ID PESC_XENLA Reviewed; 574 AA.
AC Q7ZY69;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN Name=pes1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17727835; DOI=10.1016/j.ydbio.2007.07.037;
RA Gessert S., Maurus D., Roessner A., Kuehl M.;
RT "Pescadillo is required for Xenopus laevis eye development and neural crest
RT migration.";
RL Dev. Biol. 310:99-112(2007).
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 (By similarity). Required for neural crest migration and eye
CC development. {ECO:0000255|HAMAP-Rule:MF_03028,
CC ECO:0000269|PubMed:17727835}.
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.
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 -!- DEVELOPMENTAL STAGE: Maternally expressed. Strongly expressed in the
CC anterior neural plate at stage 18. Expressed in the migrating cranial
CC neural crest and the developing eye at stage 23. Also expressed in the
CC midbrain-hindbrain boundary, migrating neural crest cells and the
CC periocular mesenchyme at stages 26-31. Expression appears to require
CC Wnt-4 activity. {ECO:0000269|PubMed:17727835}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC Rule:MF_03028}.
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DR EMBL; BC043950; AAH43950.1; -; mRNA.
DR RefSeq; NP_001080557.1; NM_001087088.1.
DR AlphaFoldDB; Q7ZY69; -.
DR SMR; Q7ZY69; -.
DR DNASU; 380249; -.
DR GeneID; 380249; -.
DR KEGG; xla:380249; -.
DR AGR; Xenbase:XB-GENE-480674; -.
DR CTD; 380249; -.
DR Xenbase; XB-GENE-480674; pes1.S.
DR OrthoDB; 169151at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 380249; Expressed in pancreas and 19 other cell types or tissues.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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: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:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR CDD; cd17709; BRCT_pescadillo_like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 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; PESCADILLO - RELATED; 1.
DR PANTHER; PTHR12221:SF6; PESCADILLO HOMOLOG; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF06732; Pescadillo_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..574
FT /note="Pescadillo homolog"
FT /id="PRO_0000370447"
FT DOMAIN 323..416
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..478
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 67117 MW; 3886A2DA331619BF CRC64;
MGGLEKKKYE RGSATNYITR NKARKKLQLS LPDFRRLCIL KGIYPHEPKH KKKVNKGSTA
PRTFYLLKDI KFLLHEPIVG KFREYKVFVR RLRKAYGKRE WDSVDRIRDN KPSYKLDHII
KERYPTFIDA VRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLSVEFLN YVIDSRSLRK
VFLSIKGIYY QADILGQTLT WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFHLYQ
TLNLQYPPKL DSFSEVDLKS DGEDKYALET EVYMEKLAAL SASLSRVIPS EPNDDTEVDE
FPADPENAGL EEEQKRQLQE EEKHKSLFVG LKFFLNREVP RDALAFIIRS FGGEVSWDAS
VCIGATYNST DPSITHHIVD RPSIQTQIIN RYYLQPQWVF DCVNARLLLP VEDYFPGVLL
PPHLSPFVHE KEGDYIPPEK LRLMAMQKGE NLGLDEEDDD DDDDDEEEDD DDDEEEEDKK
LRQLENKKVG QKNLNVKVTA GKVKVEDRTQ VAEQEKNEEK RLAIMMMKKK EKYLYNKIMF
GKKRKVREAN KLALKRKAHD EAVKVERKKK AKKH
//
