NMT1_MOUSE
ID NMT1_MOUSE Reviewed; 496 AA.
AC O70310;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 1;
DE EC=2.3.1.97 {ECO:0000269|PubMed:15753093};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 1;
DE Short=NMT 1;
DE Short=Type I N-myristoyltransferase;
DE AltName: Full=Peptide N-myristoyltransferase 1;
GN Name=Nmt1 {ECO:0000303|PubMed:9506952, ECO:0000312|MGI:MGI:102579};
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=9506952; DOI=10.1074/jbc.273.12.6595;
RA Giang D.K., Cravatt B.F.;
RT "A second mammalian N-myristoyltransferase.";
RL J. Biol. Chem. 273:6595-6598(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=15753093; DOI=10.1074/jbc.m412917200;
RA Yang S.H., Shrivastav A., Kosinski C., Sharma R.K., Chen M.H.,
RA Berthiaume L.G., Peters L.L., Chuang P.T., Young S.G., Bergo M.O.;
RT "N-myristoyltransferase 1 is essential in early mouse development.";
RL J. Biol. Chem. 280:18990-18995(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-47, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular and viral proteins (PubMed:15753093). Also able to
CC mediate N-terminal lysine myristoylation of proteins: catalyzes
CC myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (By similarity).
CC Lysine myristoylation is required to maintain ARF6 on membranes during
CC the GTPase cycle (By similarity). Required for normal embryogenesis
CC (PubMed:15753093). {ECO:0000250|UniProtKB:P30419,
CC ECO:0000269|PubMed:15753093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133050; EC=2.3.1.97;
CC Evidence={ECO:0000269|PubMed:15753093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-L-lysyl-[protein] + tetradecanoyl-CoA = CoA
CC + H(+) + N-terminal glycyl-(N(6)-tetradecanoyl)-L-lysyl-[protein];
CC Xref=Rhea:RHEA:70671, Rhea:RHEA-COMP:17947, Rhea:RHEA-COMP:17948,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:189855, ChEBI:CHEBI:189856;
CC Evidence={ECO:0000250|UniProtKB:P30419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70672;
CC Evidence={ECO:0000250|UniProtKB:P30419};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30419}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P30419}. Membrane
CC {ECO:0000250|UniProtKB:P30419}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P30419}. Note=Copurifies with ribosomes.
CC {ECO:0000250|UniProtKB:P30419}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15753093}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality. Embryos die between
CC 3.5 and 7.5 dpc. {ECO:0000269|PubMed:15753093}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; AF043326; AAC09296.1; -; mRNA.
DR EMBL; BC016526; AAH16526.1; -; mRNA.
DR EMBL; BC021635; AAH21635.1; -; mRNA.
DR CCDS; CCDS25511.1; -.
DR RefSeq; NP_032733.1; NM_008707.3.
DR RefSeq; XP_006532508.1; XM_006532445.3.
DR AlphaFoldDB; O70310; -.
DR SMR; O70310; -.
DR BioGRID; 201793; 18.
DR IntAct; O70310; 1.
DR STRING; 10090.ENSMUSP00000021314; -.
DR iPTMnet; O70310; -.
DR PhosphoSitePlus; O70310; -.
DR SwissPalm; O70310; -.
DR EPD; O70310; -.
DR jPOST; O70310; -.
DR PaxDb; O70310; -.
DR PeptideAtlas; O70310; -.
DR PRIDE; O70310; -.
DR ProteomicsDB; 293588; -.
DR Antibodypedia; 17578; 204 antibodies from 25 providers.
DR DNASU; 18107; -.
DR Ensembl; ENSMUST00000021314; ENSMUSP00000021314; ENSMUSG00000020936.
DR GeneID; 18107; -.
DR KEGG; mmu:18107; -.
DR UCSC; uc007ltd.1; mouse.
DR CTD; 4836; -.
DR MGI; MGI:102579; Nmt1.
DR VEuPathDB; HostDB:ENSMUSG00000020936; -.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; O70310; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; O70310; -.
DR TreeFam; TF300701; -.
DR BRENDA; 2.3.1.97; 3474.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR BioGRID-ORCS; 18107; 8 hits in 77 CRISPR screens.
DR ChiTaRS; Nmt1; mouse.
DR PRO; PR:O70310; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O70310; protein.
DR Bgee; ENSMUSG00000020936; Expressed in ileal epithelium and 255 other tissues.
DR ExpressionAtlas; O70310; baseline and differential.
DR Genevisible; O70310; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IMP:MGI.
DR GO; GO:0019107; F:myristoyltransferase activity; ISO:MGI.
DR GO; GO:0018030; F:peptidyl-lysine N6-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042180; P:cellular ketone metabolic process; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; ISS:UniProtKB.
DR GO; GO:0006499; P:N-terminal protein myristoylation; IMP:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000903; NMT.
DR InterPro; IPR022677; NMT_C.
DR InterPro; IPR022678; NMT_CS.
DR InterPro; IPR022676; NMT_N.
DR PANTHER; PTHR11377; PTHR11377; 1.
DR Pfam; PF01233; NMT; 1.
DR Pfam; PF02799; NMT_C; 1.
DR PIRSF; PIRSF015892; N-myristl_transf; 1.
DR SUPFAM; SSF55729; SSF55729; 2.
DR PROSITE; PS00975; NMT_1; 1.
DR PROSITE; PS00976; NMT_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..496
FT /note="Glycylpeptide N-tetradecanoyltransferase 1"
FT /id="PRO_0000064222"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 119
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 120
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 247
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 248
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 249
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 250
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 256
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 258
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 259
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 260
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30419"
SQ SEQUENCE 496 AA; 56888 MW; 61FA7B854A5CF3BC CRC64;
MADESETAVK LPAPSLPLMM EGNGNGHEHC SDCENEEDNS HNRSGLSPAN DTGAKKKKKK
QKKKKEKGSD MESTQDQPVK MTSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW
DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY TLPQGFTWDA LDLGDRGVLK ELYTLLNENY
VEDDDNMFRF DYSPEFLLWA LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK
KMVEINFLCV HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS
LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP MEKKDIPVVH QLLSRYLKQF
HLTPVMNQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY
SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN
WKCPSMGAEK VGLVLQ
