NSUN4_MOUSE
ID NSUN4_MOUSE Reviewed; 381 AA.
AC Q9CZ57; Q9D7F0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=5-methylcytosine rRNA methyltransferase NSUN4;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q95XR2};
DE AltName: Full=5-methylcytosine tRNA methyltransferase NSUN4 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q95XR2};
DE AltName: Full=NOL1/NOP2/Sun domain family member 4;
DE AltName: Full=Sperm head and tail associated protein;
DE Flags: Precursor;
GN Name=Nsun4; Synonyms=Shtap;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=21531335; DOI=10.1016/j.cmet.2011.04.002;
RA Camara Y., Asin-Cayuela J., Park C.B., Metodiev M.D., Shi Y.,
RA Ruzzenente B., Kukat C., Habermann B., Wibom R., Hultenby K., Franz T.,
RA Erdjument-Bromage H., Tempst P., Hallberg B.M., Gustafsson C.M.,
RA Larsson N.G.;
RT "MTERF4 regulates translation by targeting the methyltransferase NSUN4 to
RT the mammalian mitochondrial ribosome.";
RL Cell Metab. 13:527-539(2011).
RN [5]
RP FUNCTION IN 12S RRNA METHYLATION, FUNCTION IN MITORIBOSOMAL ASSEMBLY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24516400; DOI=10.1371/journal.pgen.1004110;
RA Metodiev M.D., Spahr H., Loguercio Polosa P., Meharg C., Becker C.,
RA Altmueller J., Habermann B., Larsson N.G., Ruzzenente B.;
RT "NSUN4 is a dual function mitochondrial protein required for both
RT methylation of 12S rRNA and coordination of mitoribosomal assembly.";
RL PLoS Genet. 10:E1004110-E1004110(2014).
CC -!- FUNCTION: Involved in mitochondrial ribosome assembly. 5-methylcytosine
CC rRNA methyltransferase that probably is involved in mitochondrial
CC ribosome small subunit (SSU) maturation by methylation of mitochondrial
CC 12S rRNA at position 911; the function is independent of MTERFD2/MTERF4
CC and assembled mitochondrial ribosome large subunit (LSU). Targeted to
CC LSU by MTERFD2/MTERF4 and probably is involved in a final step in
CC ribosome biogenesis to ensure that SSU and LSU are assembled. In vitro
CC can methylate 16S rRNA of the LSU; the methylation is enhanced by
CC MTERFD/MTERF4. {ECO:0000269|PubMed:24516400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61484, Rhea:RHEA-COMP:15836, Rhea:RHEA-COMP:15837,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q95XR2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in tRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61468, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:15827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q95XR2};
CC -!- SUBUNIT: Heterodimer with MTERFD2/MTERF4; this interaction seems to be
CC required for NSUN4 recruitment to the mitochondrial large ribosomal
CC subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9CZ57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZ57-2; Sequence=VSP_025974, VSP_025975;
CC Name=3;
CC IsoId=C4P6S0-1; Sequence=External;
CC Name=4;
CC IsoId=C4P6S0-2; Sequence=External;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:24516400}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; AK009285; BAB26195.1; -; mRNA.
DR EMBL; AK012994; BAB28584.1; -; mRNA.
DR EMBL; AL627105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024628; AAH24628.1; -; mRNA.
DR CCDS; CCDS18502.1; -. [Q9CZ57-1]
DR RefSeq; NP_082418.1; NM_028142.4. [Q9CZ57-1]
DR AlphaFoldDB; Q9CZ57; -.
DR SMR; Q9CZ57; -.
DR IntAct; Q9CZ57; 1.
DR MINT; Q9CZ57; -.
DR iPTMnet; Q9CZ57; -.
DR PhosphoSitePlus; Q9CZ57; -.
DR EPD; Q9CZ57; -.
DR MaxQB; Q9CZ57; -.
DR PaxDb; Q9CZ57; -.
DR PeptideAtlas; Q9CZ57; -.
DR PRIDE; Q9CZ57; -.
DR ProteomicsDB; 293752; -. [Q9CZ57-1]
DR ProteomicsDB; 293753; -. [Q9CZ57-2]
DR Antibodypedia; 32791; 71 antibodies from 19 providers.
DR DNASU; 72181; -.
DR Ensembl; ENSMUST00000030475; ENSMUSP00000030475; ENSMUSG00000028706. [Q9CZ57-1]
DR GeneID; 72181; -.
DR KEGG; mmu:72181; -.
DR UCSC; uc008ufu.2; mouse. [Q9CZ57-1]
DR UCSC; uc012djh.1; mouse. [Q9CZ57-2]
DR CTD; 387338; -.
DR MGI; MGI:1919431; Nsun4.
DR VEuPathDB; HostDB:ENSMUSG00000028706; -.
DR GeneTree; ENSGT00500000045816; -.
DR HOGENOM; CLU_041061_2_0_1; -.
DR OrthoDB; 1239772at2759; -.
DR PhylomeDB; Q9CZ57; -.
DR TreeFam; TF321304; -.
DR BioGRID-ORCS; 72181; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Nsun4; mouse.
DR Proteomes; UP000000589; Chromosome 4.
DR Bgee; ENSMUSG00000028706; Expressed in primary oocyte and 269 other tissues.
DR ExpressionAtlas; Q9CZ57; baseline and differential.
DR Genevisible; Q9CZ57; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IMP:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; PTHR22808; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding; S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..381
FT /note="5-methylcytosine rRNA methyltransferase NSUN4"
FT /id="PRO_0000289235"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 178..184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CB9"
FT VAR_SEQ 1..147
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025974"
FT VAR_SEQ 148..195
FT /note="GLMDYYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQTGCCR ->
FT MVFITSIETQREDTSVSKRLGHTHVVPATQEAETELLENFKNSLGTTG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025975"
SQ SEQUENCE 381 AA; 42853 MW; F2BD877EA4C2880A CRC64;
MAAPVLRCVR KLLKLVDFTP VPRRYRYKKK WATTEPQFTA SRLALQNFDM TYSVQFGDLW
PSIRVSLLSE QKYGALVNNF AAWDSVSAKL EQLSAKDFVS EAISHQKLEP ESGLSPTPSL
DCSPNLRCFT FSRGDVSRFP PARLGSLGLM DYYLMDAASL LPVLALGLQH GDTVLDLCAA
PGGKTLALLQ TGCCRNLAAN DLSTSRTGRL QKVLHSYVPQ DIREGNQVRV TSWDGRKWGE
LEGDTYDRVL VDVPCTTDRH SLHEEENNIF QRSRKKERQM LPMLQVQLLA AGLLATKPGG
HVVYSTCSLS HLQNEYVVQG AIELLANQYN IKVQVEDLSH FRKLFMDTFC FFPSCQVGEL
VIPNLMVNFG PMYFCKLHRL P
