ID   METL9_BOVIN             Reviewed;         318 AA.
AC   Q0VCJ8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein-L-histidine N-pros-methyltransferase {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H1A3};
DE   AltName: Full=Methyltransferase-like protein 9 {ECO:0000250|UniProtKB:Q9H1A3};
DE   Flags: Precursor;
GN   Name=METTL9 {ECO:0000250|UniProtKB:Q9H1A3};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC       catalyzes 1-methylhistidine (pros-methylhistidine) methylation of
CC       target proteins. Mediates methylation of proteins with a His-x-His
CC       (HxH) motif (where 'x' is preferably a small amino acid). Catalyzes
CC       methylation of target proteins such as S100A9, NDUFB3, SLC39A5,
CC       SLC39A7, ARMC6 and DNAJB12; 1-methylhistidine modification may affect
CC       the binding of zinc and other metals to its target proteins.
CC       Constitutes the main methyltransferase for the 1-methylhistidine
CC       modification in cell. {ECO:0000250|UniProtKB:Q9H1A3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(pros)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:67076, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:17184,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29979, ChEBI:CHEBI:43903,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000250|UniProtKB:Q9H1A3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67077;
CC         Evidence={ECO:0000250|UniProtKB:Q9H1A3};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9H1A3}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9H1A3}. Note=Colocalizes with membranous
CC       compartments such as the endoplasmic reticulum and mitochondria.
CC       {ECO:0000250|UniProtKB:Q9H1A3}.
CC   -!- SIMILARITY: Belongs to the METTL9 family. {ECO:0000305}.
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DR   EMBL; BC120133; AAI20134.1; -; mRNA.
DR   RefSeq; NP_001073836.1; NM_001080367.2.
DR   AlphaFoldDB; Q0VCJ8; -.
DR   SMR; Q0VCJ8; -.
DR   STRING; 9913.ENSBTAP00000025118; -.
DR   PaxDb; Q0VCJ8; -.
DR   PRIDE; Q0VCJ8; -.
DR   Ensembl; ENSBTAT00000025118; ENSBTAP00000025118; ENSBTAG00000018868.
DR   GeneID; 787067; -.
DR   KEGG; bta:787067; -.
DR   CTD; 51108; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018868; -.
DR   VGNC; VGNC:31418; METTL9.
DR   eggNOG; KOG3987; Eukaryota.
DR   GeneTree; ENSGT00390000013648; -.
DR   HOGENOM; CLU_056100_0_0_1; -.
DR   InParanoid; Q0VCJ8; -.
DR   OMA; PYMHYVE; -.
DR   OrthoDB; 899076at2759; -.
DR   TreeFam; TF314187; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000018868; Expressed in oviduct epithelium and 106 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0106370; F:protein-L-histidine N-pros-methyltransferase activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR007884; METL9.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12890; PTHR12890; 1.
DR   Pfam; PF05219; DREV; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Methyltransferase; Mitochondrion;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..318
FT                   /note="Protein-L-histidine N-pros-methyltransferase"
FT                   /id="PRO_0000317489"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  36536 MW;  83AF4D7C78342628 CRC64;
     MRLLAGWLCL SLASVWLARR MWTLRSPLTR SLYVNMTSGP GGPAAAAGGR KENHQWYVCN
     REKLCESLQA VFVQSYLDQG TQIFLNNSIE KSGWLFIQLY HSFVSSVFSL FMSRTSINGL
     LGRGSMFVFS PDQFQRLLKI NPDWKTHRLL DLGAGDGEVT KIMSPHFEEI YATELSETMI
     WQLQKKKYRV LGINEWQKTG FQYDVISCLN LLDRCDQPLT LLKDIRSVLE PTRGRVILAL
     VLPFHPYVEN VGGKWDKPSE ILEIKGQNWE EQVNSLPEVF RKAGFVIEAF TRLPYLCEGD
     MYNDYYVLDD AVFVLKPV