NUCL1_ARATH
ID NUCL1_ARATH Reviewed; 557 AA.
AC Q9FVQ1;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Nucleolin 1 {ECO:0000303|PubMed:27792779};
DE AltName: Full=Protein NUCLEOLIN LIKE 1 {ECO:0000303|PubMed:17108323};
DE Short=AtNUC-L1 {ECO:0000303|PubMed:17108323};
DE AltName: Full=Protein PARALLEL 1 {ECO:0000303|PubMed:17369435};
DE Short=AtPARL1 {ECO:0000303|PubMed:17369435};
GN Name=NUCL1 {ECO:0000303|PubMed:17108323};
GN Synonyms=NUC1 {ECO:0000303|PubMed:27792779},
GN PARL1 {ECO:0000303|PubMed:17369435};
GN OrderedLocusNames=At1g48920 {ECO:0000312|Araport:AT1G48920};
GN ORFNames=F27K7.6 {ECO:0000312|EMBL:AAG29744.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17108323; DOI=10.1091/mbc.e06-08-0751;
RA Pontvianne F., Matia I., Douet J., Tourmente S., Medina F.J.,
RA Echeverria M., Saez-Vasquez J.;
RT "Characterization of AtNUC-L1 reveals a central role of nucleolin in
RT nucleolus organization and silencing of AtNUC-L2 gene in Arabidopsis.";
RL Mol. Biol. Cell 18:369-379(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17286797; DOI=10.1111/j.1365-313x.2006.03016.x;
RA Kojima H., Suzuki T., Kato T., Enomoto K., Sato S., Kato T., Tabata S.,
RA Saez-Vasquez J., Echeverria M., Nakagawa T., Ishiguro S., Nakamura K.;
RT "Sugar-inducible expression of the nucleolin-1 gene of Arabidopsis thaliana
RT and its role in ribosome synthesis, growth and development.";
RL Plant J. 49:1053-1063(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17369435; DOI=10.1104/pp.106.093575;
RA Petricka J.J., Nelson T.M.;
RT "Arabidopsis nucleolin affects plant development and patterning.";
RL Plant Physiol. 144:173-186(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21124873; DOI=10.1371/journal.pgen.1001225;
RA Pontvianne F., Abou-Ellail M., Douet J., Comella P., Matia I.,
RA Chandrasekhara C., Debures A., Blevins T., Cooke R., Medina F.J.,
RA Tourmente S., Pikaard C.S., Saez-Vasquez J.;
RT "Nucleolin is required for DNA methylation state and the expression of rRNA
RT gene variants in Arabidopsis thaliana.";
RL PLoS Genet. 6:E1001225-E1001225(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27334696; DOI=10.1242/bio.019109;
RA Matsumura Y., Ohbayashi I., Takahashi H., Kojima S., Ishibashi N., Keta S.,
RA Nakagawa A., Hayashi R., Saez-Vasquez J., Echeverria M., Sugiyama M.,
RA Nakamura K., Machida C., Machida Y.;
RT "A genetic link between epigenetic repressor AS1-AS2 and a putative small
RT subunit processome in leaf polarity establishment of Arabidopsis.";
RL Biol. Open 5:942-954(2016).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH THAL.
RC STRAIN=cv. Columbia;
RX PubMed=27792779; DOI=10.1371/journal.pgen.1006408;
RA Chen Y.-J.C., Wang H.-J., Jauh G.-Y.;
RT "Dual role of a SAS10/C1D family protein in ribosomal RNA gene expression
RT and processing is essential for reproduction in Arabidopsis thaliana.";
RL PLoS Genet. 12:e1006408-e1006408(2016).
CC -!- FUNCTION: Involved in pre-rRNA processing and ribosome assembly
CC (PubMed:17108323, PubMed:17286797, PubMed:17369435, PubMed:21124873).
CC Is associated with intranucleolar chromatin and pre-ribosomal particles
CC and plays a role in controlling activation and repression of a specific
CC subset of rRNA genes located in distinctive nucleolar organizer
CC regions. Binds specifically rDNA chromatin and may be required to
CC maintain rDNA chromatin structure, but is probably not required for the
CC overall histone methylation status of 45S rRNA genes (PubMed:17108323,
CC PubMed:17286797, PubMed:21124873). Involved in leaf polarity
CC establishment by functioning cooperatively with AS1 to repress abaxial
CC genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox
CC genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in
CC leaf primordia at shoot apical meristems at high temperatures
CC (PubMed:27334696). {ECO:0000269|PubMed:17108323,
CC ECO:0000269|PubMed:17286797, ECO:0000269|PubMed:17369435,
CC ECO:0000269|PubMed:21124873, ECO:0000269|PubMed:27334696}.
CC -!- SUBUNIT: Interacts with THAL in the nucleus.
CC {ECO:0000269|PubMed:27792779}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17108323,
CC ECO:0000269|PubMed:17286797, ECO:0000269|PubMed:17369435,
CC ECO:0000269|PubMed:27792779}. Note=Found in the dense fibrillar
CC component region of the nucleolus. {ECO:0000269|PubMed:17108323}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, shoots and flowers.
CC {ECO:0000269|PubMed:17108323, ECO:0000269|PubMed:17286797,
CC ECO:0000269|PubMed:17369435}.
CC -!- INDUCTION: By glucose and sucrose (at protein level).
CC {ECO:0000269|PubMed:17286797}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth, bushy plants with stunted leaves,
CC abnormal vascular patterns and many stems (PubMed:17286797,
CC PubMed:17369435, PubMed:21124873). Plants exhibit a pointed narrow
CC shape of leaves, but no filamentous leaves. Plants with double
CC mutations in this protein and in AS2 or AS1 protein show severe defects
CC in leaf shape and filamentous leaves are efficiently formed, although a
CC few normally shaped leaves and markedly narrow leaves are also
CC generated (PubMed:27334696). Altered nucleolus ultrastructure
CC (PubMed:17108323). {ECO:0000269|PubMed:17108323,
CC ECO:0000269|PubMed:17286797, ECO:0000269|PubMed:17369435,
CC ECO:0000269|PubMed:21124873, ECO:0000269|PubMed:27334696}.
CC -!- MISCELLANEOUS: Disruption of NUCL1 induces NUCL2 expression.
CC {ECO:0000305|PubMed:17108323}.
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DR EMBL; AC084414; AAG29744.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32367.1; -; Genomic_DNA.
DR EMBL; BT005793; AAO64195.1; -; mRNA.
DR PIR; A96527; A96527.
DR RefSeq; NP_175322.1; NM_103785.4.
DR AlphaFoldDB; Q9FVQ1; -.
DR SMR; Q9FVQ1; -.
DR BioGRID; 26539; 9.
DR IntAct; Q9FVQ1; 2.
DR STRING; 3702.AT1G48920.1; -.
DR iPTMnet; Q9FVQ1; -.
DR MetOSite; Q9FVQ1; -.
DR PaxDb; Q9FVQ1; -.
DR PRIDE; Q9FVQ1; -.
DR ProteomicsDB; 250585; -.
DR EnsemblPlants; AT1G48920.1; AT1G48920.1; AT1G48920.
DR GeneID; 841314; -.
DR Gramene; AT1G48920.1; AT1G48920.1; AT1G48920.
DR KEGG; ath:AT1G48920; -.
DR Araport; AT1G48920; -.
DR TAIR; locus:2028451; AT1G48920.
DR eggNOG; KOG4210; Eukaryota.
DR HOGENOM; CLU_030920_1_0_1; -.
DR InParanoid; Q9FVQ1; -.
DR OMA; DIHQIRN; -.
DR OrthoDB; 1202220at2759; -.
DR PRO; PR:Q9FVQ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVQ1; baseline and differential.
DR Genevisible; Q9FVQ1; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0034057; F:RNA strand-exchange activity; IBA:GO_Central.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0000478; P:endonucleolytic cleavage involved in rRNA processing; IMP:TAIR.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0080056; P:petal vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0042254; P:ribosome biogenesis; TAS:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR GO; GO:0080057; P:sepal vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR CDD; cd12450; RRM1_NUCLs; 1.
DR CDD; cd12451; RRM2_NUCLs; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034349; NUCL_RRM1.
DR InterPro; IPR034350; NUCL_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Repressor; RNA-binding;
KW rRNA processing; Stress response.
FT CHAIN 1..557
FT /note="Nucleolin 1"
FT /id="PRO_0000417401"
FT DOMAIN 297..374
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 401..481
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 58773 MW; F6CAA737689B4CBA CRC64;
MGKSKSATKV VAEIKATKPL KKGKREPEDD IDTKVSLKKQ KKDVIAAVQK EKAVKKVPKK
VESSDDSDSE SEEEEKAKKV PAKKAASSSD ESSDDSSSDD EPAPKKAVAA TNGTVAKKSK
DDSSSSDDDS SDEEVAVTKK PAAAAKNGSV KAKKESSSED DSSSEDEPAK KPAAKIAKPA
AKDSSSSDDD SDEDSEDEKP ATKKAAPAAA KAASSSDSSD EDSDEESEDE KPAQKKADTK
ASKKSSSDES SESEEDESED EEETPKKKSS DVEMVDAEKS SAKQPKTPST PAAGGSKTLF
AANLSFNIER ADVENFFKEA GEVVDVRFST NRDDGSFRGF GHVEFASSEE AQKALEFHGR
PLLGREIRLD IAQERGERGE RPAFTPQSGN FRSGGDGGDE KKIFVKGFDA SLSEDDIKNT
LREHFSSCGE IKNVSVPIDR DTGNSKGIAY LEFSEGKEKA LELNGSDMGG GFYLVVDEPR
PRGDSSGGGG FGRGNGRFGS GGGRGRDGGR GRFGSGGGRG RDGGRGRFGS GGGRGSDRGR
GRPSFTPQGK KTTFGDE
