MET17_MOUSE
ID MET17_MOUSE Reviewed; 461 AA.
AC Q3U2U7; B2RSP2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Methyltransferase-like protein 17, mitochondrial {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=Mettl17 {ECO:0000303|PubMed:31487196, ECO:0000312|MGI:MGI:1098577};
GN Synonyms=D14Ertd209e {ECO:0000312|MGI:MGI:1098577};
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=NOD;
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 MRNA].
RC TISSUE=Brain;
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MRPS15 AND MRPS27, AND
RP MUTAGENESIS OF 194-GLY--GLY-198.
RX PubMed=31487196; DOI=10.1096/fj.201901331r;
RA Shi Z., Xu S., Xing S., Yao K., Zhang L., Xue L., Zhou P., Wang M., Yan G.,
RA Yang P., Liu J., Hu Z., Lan F.;
RT "Mettl17, a regulator of mitochondrial ribosomal RNA modifications, is
RT required for the translation of mitochondrial coding genes.";
RL FASEB J. 33:13040-13050(2019).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent RNA
CC methyltransferase required to stabilize the mitochondrial small
CC ribosomal subunit (mt-SSU) (PubMed:31487196). Required for protein
CC translation in mitochondria (PubMed:31487196).
CC {ECO:0000269|PubMed:31487196}.
CC -!- SUBUNIT: Interacts with mitochondrial small ribosomal subunit (mt-SSU)
CC subunits MRPS15 and MRPS27. {ECO:0000269|PubMed:31487196}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:31487196}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Rsm22 family.
CC {ECO:0000305}.
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DR EMBL; AK155096; BAE33043.1; -; mRNA.
DR EMBL; BC138944; AAI38945.1; -; mRNA.
DR CCDS; CCDS36913.1; -.
DR RefSeq; NP_001025161.1; NM_001029990.1.
DR AlphaFoldDB; Q3U2U7; -.
DR SMR; Q3U2U7; -.
DR BioGRID; 206646; 2.
DR STRING; 10090.ENSMUSP00000047720; -.
DR iPTMnet; Q3U2U7; -.
DR PhosphoSitePlus; Q3U2U7; -.
DR MaxQB; Q3U2U7; -.
DR PaxDb; Q3U2U7; -.
DR PRIDE; Q3U2U7; -.
DR ProteomicsDB; 292221; -.
DR Antibodypedia; 7177; 72 antibodies from 16 providers.
DR Ensembl; ENSMUST00000047899; ENSMUSP00000047720; ENSMUSG00000004561.
DR GeneID; 52535; -.
DR KEGG; mmu:52535; -.
DR UCSC; uc007tng.1; mouse.
DR CTD; 64745; -.
DR MGI; MGI:1098577; Mettl17.
DR VEuPathDB; HostDB:ENSMUSG00000004561; -.
DR eggNOG; KOG2539; Eukaryota.
DR GeneTree; ENSGT00390000006103; -.
DR InParanoid; Q3U2U7; -.
DR OMA; SKHAICR; -.
DR OrthoDB; 1439584at2759; -.
DR TreeFam; TF313708; -.
DR BioGRID-ORCS; 52535; 15 hits in 73 CRISPR screens.
DR PRO; PR:Q3U2U7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3U2U7; protein.
DR Bgee; ENSMUSG00000004561; Expressed in retinal neural layer and 235 other tissues.
DR ExpressionAtlas; Q3U2U7; baseline and differential.
DR Genevisible; Q3U2U7; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IPI:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR015324; Ribosomal_Rsm22-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF09243; Rsm22; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..461
FT /note="Methyltransferase-like protein 17, mitochondrial"
FT /id="PRO_0000312164"
FT MUTAGEN 194..198
FT /note="GSGTG->ASATA: Abolished S-adenosyl-L-methionine-
FT binding and ability to stabilize the small subunits of
FT mitochondrial ribosome."
FT /evidence="ECO:0000269|PubMed:31487196"
FT CONFLICT 77
FT /note="F -> Y (in Ref. 1; BAE33043)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="V -> I (in Ref. 1; BAE33043)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="R -> S (in Ref. 1; BAE33043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52061 MW; BDCA4C2D04DAC7B2 CRC64;
MATARTPRFL LLFCRSCRSL RGPQSRAYAA LVPGVSQVDN GSDFLGKKPH RKHPGILHLP
HVQLPQALAD AAQLMLFERP MRSVEKQVQA LTNYLWSRHL PVEPEELQRR AAYLEKKFLE
KQDSAPTEEK LREAVLHALR KTTYHWQELS YSEELSLIYM AARLDGGFAA VFRAFHEIQA
RIPEFRPQTL MDFGSGTGSV AWAAHRTWGQ SLREYVCVDS SAAMLGLAEK LLKGGSESGK
PCIPGVFFRQ FLPVSPKVQF DVVVSAYALS ELPSRADRIE VIQNLWRKTS HFLVLVENGT
KAGHRLLMDA RNLVLGEKEK SPLDLRPSFV FAPCPHELPC PQLNASKSLA CSFSQAYHPI
PFNWNKKPKE EIFSMVILAR GSPKEANRWP RITQPVLKRP RHVHCHLCCP DGHMQHAVVT
ARRHGRDLYR CARVSSWGDL LPVIAPSEFP PSSPDEEPPE N
