ID   A0A0A6YX97_MOUSE        Unreviewed;       144 AA.
AC   A0A0A6YX97;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-NOV-2024, entry version 44.
DE   RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1 {ECO:0000256|ARBA:ARBA00040761};
DE            EC=2.1.1.244 {ECO:0000256|ARBA:ARBA00039112};
DE   AltName: Full=Alpha N-terminal protein methyltransferase 1A {ECO:0000256|ARBA:ARBA00041207};
DE   AltName: Full=Methyltransferase-like protein 11A {ECO:0000256|ARBA:ARBA00042768};
DE   AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A {ECO:0000256|ARBA:ARBA00041385};
DE   Flags: Fragment;
GN   Name=Ntmt1 {ECO:0000313|Ensembl:ENSMUSP00000141900.2,
GN   ECO:0000313|MGI:MGI:1913867};
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 {ECO:0000313|Ensembl:ENSMUSP00000141900.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000141900.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141900.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
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   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000141900.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141900.2};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000141900.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141900.2};
RG   Ensembl;
RL   Submitted (AUG-2024) to UniProtKB.
CC   -!- FUNCTION: Distributive alpha-N-methyltransferase that methylates the N-
CC       terminus of target proteins containing the N-terminal motif
CC       [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved.
CC       Specifically catalyzes mono-, di- or tri-methylation of the exposed
CC       alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-
CC       Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys
CC       motif. Some of the substrates may be primed by NTMT2-mediated
CC       monomethylation. Catalyzes the trimethylation of the N-terminal Gly in
CC       CENPA (after removal of Met-1). Responsible for the N-terminal
CC       methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required
CC       during mitosis for normal bipolar spindle formation and chromosome
CC       segregation via its action on RCC1. {ECO:0000256|ARBA:ARBA00046023}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-
CC         [protein] + 3 S-adenosyl-L-homocysteine + 3 H(+);
CC         Xref=Rhea:RHEA:54712, Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13971,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138057, ChEBI:CHEBI:138315; EC=2.1.1.244;
CC         Evidence={ECO:0000256|ARBA:ARBA00035913};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-
CC         L-methionine = N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-
CC         [protein] + 2 S-adenosyl-L-homocysteine + 2 H(+);
CC         Xref=Rhea:RHEA:54736, Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138059, ChEBI:CHEBI:138318; EC=2.1.1.244;
CC         Evidence={ECO:0000256|ARBA:ARBA00036157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl-
CC         [protein] + 3 S-adenosyl-L-homocysteine + 3 H(+);
CC         Xref=Rhea:RHEA:54724, Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13973,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138061, ChEBI:CHEBI:138317; EC=2.1.1.244;
CC         Evidence={ECO:0000256|ARBA:ARBA00036171};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC       {ECO:0000256|ARBA:ARBA00009059}.
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DR   Antibodypedia; 17874; 155 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000143970.3; ENSMUSP00000141900.2; ENSMUSG00000026857.10.
DR   AGR; MGI:1913867; -.
DR   MGI; MGI:1913867; Ntmt1.
DR   VEuPathDB; HostDB:ENSMUSG00000026857; -.
DR   GeneTree; ENSGT00390000008371; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000026857; Expressed in saccule of membranous labyrinth and 241 other cell types or tissues.
DR   ExpressionAtlas; A0A0A6YX97; baseline and differential.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006480; P:N-terminal protein amino acid methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR008576; MeTrfase_NTM1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12753; AD-003 - RELATED; 1.
DR   PANTHER; PTHR12753:SF1; N-TERMINAL XAA-PRO-LYS N-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF05891; Methyltransf_PK; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A0A6YX97,
KW   ECO:0007829|ProteomicsDB:A0A0A6YX97};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000141900.2"
SQ   SEQUENCE   144 AA;  16366 MW;  EE71B85142E03F54 CRC64;
     XSEVIEDEKQ FYSKAKTYWK QIPPTVDGML GGYGHISNID LNSSRKFLQR FLREGPNKTG
     TSCALDCGAG IGRITKRLLL PLFRVVDMVD VTEDFLAKAK TYLGEEGKRV RNYFCCGLQD
     FSPEPGSYDV IWIQWVIELW PPLA
//