NMT2_BOVIN
ID NMT2_BOVIN Reviewed; 498 AA.
AC Q9N181;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 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 II N-myristoyltransferase.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
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; AF222687; AAF31456.1; -; mRNA.
DR RefSeq; NP_776881.1; NM_174456.2.
DR AlphaFoldDB; Q9N181; -.
DR SMR; Q9N181; -.
DR STRING; 9913.ENSBTAP00000055459; -.
DR Ensembl; ENSBTAT00000050460; ENSBTAP00000047156; ENSBTAG00000007703.
DR GeneID; 282049; -.
DR KEGG; bta:282049; -.
DR CTD; 9397; -.
DR VEuPathDB; HostDB:ENSBTAG00000007703; -.
DR VGNC; VGNC:32138; NMT2.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; Q9N181; -.
DR OMA; ILNVKSC; -.
DR OrthoDB; 1025421at2759; -.
DR BRENDA; 2.3.1.97; 908.
DR Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000007703; Expressed in occipital lobe and 103 other tissues.
DR ExpressionAtlas; Q9N181; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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 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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..498
FT /note="Glycylpeptide N-tetradecanoyltransferase 2"
FT /id="PRO_0000064225"
FT REGION 1..87
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..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 122
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 250
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 252
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 258
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 260
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 261
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 262
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 498 AA; 56803 MW; D3ECB34B98CA4D67 CRC64;
MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GDLGAKKKKK KQKRKKEKPN
SGGTKSDSAS DSQEIKIQPP SKNSTIPVQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ
FWDTQPVPKL NEVITSHGAI EADKENVRQE PYSLPQGFMW DTLDLGNAEV LRELYTLLNE
NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS
VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPVATCRYWH
RSLNPRKLVE VKFSHLSRNM TLQRTMKLYR LPDATKTSGL RPMEPRDIKA VQELTNTYLK
QFHLAPVMDE EEVAHWFLPQ EHIIDTFVVE NSSGKLTDFL SFYTLPSTVM HHPAHKSLKA
AYSFYNIHTE TPLLDLMSDA LIIAKLKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL
YNWRCPGTES EKVGLVLQ
