RGD.
DR GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; ISO:RGD.
DR Gene3D; 3.40.50.10190; -; 1.
DR HAMAP; MF_03028; Pescadillo; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR010613; PES.
DR PANTHER; PTHR12221; PTHR12221; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF06732; Pescadillo_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Isopeptide bond; Nucleus; Reference proteome;
KW Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT CHAIN 1..586
FT /note="Pescadillo homolog"
FT /id="PRO_0000370445"
FT DOMAIN 321..414
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 1..257
FT /note="Sufficient for nucleolar localization"
FT /evidence="ECO:0000250"
FT REGION 1..54
FT /note="Required for 28S ribosomal RNA processing"
FT /evidence="ECO:0000250"
FT REGION 305..414
FT /note="Sufficient for interaction with MAP1B"
FT /evidence="ECO:0000250"
FT REGION 447..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..586
FT /note="Required for 28S ribosomal RNA processing"
FT /evidence="ECO:0000250"
FT REGION 562..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00541"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O00541"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O00541"
SQ SEQUENCE 586 AA; 67604 MW; D747C6EB67D0F6D2 CRC64;
MGGLEKKKYE RGSATNYITR NKARKKLQLS LPDFRRLCIL KGIYPHEPKH KKKVNKGSTA
ARTFYLIKDI KFLLHEPIVN KFREYKVFVR KLRKAYGKSE WNAVERLKDN KPSYKLDHIV
KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFMH YVIAARALRK
VFLSIKGIYY QAEVLGQPIV WIAPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ
SLNLHYPPKI ESQAQAEMKV SEDTYALDSE SSMEKLAALS ASLARVVVPA VEEAEADEFP
TDGEVTAQEE DRRKELEAQE KHKKLFEGLK FFLNREVPRE ALAFIIRSFG GDVSWDKSLC
IGATYDSTDS GITHQIVDRP GQQTPIIGRY YVQPQWVFDC VNARLLLPVA EYFPGVQLPP
HLSPFVSEKE GDYIPPEKLK LLALQRGEDP GNLEEEEEDE DDEGDDSEGD GDVAVENEEE
VVEAESEEEE EAHLSALEQQ RLGGKKPQVM AGTVKLEDRQ RLAQEEESEA KRLAIMMMKK
REKYLYQKIM FGKRRKIREA NKLAEKRKAH DDAVRSEKKA KRTRPV
