NUCL2_ARATH
ID NUCL2_ARATH Reviewed; 636 AA.
AC Q1PEP5; Q9LIH8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Nucleolin 2 {ECO:0000303|PubMed:27792779};
DE AltName: Full=Protein NUCLEOLIN LIKE 2 {ECO:0000303|PubMed:17108323};
DE Short=AtNUC-L2 {ECO:0000303|PubMed:17108323};
DE AltName: Full=Protein PARALLEL LIKE 1;
DE Short=AtPARLL1;
GN Name=NUCL2 {ECO:0000303|PubMed:17108323};
GN Synonyms=NUC2 {ECO:0000303|PubMed:27792779}, PARLL1;
GN OrderedLocusNames=At3g18610 {ECO:0000312|Araport:AT3G18610};
GN ORFNames=K24M9.11 {ECO:0000312|EMBL:BAB02219.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP SUBCELLULAR LOCATION.
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 TISSUE SPECIFICITY.
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 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 {ECO:0000250}.
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:27792779}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in flower buds.
CC {ECO:0000269|PubMed:17286797}.
CC -!- MISCELLANEOUS: Disruption of NUCL1 induces NUCL2 expression.
CC {ECO:0000305|PubMed:17108323}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001303; BAB02219.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76122.1; -; Genomic_DNA.
DR EMBL; DQ446672; ABE65946.1; -; mRNA.
DR RefSeq; NP_188491.1; NM_112747.3.
DR AlphaFoldDB; Q1PEP5; -.
DR SMR; Q1PEP5; -.
DR STRING; 3702.AT3G18610.1; -.
DR iPTMnet; Q1PEP5; -.
DR PaxDb; Q1PEP5; -.
DR PRIDE; Q1PEP5; -.
DR ProteomicsDB; 249352; -.
DR EnsemblPlants; AT3G18610.1; AT3G18610.1; AT3G18610.
DR GeneID; 821392; -.
DR Gramene; AT3G18610.1; AT3G18610.1; AT3G18610.
DR KEGG; ath:AT3G18610; -.
DR Araport; AT3G18610; -.
DR TAIR; locus:2086884; AT3G18610.
DR eggNOG; KOG4210; Eukaryota.
DR HOGENOM; CLU_030920_1_0_1; -.
DR InParanoid; Q1PEP5; -.
DR OMA; SCENENV; -.
DR OrthoDB; 1202220at2759; -.
DR PRO; PR:Q1PEP5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1PEP5; baseline and differential.
DR Genevisible; Q1PEP5; AT.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 Nucleus; Reference proteome; Repeat; RNA-binding; rRNA processing.
FT CHAIN 1..636
FT /note="Nucleolin 2"
FT /id="PRO_0000417403"
FT DOMAIN 384..460
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 479..558
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 68987 MW; 968CD60649717205 CRC64;
MGKSSKKSVT EVETPASMTK PLKKGKRDAE EDLDMQVTKK QKKELIDVVQ KEKAEKTVPK
KVESSSSDAS DSDEEEKTKE TPSKLKDESS SEEEDDSSSD EEIAPAKKRP EPIKKAKVES
SSSDDDSTSD EETAPVKKQP AVLEKAKVES SSSDDDSSSD EETVPVKKQP AVLEKAKIES
SSSDDDSSSD EETVPMKKQT AVLEKAKAES SSSDDGSSSD EEPTPAKKEP IVVKKDSSDE
SSSDEETPVV KKKPTTVVKD AKAESSSSEE ESSSDDEPTP AKKPTVVKNA KPAAKDSSSS
EEDSDEEESD DEKPPTKKAK VSSKTSKQES SSDESSDESD KEESKDEKVT PKKKDSDVEM
VDAEQKSNAK QPKTPTNQTQ GGSKTLFAGN LSYQIARSDI ENFFKEAGEV VDVRLSSFDD
GSFKGYGHIE FASPEEAQKA LEMNGKLLLG RDVRLDLANE RGTPRNSNPG RKGEGSQSRT
IYVRGFSSSL GEDEIKKELR SHFSKCGEVT RVHVPTDRET GASRGFAYID LTSGFDEALQ
LSGSEIGGGN IHVEESRPRD SDEGRSSNRA PARGAPRGRH SDRAPRGGRF SDRAPRGRHS
DRGAPRGRFS TRGRGPSKPS VMESSKGTKT VFNDEE
