NEP1_MOUSE
ID NEP1_MOUSE Reviewed; 244 AA.
AC O35130;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase NEP1 {ECO:0000250|UniProtKB:Q92979};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q92979};
DE AltName: Full=18S rRNA (pseudouridine(1248)-N1)-methyltransferase {ECO:0000250|UniProtKB:Q92979};
DE AltName: Full=18S rRNA Psi1248 methyltransferase {ECO:0000250|UniProtKB:Q92979};
DE AltName: Full=Nucleolar protein EMG1 homolog {ECO:0000250|UniProtKB:Q92979};
DE AltName: Full=Protein C2f {ECO:0000250|UniProtKB:Q92979};
DE AltName: Full=Ribosome biogenesis protein NEP1 {ECO:0000250|UniProtKB:Q92979};
GN Name=Emg1 {ECO:0000250|UniProtKB:Q92979};
GN Synonyms=C2f {ECO:0000250|UniProtKB:Q92979}, Grcc2f;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9445485;
RA Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J.,
RA Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.;
RT "Comparative sequence analysis of a gene-rich cluster at human chromosome
RT 12p13 and its syntenic region in mouse chromosome 6.";
RL Genome Res. 8:29-40(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-
CC methyltransferase that methylates pseudouridine at position 1248
CC (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified
CC N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi)
CC conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at
CC this position. Has also an essential role in 40S ribosomal subunit
CC biogenesis independent on its methyltransferase activity, facilitating
CC the incorporation of ribosomal protein S19 during the formation of pre-
CC ribosomes. {ECO:0000250|UniProtKB:Q06287,
CC ECO:0000250|UniProtKB:Q92979}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pseudouridine(1248) in human 18S rRNA + S-adenosyl-L-
CC methionine = H(+) + N(1)-methylpseudouridine(1248) in human 18S rRNA
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46712, Rhea:RHEA-
CC COMP:11638, Rhea:RHEA-COMP:11639, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:74890; Evidence={ECO:0000250|UniProtKB:Q92979};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06287}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q92979}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase NEP1 family. {ECO:0000305}.
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DR EMBL; AC002397; AAC36006.1; -; Genomic_DNA.
DR EMBL; BC002004; AAH02004.1; -; mRNA.
DR CCDS; CCDS20524.1; -.
DR RefSeq; NP_038564.1; NM_013536.2.
DR AlphaFoldDB; O35130; -.
DR SMR; O35130; -.
DR BioGRID; 200052; 4.
DR IntAct; O35130; 1.
DR STRING; 10090.ENSMUSP00000004379; -.
DR iPTMnet; O35130; -.
DR PhosphoSitePlus; O35130; -.
DR EPD; O35130; -.
DR jPOST; O35130; -.
DR PaxDb; O35130; -.
DR PeptideAtlas; O35130; -.
DR PRIDE; O35130; -.
DR ProteomicsDB; 252947; -.
DR Antibodypedia; 6124; 191 antibodies from 24 providers.
DR DNASU; 14791; -.
DR Ensembl; ENSMUST00000004379; ENSMUSP00000004379; ENSMUSG00000004268.
DR GeneID; 14791; -.
DR KEGG; mmu:14791; -.
DR UCSC; uc009drg.2; mouse.
DR CTD; 10436; -.
DR MGI; MGI:1315195; Emg1.
DR VEuPathDB; HostDB:ENSMUSG00000004268; -.
DR eggNOG; KOG3073; Eukaryota.
DR GeneTree; ENSGT00390000000305; -.
DR HOGENOM; CLU_055846_1_1_1; -.
DR InParanoid; O35130; -.
DR OMA; QEQDWDA; -.
DR OrthoDB; 1266231at2759; -.
DR PhylomeDB; O35130; -.
DR TreeFam; TF314335; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 14791; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Emg1; mouse.
DR PRO; PR:O35130; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O35130; protein.
DR Bgee; ENSMUSG00000004268; Expressed in medial ganglionic eminence and 264 other tissues.
DR ExpressionAtlas; O35130; baseline and differential.
DR Genevisible; O35130; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0017126; P:nucleologenesis; IMP:MGI.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR CDD; cd18088; Nep1-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12636; PTHR12636; 1.
DR Pfam; PF03587; EMG1; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing; rRNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..244
FT /note="Ribosomal RNA small subunit methyltransferase NEP1"
FT /id="PRO_0000158607"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 219..224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 84
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 86
FT /note="Stabilizes Arg-84"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 125
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 128
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 132
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92979"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 244 AA; 26974 MW; F9B1A6161D30F8BD CRC64;
MSAASGGFQP RERRFSVQEQ DWETTPPKKL RLGAGSKCGG RRLIVVLEGA SLETVKVGKT
YELLNCDRHK SMLLKNGRDP GEVRPDITHQ SLLMLMDSPL NRAGLLQVYI HTQKNVLIEV
NPQTRIPRTF DRFCGLMVQL LHKLSVRAAD GPQKLLKVIK NPVSDHFPVG CMKIGTSFSV
EDISDIRELV PSSDPVVFVV GAFAHGKVSV EYTEKMVSIS NYPLSAALTC AKVTTAFEEV
WGVI
