MET18_MOUSE
ID MET18_MOUSE Reviewed; 362 AA.
AC Q9CZ09; Q810I8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histidine protein methyltransferase 1 homolog {ECO:0000305};
DE EC=2.1.1.85 {ECO:0000250|UniProtKB:O95568};
DE AltName: Full=Methyltransferase-like protein 18 {ECO:0000312|MGI:MGI:1917212};
GN Name=Mettl18 {ECO:0000312|MGI:MGI:1917212};
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=Egg, and Embryo;
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 STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: Protein-L-histidine N-tele-methyltransferase that
CC specifically monomethylates RPL3. Through the methylation of RPL3
CC regulates the dynamics of pre-rRNA processing, ribosome biogenesis, and
CC translation. {ECO:0000250|UniProtKB:O95568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC Evidence={ECO:0000250|UniProtKB:O95568};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC Evidence={ECO:0000250|UniProtKB:O95568};
CC -!- SUBUNIT: Interacts with GRWD1 and members of the heat shock protein 90
CC and 70 families; these proteins may possibly be methylation substrates
CC for the enzyme. {ECO:0000250|UniProtKB:O95568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O95568}. Nucleus {ECO:0000250|UniProtKB:O95568}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:O95568}.
CC -!- PTM: Monomethylated at His-144 through automethylation. Automethylation
CC at His-144 positively regulates the methyltransferase activity toward
CC RPL3. Probably methylated on other residues.
CC {ECO:0000250|UniProtKB:O95568}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK013137; BAB28672.1; -; mRNA.
DR EMBL; AK139786; BAE24137.1; -; mRNA.
DR EMBL; BC050143; AAH50143.1; -; mRNA.
DR EMBL; BC052693; AAH52693.1; -; mRNA.
DR CCDS; CCDS15431.1; -.
DR RefSeq; NP_081555.2; NM_027279.2.
DR RefSeq; XP_006497046.1; XM_006496983.2.
DR AlphaFoldDB; Q9CZ09; -.
DR SMR; Q9CZ09; -.
DR STRING; 10090.ENSMUSP00000048636; -.
DR iPTMnet; Q9CZ09; -.
DR PhosphoSitePlus; Q9CZ09; -.
DR EPD; Q9CZ09; -.
DR MaxQB; Q9CZ09; -.
DR PaxDb; Q9CZ09; -.
DR PRIDE; Q9CZ09; -.
DR ProteomicsDB; 292222; -.
DR Antibodypedia; 34368; 44 antibodies from 12 providers.
DR DNASU; 69962; -.
DR Ensembl; ENSMUST00000045694; ENSMUSP00000048636; ENSMUSG00000041396.
DR Ensembl; ENSMUST00000111490; ENSMUSP00000107116; ENSMUSG00000041396.
DR GeneID; 69962; -.
DR KEGG; mmu:69962; -.
DR UCSC; uc007dhv.2; mouse.
DR CTD; 92342; -.
DR MGI; MGI:1917212; Mettl18.
DR VEuPathDB; HostDB:ENSMUSG00000041396; -.
DR eggNOG; KOG2920; Eukaryota.
DR GeneTree; ENSGT00390000000464; -.
DR HOGENOM; CLU_038704_0_1_1; -.
DR InParanoid; Q9CZ09; -.
DR OMA; CKCRFFS; -.
DR OrthoDB; 803097at2759; -.
DR PhylomeDB; Q9CZ09; -.
DR TreeFam; TF320884; -.
DR BioGRID-ORCS; 69962; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q9CZ09; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CZ09; protein.
DR Bgee; ENSMUSG00000041396; Expressed in primary oocyte and 220 other tissues.
DR Genevisible; Q9CZ09; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042038; P:peptidyl-histidine methylation, to form tele-methylhistidine; IBA:GO_Central.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0090069; P:regulation of ribosome biogenesis; ISS:UniProtKB.
DR GO; GO:2000232; P:regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..362
FT /note="Histidine protein methyltransferase 1 homolog"
FT /id="PRO_0000247200"
FT REGION 18..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 237..243
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT COMPBIAS 28..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 206..208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 259..261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT MOD_RES 144
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:O95568"
FT CONFLICT 233
FT /note="G -> S (in Ref. 1; BAB28672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40448 MW; 9D291A856E631CC1 CRC64;
MAFQFNFSIE EDLENKLTSL DDGTCVLESQ KGKQDKRQST ERPGLPRDHS WKCSSLGNAA
SSEDTGSPPP IADRSDDPEA CKHQPSWKPA KEHVMPKDVN HVLENTVLEM LPGPQHANTA
VVKTVSLKEK FPGENIVSKS FSSHSDLIPG VYEGGLKIWE CTFDLLTYFT KAKVKFAGQK
VLDLGCGSGL LGITASKGGA REVHFQDYNG LVIDEVTLPN VVANVPLQDD SNGKNEPDGK
RQRKSEVGRE ICKCRLFSGE WAEFCKLVLR EKLFVKYDLI LTSETIYNPD YYSTLHETFL
RLLSRSGRVL LASKAHYFGV GGGVHLFQKF VEEKGVFETR TLEVIDEGLK RFLMEMTFKH
PS
