NCL1_CAEEL
ID NCL1_CAEEL Reviewed; 851 AA.
AC P34611;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=B-box type zinc finger protein ncl-1;
GN Name=ncl-1 {ECO:0000303|PubMed:9508766, ECO:0000312|WormBase:ZK112.2g};
GN ORFNames=ZK112.2 {ECO:0000312|WormBase:ZK112.2g};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9508766; DOI=10.1083/jcb.140.6.1321;
RA Frank D.J., Roth M.B.;
RT "Ncl-1 is required for the regulation of cell size and ribosomal RNA
RT synthesis in Caenorhabditis elegans.";
RL J. Cell Biol. 140:1321-1329(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8582642; DOI=10.1093/genetics/141.3.989;
RA Hedgecock E.M., Herman R.K.;
RT "The ncl-1 gene and genetic mosaics of Caenorhabditis elegans.";
RL Genetics 141:989-1006(1995).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18652816; DOI=10.1016/j.ydbio.2008.06.037;
RA Hyenne V., Desrosiers M., Labbe J.C.;
RT "C. elegans Brat homologs regulate PAR protein-dependent polarity and
RT asymmetric cell division.";
RL Dev. Biol. 321:368-378(2008).
RN [6]
RP FUNCTION.
RX PubMed=22768349; DOI=10.1371/journal.pone.0040290;
RA Korcekova D., Gombitova A., Raska I., Cmarko D., Lanctot C.;
RT "Nucleologenesis in the Caenorhabditis elegans embryo.";
RL PLoS ONE 7:E40290-E40290(2012).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26492166; DOI=10.1371/journal.pgen.1005580;
RA Yi Y.H., Ma T.H., Lee L.W., Chiou P.T., Chen P.H., Lee C.M., Chu Y.D.,
RA Yu H., Hsiung K.C., Tsai Y.T., Lee C.C., Chang Y.S., Chan S.P., Tan B.C.,
RA Lo S.J.;
RT "A Genetic Cascade of let-7-ncl-1-fib-1 Modulates Nucleolar Size and rRNA
RT Pool in Caenorhabditis elegans.";
RL PLoS Genet. 11:E1005580-E1005580(2015).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28853436; DOI=10.1038/ncomms16083;
RA Tiku V., Jain C., Raz Y., Nakamura S., Heestand B., Liu W., Spaeth M.,
RA Suchiman H.E.D., Mueller R.U., Slagboom P.E., Partridge L., Antebi A.;
RT "Small nucleoli are a cellular hallmark of longevity.";
RL Nat. Commun. 8:16083-16083(2016).
CC -!- FUNCTION: Translational repressor that inhibits protein synthesis
CC (PubMed:9508766, PubMed:26492166). Represses the translation of mRNAs
CC such as fib-1, probably by being recruited by RNA-binding protein nos-2
CC and the Pumilio proteins puf-5, puf-8 and puf-9 to the consensus core
CC PUF binding motif in the 3'-UTR of fib-1 mRNA (PubMed:26492166).
CC Negatively regulates ribosomal RNA (rRNA) synthesis, ribosomal protein
CC synthesis and nucleolus size (PubMed:9508766, PubMed:8582642,
CC PubMed:22768349, PubMed:26492166, PubMed:28853436). Its role in the
CC negative regulation of nucleolus size is most likely through its
CC negative regulation of the translation of proteins such as the rRNA 2'-
CC O-methyltransferase fib-1, and dao-5 (PubMed:26492166,
CC PubMed:28853436). Might act directly as a transcription factor to
CC inhibit RNA polymerase I (rRNA) and III (5S RNA) transcription
CC (PubMed:9508766). Plays a role in embryonic development, and in
CC particular, is involved in regulating the localization of proteins,
CC such as par-2, that are required for embryonic cell polarity
CC (PubMed:18652816). Plays a role in the regulation of lifespan, and the
CC response to nutrient availability (PubMed:28853436).
CC {ECO:0000269|PubMed:18652816, ECO:0000269|PubMed:22768349,
CC ECO:0000269|PubMed:26492166, ECO:0000269|PubMed:28853436,
CC ECO:0000269|PubMed:8582642, ECO:0000269|PubMed:9508766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18652816,
CC ECO:0000269|PubMed:9508766}.
CC -!- TISSUE SPECIFICITY: Present in cells in which nucleoli are absent, and
CC absent from large cells in which nucleoli are prominent
CC (PubMed:9508766). Highly expressed in the gonads (PubMed:26492166).
CC {ECO:0000269|PubMed:26492166, ECO:0000269|PubMed:9508766}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (PubMed:9508766,
CC PubMed:18652816, PubMed:26492166). Abundant in early embryos, but
CC displays a progressive decline throughout the four larval stages, and
CC is subsequently up-regulated in the adult (PubMed:9508766,
CC PubMed:26492166). {ECO:0000269|PubMed:18652816,
CC ECO:0000269|PubMed:26492166, ECO:0000269|PubMed:9508766}.
CC -!- INDUCTION: Negatively regulated by the let-7 microRNA.
CC {ECO:0000269|PubMed:26492166}.
CC -!- DISRUPTION PHENOTYPE: No visible change in viability, fertility,
CC development, body morphology or movement (PubMed:8582642). However,
CC animals are approximately 9% larger after hatching than wild-type
CC counterparts (PubMed:9508766). Mild defects in early embryonic cell
CC development (PubMed:18652816). No visible change in lifespan, however
CC in contrast to wild-type, longevity is significantly reduced in
CC response to dietary restriction (PubMed:28853436). Furthermore, it
CC suppresses the increased longevity and reduced nucleoli size of eat-2
CC (ad465), glp-1 (e2141), isp-1 (qm150), and daf-2 RNAi and let-363 RNAi
CC longevity mutant models (PubMed:28853436). Most cells contain enlarged
CC nucleoli, with the exception being intestinal and germline nucleoli,
CC which are not markedly larger (PubMed:9508766, PubMed:8582642,
CC PubMed:26492166, PubMed:28853436). In contrast to wild-type, the oocyte
CC which is immediately adjacent to the spermatheca contains a nucleolus
CC (PubMed:26492166). Nucleoli have an increased capacity for protein
CC synthesis, specifically RNA polymerase I and III transcription
CC (PubMed:9508766). Defective ribosomal biogenesis with increased
CC expression of rRNAs such as 26S rRNAs, and ribosomal proteins including
CC rps-6 and rsp-15 (PubMed:26492166, PubMed:28853436). Knockout with fib-
CC 1 RNAi suppresses the enlarged nucleolus phenotype in embryos and
CC suppresses the increased 26S ribosomal RNA (rRNA) expression in the
CC single ncl-1 mutant (PubMed:26492166). Double knockout with par-2
CC mutant (it5ts) suppresses the lethality phenotype, embryonic polarity
CC defects of the par-2 mutant (it5ts) at 25 degrees Celsius
CC (PubMed:18652816). {ECO:0000269|PubMed:18652816,
CC ECO:0000269|PubMed:26492166, ECO:0000269|PubMed:28853436,
CC ECO:0000269|PubMed:8582642, ECO:0000269|PubMed:9508766}.
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; AF047027; AAC14263.1; -; mRNA.
DR EMBL; BX284603; CCD62763.1; -; Genomic_DNA.
DR PIR; S44890; S44890.
DR RefSeq; NP_498684.1; NM_066283.4.
DR AlphaFoldDB; P34611; -.
DR SMR; P34611; -.
DR BioGRID; 41292; 14.
DR DIP; DIP-25978N; -.
DR IntAct; P34611; 8.
DR STRING; 6239.ZK112.2; -.
DR EPD; P34611; -.
DR PaxDb; P34611; -.
DR PeptideAtlas; P34611; -.
DR EnsemblMetazoa; ZK112.2g.1; ZK112.2g.1; WBGene00003559.
DR EnsemblMetazoa; ZK112.2g.2; ZK112.2g.2; WBGene00003559.
DR EnsemblMetazoa; ZK112.2g.3; ZK112.2g.3; WBGene00003559.
DR UCSC; ZK112.2; c. elegans.
DR WormBase; ZK112.2g; CE00373; WBGene00003559; ncl-1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000170685; -.
DR HOGENOM; CLU_007697_0_0_1; -.
DR InParanoid; P34611; -.
DR PhylomeDB; P34611; -.
DR SignaLink; P34611; -.
DR PRO; PR:P34611; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003559; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34611; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0030371; F:translation repressor activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IMP:UniProtKB.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0017126; P:nucleologenesis; IMP:UniProtKB.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF01436; NHL; 5.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR PROSITE; PS51125; NHL; 5.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Repeat;
KW Repressor; Ribosome biogenesis; Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..851
FT /note="B-box type zinc finger protein ncl-1"
FT /id="PRO_0000220367"
FT REPEAT 573..616
FT /note="NHL 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 620..665
FT /note="NHL 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 666..707
FT /note="NHL 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 708..750
FT /note="NHL 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 751..794
FT /note="NHL 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT ZN_FING 127..174
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 218..261
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 303..331
FT /evidence="ECO:0000255"
FT COMPBIAS 72..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 851 AA; 91955 MW; 166FDC4623AE494C CRC64;
METQLSVQLG LDSLLTDFGL ESVMNKQQQL FANMGLSDIG APTPSTAIPV PNAHLHPSMV
AGSDPSNPVV GFGFGSPSST TSSSPPLSNS PTIEQQQHAQ LTAMMQGIMS NNNVAVSNGS
GVQVASVPAV HCSGCKSNET ATSFCQDCNA NLCDNCTMAH KFMHCFADHR VVSLTTPGTG
SSSSSTSSSS SASSTSSHQV PSLGGKQSPD SMMLGSGKRS VLCLQHRASE LVFFCVSCNL
AICRDCTVSD HPSGTHQYEL IADVADKQML KMEQLIADAR SKHADMLDMF KQVDNKQQVL
TASLHNAHAQ LEETVSNLIN VIQDQKKTLA KDIDNAFAAK QIQLTMVDKR IQSMADKLSQ
TIEFSRRLMS FASPAEVMVF KQLLDTRLQL FLGFNPDTSG VLMTPCEIEY LGAAGLFNNS
ASTVSQLLGS VHGGSPINNA PAANDFLMPQ AGLAPIGRAQ SRIIPIEQNQ LARSPPHHIA
GSLPMNAYSD SNLLRPNKDF GGSSQSLGPF NPLGASVPGA AADPFSSQYD KWSLGVEPSV
GGLLEGGNVD EEKFQTLFPP SRSQIKRQKM IYHCKFGEFG VMEGQFTEPS GVAVNGQGDI
VVADTNNHRI QVFDKEGRFK FQFGECGKRD GQLLYPNRVA VNRTTGDFVV TERSPTHQIQ
VYNQYGQFLR KFGANILQHP RGVCVDSKGR IIVVECKVMR VIIFDMFGNI LQKFSCSRYL
EFPNGVCTND KNEILISDNR AHCIKVFSYE GQYLRQIGGE GVTNYPIGVG INSLGEVVVA
DNHNNFNLTV FSQDGTMIGA LESRVKHAQC FDVALVDDGS VVLASKDYRL YLYRFLPATS
GQSTSSASSQ I
