NMT1_RAT
ID NMT1_RAT Reviewed; 496 AA.
AC Q8K1Q0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 1;
DE EC=2.3.1.97 {ECO:0000250|UniProtKB:P30419};
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;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Daval S., Jan S., Guillou H., Legrand P., Rioux V.;
RT "Cloning of rat liver NMT1.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:P30419}.
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:P30419};
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 -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ492222; CAD37349.1; -; mRNA.
DR EMBL; BC097277; AAH97277.1; -; mRNA.
DR RefSeq; NP_683689.1; NM_148891.2.
DR AlphaFoldDB; Q8K1Q0; -.
DR SMR; Q8K1Q0; -.
DR IntAct; Q8K1Q0; 4.
DR STRING; 10116.ENSRNOP00000004046; -.
DR iPTMnet; Q8K1Q0; -.
DR PhosphoSitePlus; Q8K1Q0; -.
DR jPOST; Q8K1Q0; -.
DR PaxDb; Q8K1Q0; -.
DR PRIDE; Q8K1Q0; -.
DR Ensembl; ENSRNOT00000004046; ENSRNOP00000004046; ENSRNOG00000002989.
DR GeneID; 259274; -.
DR KEGG; rno:259274; -.
DR UCSC; RGD:628642; rat.
DR CTD; 4836; -.
DR RGD; 628642; Nmt1.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; Q8K1Q0; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; Q8K1Q0; -.
DR TreeFam; TF300701; -.
DR BRENDA; 2.3.1.97; 5301.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-RNO-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR PRO; PR:Q8K1Q0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002989; Expressed in heart and 20 other tissues.
DR Genevisible; Q8K1Q0; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019107; F:myristoyltransferase activity; IDA:RGD.
DR GO; GO:0018030; F:peptidyl-lysine N6-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042180; P:cellular ketone metabolic process; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; ISS:UniProtKB.
DR GO; GO:0006499; P:N-terminal protein myristoylation; ISO:RGD.
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_0000064224"
FT REGION 1..81
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:0000250|UniProtKB:O70310"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30419"
SQ SEQUENCE 496 AA; 56860 MW; 3A7EE954E0D0156A CRC64;
MADESETAVK LPAPSLPLMM EGNGNGHEHC SDCENEEDIS HNRGGLSPAN DTGAKKKKKK
QKKKKEKGND MDSTQDQPVK MNSLPAERIQ 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
NLTPVMNQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY
SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN
WKCPSMGAEK VGLVLQ
