NMT2_MOUSE
ID NMT2_MOUSE Reviewed; 529 AA.
AC O70311;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 2;
DE EC=2.3.1.97 {ECO:0000250|UniProtKB:O60551};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 2;
DE Short=NMT 2;
DE AltName: Full=Peptide N-myristoyltransferase 2;
DE AltName: Full=Type II N-myristoyltransferase;
GN Name=Nmt2;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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. Also able to mediate N-terminal
CC lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on
CC both 'Gly-2' and 'Lys-3'. Lysine myristoylation is required to maintain
CC ARF6 on membranes during the GTPase cycle.
CC {ECO:0000250|UniProtKB:O60551}.
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:0000250|UniProtKB:O60551};
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:O60551};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70672;
CC Evidence={ECO:0000250|UniProtKB:O60551};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60551}.
CC Membrane {ECO:0000250|UniProtKB:O60551}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O60551}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; AF043327; AAC09297.1; -; mRNA.
DR CCDS; CCDS15644.1; -.
DR RefSeq; NP_032734.1; NM_008708.2.
DR AlphaFoldDB; O70311; -.
DR SMR; O70311; -.
DR BioGRID; 201794; 4.
DR IntAct; O70311; 1.
DR MINT; O70311; -.
DR STRING; 10090.ENSMUSP00000080600; -.
DR iPTMnet; O70311; -.
DR PhosphoSitePlus; O70311; -.
DR EPD; O70311; -.
DR PaxDb; O70311; -.
DR PRIDE; O70311; -.
DR ProteomicsDB; 293695; -.
DR Antibodypedia; 673; 424 antibodies from 28 providers.
DR Ensembl; ENSMUST00000081932; ENSMUSP00000080600; ENSMUSG00000026643.
DR GeneID; 18108; -.
DR KEGG; mmu:18108; -.
DR UCSC; uc008idq.2; mouse.
DR CTD; 9397; -.
DR MGI; MGI:1202298; Nmt2.
DR VEuPathDB; HostDB:ENSMUSG00000026643; -.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR InParanoid; O70311; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; O70311; -.
DR TreeFam; TF300701; -.
DR BRENDA; 2.3.1.97; 3474.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 18108; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Nmt2; mouse.
DR PRO; PR:O70311; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70311; protein.
DR Bgee; ENSMUSG00000026643; Expressed in cumulus cell and 223 other tissues.
DR ExpressionAtlas; O70311; baseline and differential.
DR Genevisible; O70311; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018030; F:peptidyl-lysine N6-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; ISS:UniProtKB.
DR GO; GO:0006499; P:N-terminal protein myristoylation; TAS: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 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..529
FT /note="Glycylpeptide N-tetradecanoyltransferase 2"
FT /id="PRO_0000064227"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 281
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 283
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 289
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 291
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 292
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 293
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60551"
SQ SEQUENCE 529 AA; 60484 MW; 7D5C93D9159F315C CRC64;
MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GDLGAKKKKK KQKRKKEKPN
SGGTKSDSAS DSQEIKIQQS SKHNAIWQQI SAGAAMGGDT MEGEWIDLRM YHKNPTIPIQ
KLQDIQRAME LLSACQGPAR NIDEATKRRY QFWDTQPVPK LNEVITSHGA IEPDKDNIRQ
EPYSLPQGFM WDTLDLSNAE VLKELYTLLN ENYVEDDDNM FRFDYSPEFL LWALRPPGWL
LQWHCGVRVS SNKKLVGFIS AIPANIRIYD SVKRMVEINF LCVHKKLRSK RVAPVLIREI
TRRVNLEGIF QAVYTAGVVL PKPVATCRYW HRSLNPRKLV EVKFSHLSRN MTLQRTMKLY
RLPDVTKTSG LRPMEPKDIK AVRELINIYL KQFHLAPVMD DAEVAHWFLP REHIIDTFVV
ENPSGKLTDF LSFYTLPSTV MHHPAHKSLK AAYSFYNIHT ETPLLDLMND ALIIAKLKGF
DVFNALDLME NKTFLEKLKF GIGDGNLQYY LYNWRCPGTD SEKVGLVLQ
