NSUN5_MOUSE
ID NSUN5_MOUSE Reviewed; 465 AA.
AC Q8K4F6; Q3U0Q8; Q80WG3; Q8C568;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=28S rRNA (cytosine-C(5))-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305|PubMed:31722427};
DE AltName: Full=NOL1/NOP2/Sun domain family member 5 {ECO:0000303|PubMed:30485550, ECO:0000303|PubMed:31174389};
DE AltName: Full=Williams-Beuren syndrome chromosomal region 20A protein homolog {ECO:0000303|PubMed:12073013};
GN Name=Nsun5 {ECO:0000303|PubMed:30485550, ECO:0000303|PubMed:31174389,
GN ECO:0000312|MGI:MGI:2140844};
GN Synonyms=Wbscr20a {ECO:0000303|PubMed:12073013};
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 [MRNA].
RX PubMed=12073013; DOI=10.1007/s00439-002-0710-x;
RA Merla G., Ucla C., Guipponi M., Reymond A.;
RT "Identification of additional transcripts in the Williams-Beuren syndrome
RT critical region.";
RL Hum. Genet. 110:429-438(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Liver, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-465.
RC STRAIN=C57BL/6J; TISSUE=Mammary 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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31174389; DOI=10.3390/cells8060552;
RA Yuan Z., Chen P., Zhang T., Shen B., Chen L.;
RT "Agenesis and hypomyelination of corpus callosum in mice lacking Nsun5, an
RT RNA methyltransferase.";
RL Cells 8:0-0(2019).
RN [5]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=30485550; DOI=10.1002/glia.23565;
RA Zhang T., Chen P., Li W., Sha S., Wang Y., Yuan Z., Shen B., Chen L.;
RT "Cognitive deficits in mice lacking Nsun5, a cytosine-5 RNA
RT methyltransferase, with impairment of oligodendrocyte precursor cells.";
RL Glia 67:688-702(2019).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31462248; DOI=10.1186/s13041-019-0496-6;
RA Chen P., Zhang T., Yuan Z., Shen B., Chen L.;
RT "Expression of the RNA methyltransferase Nsun5 is essential for developing
RT cerebral cortex.";
RL Mol. Brain 12:74-74(2019).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31722427; DOI=10.1093/nar/gkz1043;
RA Heissenberger C., Liendl L., Nagelreiter F., Gonskikh Y., Yang G.,
RA Stelzer E.M., Krammer T.L., Micutkova L., Vogt S., Kreil D.P., Sekot G.,
RA Siena E., Poser I., Harreither E., Linder A., Ehret V., Helbich T.H.,
RA Grillari-Voglauer R., Jansen-Duerr P., Kos M., Polacek N., Grillari J.,
RA Schosserer M.;
RT "Loss of the ribosomal RNA methyltransferase NSUN5 impairs global protein
RT synthesis and normal growth.";
RL Nucleic Acids Res. 47:11807-11825(2019).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C(5) position of cytosine 3438 (m5C3438) in
CC 28S rRNA (PubMed:31722427). m5C3782 promotes protein translation
CC without affecting ribosome biogenesis and fidelity (By similarity).
CC Required for corpus callosum and cerebral cortex development
CC (PubMed:31174389, PubMed:31462248). {ECO:0000250|UniProtKB:Q96P11,
CC ECO:0000269|PubMed:31174389, ECO:0000269|PubMed:31462248,
CC ECO:0000269|PubMed:31722427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 28S rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in 28S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47788, Rhea:RHEA-COMP:11915, Rhea:RHEA-COMP:11916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000305|PubMed:31722427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47789;
CC Evidence={ECO:0000305|PubMed:31722427};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96P11}.
CC -!- TISSUE SPECIFICITY: In the hippocampus, specifically expressed in adult
CC hippocampal NG2-positive oligodendrocyte precursor cells (at protein
CC level). {ECO:0000269|PubMed:30485550}.
CC -!- DEVELOPMENTAL STAGE: Present in the developing cerebral cortex from
CC embryonic day 12.5 dpc, with a peak at 14.5 dpc followed by a decrease
CC from 18.5 dpc (at protein level) (PubMed:31462248). Selectively
CC expressed in radial glial cells of cerebral cortex from 12.5 to 16.5
CC dpc, but not in intermediate progenitor cells (IPCs) or neocortical
CC neurons (at protein level) (PubMed:31462248). Highly expressed in
CC callosal oligodendrocyte precursor cells (OPCs) and oligodendrocytes
CC (OLs) from postnatal day 7 to postnatal day 28 (PubMed:31174389).
CC {ECO:0000269|PubMed:31174389, ECO:0000269|PubMed:31462248}.
CC -!- DISRUPTION PHENOTYPE: Decreased body weight and lean mass without
CC alterations in food intake (PubMed:31722427). Adult mice show spatial
CC cognitive deficits, possibly caused by defects in development and
CC function of oligodendrocyte precursor cells (PubMed:30485550). Mice
CC display a reduction of the corpus callosum with a decline in the number
CC of myelinated axons and loose myelin sheath (PubMed:31174389). They
CC also show impaired development of the cerebral cortex, characterized by
CC impaired growth of radial glial scaffold (PubMed:31462248).
CC {ECO:0000269|PubMed:30485550, ECO:0000269|PubMed:31174389,
CC ECO:0000269|PubMed:31462248, ECO:0000269|PubMed:31722427}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF412029; AAM62311.1; -; mRNA.
DR EMBL; AK079400; BAC37634.1; -; mRNA.
DR EMBL; AK149521; BAE28935.1; -; mRNA.
DR EMBL; AK156651; BAE33793.1; -; mRNA.
DR EMBL; BC051209; AAH51209.1; ALT_INIT; mRNA.
DR CCDS; CCDS19740.1; -.
DR RefSeq; NP_663389.2; NM_145414.2.
DR AlphaFoldDB; Q8K4F6; -.
DR SMR; Q8K4F6; -.
DR BioGRID; 221497; 1.
DR IntAct; Q8K4F6; 1.
DR MINT; Q8K4F6; -.
DR STRING; 10090.ENSMUSP00000000940; -.
DR iPTMnet; Q8K4F6; -.
DR PhosphoSitePlus; Q8K4F6; -.
DR EPD; Q8K4F6; -.
DR MaxQB; Q8K4F6; -.
DR PaxDb; Q8K4F6; -.
DR PeptideAtlas; Q8K4F6; -.
DR PRIDE; Q8K4F6; -.
DR ProteomicsDB; 252860; -.
DR Antibodypedia; 14275; 91 antibodies from 22 providers.
DR DNASU; 100609; -.
DR Ensembl; ENSMUST00000000940; ENSMUSP00000000940; ENSMUSG00000000916.
DR GeneID; 100609; -.
DR KEGG; mmu:100609; -.
DR UCSC; uc008zyh.1; mouse.
DR CTD; 55695; -.
DR MGI; MGI:2140844; Nsun5.
DR VEuPathDB; HostDB:ENSMUSG00000000916; -.
DR eggNOG; KOG2360; Eukaryota.
DR GeneTree; ENSGT00940000155974; -.
DR HOGENOM; CLU_005316_7_4_1; -.
DR InParanoid; Q8K4F6; -.
DR OMA; IQMGKHP; -.
DR OrthoDB; 1128973at2759; -.
DR PhylomeDB; Q8K4F6; -.
DR TreeFam; TF314285; -.
DR BioGRID-ORCS; 100609; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Nsun5; mouse.
DR PRO; PR:Q8K4F6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K4F6; protein.
DR Bgee; ENSMUSG00000000916; Expressed in dorsal pancreas and 223 other tissues.
DR ExpressionAtlas; Q8K4F6; baseline and differential.
DR Genevisible; Q8K4F6; MM.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0022038; P:corpus callosum development; IMP:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IDA:UniProtKB.
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; PTHR22807; PTHR22807; 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 Acetylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96P11"
FT CHAIN 2..465
FT /note="28S rRNA (cytosine-C(5))-methyltransferase"
FT /id="PRO_0000261670"
FT REGION 430..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 234..240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q96P11"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P11"
FT CONFLICT 40
FT /note="V -> M (in Ref. 2; BAE33793)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Q -> H (in Ref. 1; AAM62311)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="S -> N (in Ref. 2; BAE33793)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="L -> F (in Ref. 3; AAH51209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 51030 MW; E0545B5290D46D9A CRC64;
MGLYAAAAAV LAGVESRQGS LKGLVYSSNF QNLKQLYALV CETQRYSAVL DAVIASAGLL
RAEKKLRPHL AKVLVYELLL GKGFRGGGGR WKALLGRHQA RLKAELARLK VHRGVSRNED
LLQESSRPGQ AYQVPRFVRV NTLKTRPEDA IDYFKRQGFS YQGRASSLED LRALKGQHFL
LDPLLPELLV FPAQTDLHEH PLYRAGHLIL QDKASCLPAM LLSPPPGSHV IDACAAPGNK
TSYIAALLKN QGKIFAFDQD AKRLAAMATL VARAGVSCCE LAEKDFLTVS PSDQRYSQVQ
YILLDPSCSG SGMLSRQLEE HGEGTPSKER LQALAGFQQR ALCHALRFPS LQRLVYSTCS
LCQEENEDVV QEALQHNSGT FRLAPVLPTW PHRGLSTFPG SEHCLRASPE TTLTGGFFIA
VFERAEVVPT PAPQTDAMDP EPLSQVPKRK RRRKAAVGAS MQPST
