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Database: UniProt
Entry: G1SXM3_RABIT
LinkDB: G1SXM3_RABIT
Original site: G1SXM3_RABIT 
ID   G1SXM3_RABIT            Unreviewed;       665 AA.
AC   G1SXM3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Pescadillo homolog {ECO:0000256|HAMAP-Rule:MF_03028};
GN   Name=PES1 {ECO:0000256|HAMAP-Rule:MF_03028,
GN   ECO:0000313|Ensembl:ENSOCUP00000008314.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000008314.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000008314.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000008314.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000008314.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000008314.3};
RG   Ensembl;
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   EMBL; AAGW02067652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02067653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02067654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02067655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1SXM3; -.
DR   Ensembl; ENSOCUT00000009648.4; ENSOCUP00000008314.3; ENSOCUG00000009646.4.
DR   eggNOG; KOG1471; Eukaryota.
DR   GeneTree; ENSGT00390000002626; -.
DR   TreeFam; TF313988; -.
DR   Proteomes; UP000001811; Chromosome 21.
DR   Bgee; ENSOCUG00000009646; Expressed in liver and 15 other cell types or tissues.
DR   ExpressionAtlas; G1SXM3; baseline.
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   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 1.
DR   HAMAP; MF_03028; Pescadillo; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   InterPro; IPR010613; PES.
DR   PANTHER; PTHR12221; PESCADILLO - RELATED; 1.
DR   PANTHER; PTHR12221:SF6; PESCADILLO HOMOLOG; 1.
DR   Pfam; PF06732; Pescadillo_N; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|HAMAP-Rule:MF_03028};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03028};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_03028};
KW   Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_03028}.
FT   DOMAIN          512..643
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   REGION          396..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..477
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  75335 MW;  17635D1E692F6D74 CRC64;
     MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH KKKVNKGSTA
     ARTFYLLKDI KFLLHEPIVS KFREYKVFVR KLRKAYGKSE WNTVERLKDN KPSYKLDHIV
     KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFLH YVIAARALRK
     VFLSIKGIYY QAEVLGQPIV WITPYTFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ
     SLNLQYPPKL EGQAHTDRKV SEDTYALDSE SSMEKLAALS ASLARVVVPA AEEEAEVDEF
     PADGEVAAQE QERRKELEAQ EKHRKLFEGL KFFLNREVPR EALAFVISSF GGSYPRCGPA
     VLRQLEPWES RAGTDSVCRE REAQLGACPV SVPGPRIFRS QSPGTWPLER RGRVWRSSES
     GQRNQQGTRH RATQPLFPRQ WGTGSVARSA PAPGQLLAQP APPSVDPHPP MQTPLSPPPH
     ADNWKQDLHK FISPDQLPAV FGGTMTDPDG NPKCLTKINP GGEVPKSYYK RQQVRLQYEH
     TVSVGRGSSQ QVENEILFPG CVLRWQFASD GGDIGFGVFL KTKMGERQRA GEMTEVLPSQ
     HYNAHLVPED GSLTCAEAGV YVLRFDNTYS LVHAKKVSYT VEVLLPDEAS QEKLQSLRAS
     SPSAQ
//
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