NMT1_BOVIN
ID NMT1_BOVIN Reviewed; 497 AA.
AC P31717; Q9N177;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 1;
DE EC=2.3.1.97 {ECO:0000269|PubMed:8452528};
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; Synonyms=NMT;
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 [MRNA].
RC TISSUE=Retina;
RA Rundle D.R., Alvarez R.A., Anderson R.E.;
RT "Bovine retina type I N-myristoyltransferase.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 95-104; 114-123; 168-191 AND 449-459, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Brain;
RX PubMed=8452528; DOI=10.1042/bj2900405;
RA McIlhinney R.A.J., McGlone K., Willis A.C.;
RT "Purification and partial sequencing of myristoyl-CoA:protein N-
RT myristoyltransferase from bovine brain.";
RL Biochem. J. 290:405-410(1993).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular and viral proteins. {ECO:0000269|PubMed:8452528}.
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:8452528};
CC -!- SUBUNIT: May be associated with other proteins.
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 -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8452528}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; AF223384; AAF31460.1; -; mRNA.
DR PIR; S30363; S30363.
DR AlphaFoldDB; P31717; -.
DR SMR; P31717; -.
DR STRING; 9913.ENSBTAP00000007950; -.
DR PaxDb; P31717; -.
DR PeptideAtlas; P31717; -.
DR PRIDE; P31717; -.
DR eggNOG; KOG2779; Eukaryota.
DR InParanoid; P31717; -.
DR BRENDA; 2.3.1.97; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; ISS:UniProtKB.
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; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..497
FT /note="Glycylpeptide N-tetradecanoyltransferase 1"
FT /id="PRO_0000064220"
FT REGION 1..82
FT /note="Disordered"
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:0000250|UniProtKB:P30419"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT CONFLICT 114..115
FT /note="KR -> AK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="T -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..169
FT /note="VL -> LF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 56919 MW; 701A5C0B3554B037 CRC64;
MGDESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN DTGAKKKKKK
QKKKKEKGSE TDSAQDQPVK 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
HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY
SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNNLQYYLY
NWKCPSMGAE KVGLVLQ
