MET15_MOUSE
ID MET15_MOUSE Reviewed; 406 AA.
AC Q9DCL4; Q3KQI4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=12S rRNA N4-methylcytidine methyltransferase;
DE Short=12S rRNA m4C methyltransferase;
DE EC=2.1.1.-;
DE AltName: Full=Methyltransferase 5 domain-containing protein 1;
DE AltName: Full=Methyltransferase-like protein 15;
DE Flags: Precursor;
GN Name=Mettl15 {ECO:0000312|MGI:MGI:1924144}; Synonyms=Mett5d1;
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].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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].
RC TISSUE=Bone;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: N4-methylcytidine (m4C) methyltransferase responsible for the
CC methylation of position C839 in mitochondrial 12S rRNA. Involved in the
CC stabilization of 12S rRNA folding, therefore facilitating the assembly
CC of the mitochondrial small ribosomal subunits.
CC {ECO:0000250|UniProtKB:A6NJ78}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:62524, Rhea:RHEA-COMP:16109, Rhea:RHEA-COMP:16110,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:A6NJ78};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62525;
CC Evidence={ECO:0000250|UniProtKB:A6NJ78};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:A6NJ78}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000305}.
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DR EMBL; AK002682; BAB22281.2; -; mRNA.
DR EMBL; AL691430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX813309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX813328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106186; AAI06187.1; -; mRNA.
DR EMBL; BC115926; AAI15927.1; -; mRNA.
DR EMBL; BC117549; AAI17550.1; -; mRNA.
DR CCDS; CCDS16506.1; -.
DR RefSeq; NP_084066.2; NM_029790.3.
DR RefSeq; XP_006500441.1; XM_006500378.1.
DR RefSeq; XP_006500442.1; XM_006500379.3.
DR AlphaFoldDB; Q9DCL4; -.
DR SMR; Q9DCL4; -.
DR STRING; 10090.ENSMUSP00000080337; -.
DR iPTMnet; Q9DCL4; -.
DR PhosphoSitePlus; Q9DCL4; -.
DR EPD; Q9DCL4; -.
DR MaxQB; Q9DCL4; -.
DR PaxDb; Q9DCL4; -.
DR PeptideAtlas; Q9DCL4; -.
DR PRIDE; Q9DCL4; -.
DR ProteomicsDB; 295936; -.
DR Antibodypedia; 25483; 44 antibodies from 15 providers.
DR DNASU; 76894; -.
DR Ensembl; ENSMUST00000081631; ENSMUSP00000080337; ENSMUSG00000057234.
DR GeneID; 76894; -.
DR KEGG; mmu:76894; -.
DR UCSC; uc008llv.1; mouse.
DR CTD; 196074; -.
DR MGI; MGI:1924144; Mettl15.
DR VEuPathDB; HostDB:ENSMUSG00000057234; -.
DR eggNOG; KOG2782; Eukaryota.
DR GeneTree; ENSGT00390000014756; -.
DR HOGENOM; CLU_038422_1_0_1; -.
DR InParanoid; Q9DCL4; -.
DR OMA; NPAKRTF; -.
DR OrthoDB; 809593at2759; -.
DR PhylomeDB; Q9DCL4; -.
DR TreeFam; TF106425; -.
DR BioGRID-ORCS; 76894; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Mettl15; mouse.
DR PRO; PR:Q9DCL4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DCL4; protein.
DR Bgee; ENSMUSG00000057234; Expressed in pineal body and 221 other tissues.
DR ExpressionAtlas; Q9DCL4; baseline and differential.
DR Genevisible; Q9DCL4; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 1.10.150.170; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11265; PTHR11265; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF81799; SSF81799; 1.
DR TIGRFAMs; TIGR00006; TIGR00006; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..406
FT /note="12S rRNA N4-methylcytidine methyltransferase"
FT /id="PRO_0000308333"
FT BINDING 100..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NJ78"
FT CONFLICT 173
FT /note="S -> P (in Ref. 3; AAI06187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 45282 MW; 6910C9302AA6BDD9 CRC64;
MLRYPYFYRT YNRLFSHFVD SGASNLDVCP HTIHTAVALH TESKAVEGTA LCGPQKVYSS
EEKELEAMAK LHIPVMVDQV VHCLAPQKGQ VFLDMTFGSG GHTRAILQKE PDVMVYALDR
DPVAYAIAEQ LSRLYPTQIQ ALLGQFSQAE ALLMKAGVQP GTIDGILMDL GCSSMQLDAP
ERGFSLRKDG PLDMRMDGDR YPDTPTASDV VNALDQQALA SILRAYGEEK HAKKIASAII
QARSTYPISR TQQLASIVAG AFPPSAVYAR KDLLQRSTHI ATKTFQALRI FVNNELNELY
AGLRTAEKFL KTGGRLVALS FHSLEDRIVK RFLLGISMTE RFNLSIRQKV KQTSQLDSDQ
ETEERHSVRA PLKWELIHKK VLTPEDQDVQ DNPRGRSAKL RAAIKL
