ID A0A3Q7SIU3_VULVU Unreviewed; 581 AA.
AC A0A3Q7SIU3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Pescadillo homolog {ECO:0000256|HAMAP-Rule:MF_03028};
GN Name=LOC112924914 {ECO:0000313|RefSeq:XP_025861319.1};
GN Synonyms=PES1 {ECO:0000256|HAMAP-Rule:MF_03028};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025861319.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025861319.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025861319.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025861319.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03028}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and
CC WDR12. The PeBoW complex also associates with the 66S pre-ribosome.
CC Interacts with IRS1 and UBTF. May interact with MAP1B.
CC {ECO:0000256|HAMAP-Rule:MF_03028}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03028}.
CC Chromosome {ECO:0000256|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. {ECO:0000256|HAMAP-Rule:MF_03028}.
CC -!- PTM: Sumoylated. {ECO:0000256|HAMAP-Rule:MF_03028}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000256|HAMAP-
CC Rule:MF_03028}.
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DR RefSeq; XP_025861319.1; XM_026005534.1.
DR AlphaFoldDB; A0A3Q7SIU3; -.
DR STRING; 9627.ENSVVUP00000042180; -.
DR KEGG; vvp:112924914; -.
DR OrthoDB; 169151at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
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); IEA:UniProtKB-UniRule.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Chromosome {ECO:0000256|HAMAP-Rule:MF_03028};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_03028};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03028};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_03028};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_03028}; Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_03028}.
FT DOMAIN 321..414
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 448..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..538
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03028"
FT COMPBIAS 454..481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 67236 MW; 7199B9CBECB91527 CRC64;
MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRPCIL KAIYPHEPKH KKKVNKGSTA
ARTFYLLKDI KFLLHEPIVN KFQEYKVFVR KLRKAYGKSE WNTVERLKDN KPNYKLDHIV
KERYPTFVDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFLH YVIAARALRK
VFLSIKGIYY QAEVLGQPIV WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGLVNFRLYQ
SLNLHYPPKL EGQAQTEAKT SEDTYALDSE SSMEKLAALG ASLARMVVPV EEEAEMDEFP
ADGEMTVQEE DRRKELEAQE KQKKLFEGLK FFLNREVPRE ALAFVIRSFG GDVSWDKSLC
IGATYDVTDP CVTHQIVDRP GQQTPVIGRY YVQPQWVFDC VNARLLLPVA DYFPGVQLPP
HLSPFVSEKE GDYIPLEKLK LLALQRGEHP GNTDESEEED DDGDEGGENE EEEEEDAEAG
SEKEEEAHLT ALEEQRMEEK KPQVMAGTVK LQDKQRLAQE EENEAKRLAI MMMKKREKYL
YNKIMFGKRR KIQEANKLAE KQKAHDEAVR SQKKAKRIRP V
//
