PESC_ARATH
ID PESC_ARATH Reviewed; 590 AA.
AC Q9LYK7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
DE Short=AtPES {ECO:0000303|PubMed:25443833};
GN Name=PES {ECO:0000303|PubMed:25443833};
GN OrderedLocusNames=At5g14520 {ECO:0000312|Araport:AT5G14520};
GN ORFNames=T15N1_10 {ECO:0000312|EMBL:CAB87619.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1016/j.plantsci.2007.06.009;
RA Zografidis A., Kapolas G., Kitsios G., McCann M., Roberts K., Milioni D.,
RA Haralampidis K.;
RT "Isolation and characterization of ZePES and AtPES, the pescadillo
RT orthologs from Zinnia and Arabidopsis.";
RL Plant Sci. 173:358-369(2007).
RN [4]
RP FUNCTION, INTERACTION WITH BOP1 AND WDR12, AND SUBCELLULAR LOCATION.
RX PubMed=23909681; DOI=10.1111/tpj.12302;
RA Cho H.K., Ahn C.S., Lee H.S., Kim J.K., Pai H.S.;
RT "Pescadillo plays an essential role in plant cell growth and survival by
RT modulating ribosome biogenesis.";
RL Plant J. 76:393-405(2013).
RN [5]
RP FUNCTION, INTERACTION WITH BOP1 AND WDR12, AND SUBCELLULAR LOCATION.
RX PubMed=25443833; DOI=10.1016/j.plantsci.2014.08.012;
RA Zografidis A., Kapolas G., Podia V., Beri D., Papadopoulou K., Milioni D.,
RA Haralampidis K.;
RT "Transcriptional regulation and functional involvement of the Arabidopsis
RT pescadillo ortholog AtPES in root development.";
RL Plant Sci. 229:53-65(2014).
RN [6]
RP INTERACTION WITH NSN1, AND SUBCELLULAR LOCATION.
RX PubMed=26163696; DOI=10.1093/jxb/erv337;
RA Jeon Y., Park Y.J., Cho H.K., Jung H.J., Ahn T.K., Kang H., Pai H.S.;
RT "The nucleolar GTPase nucleostemin-like 1 plays a role in plant growth and
RT senescence by modulating ribosome biogenesis.";
RL J. Exp. Bot. 66:6297-6310(2015).
CC -!- FUNCTION: Required for maturation of ribosomal RNAs and formation of
CC the large ribosomal subunit (By similarity). Plays an essential role in
CC cell growth and survival through its regulation of ribosome biogenesis
CC and mitotic progression (PubMed:23909681). Required for normal root
CC cell growth and differentiation (PubMed:25443833). {ECO:0000255|HAMAP-
CC Rule:MF_03028, ECO:0000269|PubMed:23909681,
CC ECO:0000269|PubMed:25443833}.
CC -!- SUBUNIT: Interacts with BOP1 and WDR12 (PubMed:23909681,
CC PubMed:25443833). Interacts with NSN1 (PubMed:26163696).
CC {ECO:0000269|PubMed:23909681, ECO:0000269|PubMed:25443833,
CC ECO:0000269|PubMed:26163696}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03028, ECO:0000269|PubMed:23909681,
CC ECO:0000269|PubMed:25443833, ECO:0000269|PubMed:26163696,
CC ECO:0000269|Ref.3}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03028}. Note=Localizes in the granular component (GC) region of
CC the nucleolus. {ECO:0000269|PubMed:25443833}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot and root apical meristems,
CC epidermal cells and vasculature of developing leaves, trichome
CC progenitor cells, young flowers, developing pollen grains and ovules,
CC and mature pollen grains. {ECO:0000269|Ref.3}.
CC -!- MISCELLANEOUS: Plants silencing PES display severely compromised root
CC meristem structures and a reduction of the primary root length of up to
CC two-thirds. {ECO:0000269|PubMed:25443833}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC Rule:MF_03028}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL163792; CAB87619.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92043.1; -; Genomic_DNA.
DR PIR; T48625; T48625.
DR RefSeq; NP_196956.1; NM_121456.4.
DR AlphaFoldDB; Q9LYK7; -.
DR SMR; Q9LYK7; -.
DR STRING; 3702.AT5G14520.1; -.
DR iPTMnet; Q9LYK7; -.
DR PaxDb; Q9LYK7; -.
DR PRIDE; Q9LYK7; -.
DR ProteomicsDB; 236418; -.
DR EnsemblPlants; AT5G14520.1; AT5G14520.1; AT5G14520.
DR GeneID; 831303; -.
DR Gramene; AT5G14520.1; AT5G14520.1; AT5G14520.
DR KEGG; ath:AT5G14520; -.
DR Araport; AT5G14520; -.
DR TAIR; locus:2222607; AT5G14520.
DR eggNOG; KOG2481; Eukaryota.
DR HOGENOM; CLU_019619_2_0_1; -.
DR InParanoid; Q9LYK7; -.
DR OMA; TWIVPHY; -.
DR OrthoDB; 777920at2759; -.
DR PhylomeDB; Q9LYK7; -.
DR PRO; PR:Q9LYK7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYK7; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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); IBA:GO_Central.
DR GO; GO:0090069; P:regulation of ribosome biogenesis; ISS:TAIR.
DR GO; GO:2000232; P:regulation of rRNA processing; IMP:TAIR.
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 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..590
FT /note="Pescadillo homolog"
FT /id="PRO_0000437498"
FT DOMAIN 332..422
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 561..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 67944 MW; ADB0E7E0F2E93082 CRC64;
MPKHYRPTGK KKEGNAARYM TRSQALKHLQ VNLNLFRRLC IVKGIFPREP KKKIKGNHHT
YYHVKDIAFL MHEPLLEKFR EIKTYQKKVK KAKAKKNEEL ARLLLTRQPT YKLDRLIRER
YPTFIDALRD LDDCLTMVHL FAVLPASDRE NLEVKRVHNC RRLTHEWQAY ISRSHALRKV
FVSVKGIYYQ AEIEGQKITW LTPHAIQQVF TNDVDFGVLL TFLEFYETLL AFINFKLYHS
LNVKYPPILD SRLEALAADL YALSRYIDAS SRGMAVEPKV DASFSSQSND REESELRLAQ
LQHQLPSSEP GALMHLVADN NKEVEEDEET RVCKSLFKDL KFFLSREVPR ESLQLVITAF
GGMVSWEGEG APFKEDDESI THHIIDKPSA GHLYLSRVYV QPQWIYDCVN ARIILPTEKY
LVGRIPPPHL SPFVDNEAEG YVPDYAETIK RLQAAARNEV LPLPGVGKED LEDPQNLLYA
GVMSRAEEAE AAKNKKKMAA QEKQYHEELK MEINGSKDVV APVLAEGEGE ESVPDAMQIA
QEDADMPKVL MSRKKRKLYD AMKISQSRKR SGVEIIEQRK KRLNDTQPSS
