ID   MET18_RAT               Reviewed;         362 AA.
AC   Q4KM84;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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|RGD:1306783};
GN   Name=Mettl18 {ECO:0000312|RGD:1306783};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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}.
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DR   EMBL; BC098702; AAH98702.1; -; mRNA.
DR   RefSeq; NP_001020839.1; NM_001025668.1.
DR   RefSeq; XP_006250217.1; XM_006250155.3.
DR   AlphaFoldDB; Q4KM84; -.
DR   SMR; Q4KM84; -.
DR   STRING; 10116.ENSRNOP00000003480; -.
DR   PhosphoSitePlus; Q4KM84; -.
DR   PaxDb; Q4KM84; -.
DR   PRIDE; Q4KM84; -.
DR   Ensembl; ENSRNOT00000003636; ENSRNOP00000003480; ENSRNOG00000025189.
DR   GeneID; 304928; -.
DR   KEGG; rno:304928; -.
DR   UCSC; RGD:1306783; rat.
DR   CTD; 92342; -.
DR   RGD; 1306783; Mettl18.
DR   eggNOG; KOG2920; Eukaryota.
DR   GeneTree; ENSGT00390000000464; -.
DR   HOGENOM; CLU_038704_0_1_1; -.
DR   InParanoid; Q4KM84; -.
DR   OMA; CKCRFFS; -.
DR   OrthoDB; 803097at2759; -.
DR   PhylomeDB; Q4KM84; -.
DR   TreeFam; TF320884; -.
DR   PRO; PR:Q4KM84; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000025189; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q4KM84; RN.
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:RGD.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
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   Pfam; PF10294; Methyltransf_16; 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_0000247201"
FT   REGION          28..89
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        54..72
FT                   /note="Polar 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"
SQ   SEQUENCE   362 AA;  40009 MW;  5C3B48F4573B2CED CRC64;
     MAFQFNFSIE EDLENKLTSL DDGTCVLKSQ KGKEDKNQST ELPGLPQDRL WKCSSLGSAA
     SSEDTDSPPS TADRSGVPEA CEKQPSLKPA KEHVIPKDCD QVLENKVLEM LPGSQHVSTA
     VVKTISLKEK FPGENIVSQS FSSHSDLIPG VYEGGLKIWE CTFDLMTYFT KAKVKFAGQK
     VLDLGCGSGL LGITASKGGA REVHFQDYNG LVIDEVTLPN VVANVPLQGD SNGINEPAGK
     RQRKSEVAQE TCKCRLFSGE WAEFCKLVLS EKLFVKYDLI LTSETIYNPD YYSTLHETLL
     RLLSRNGRVL LASKAHYFGV GGGVHLFQKF VEEKGVFETR TLEVIDEGLK RFLMEMTFKC
     PS