NMT_DROME
ID NMT_DROME Reviewed; 472 AA.
AC O61613; Q9XZ55;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97 {ECO:0000305|PubMed:11139338};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE Short=NMT {ECO:0000303|PubMed:9044045};
DE AltName: Full=Peptide N-myristoyltransferase;
DE AltName: Full=dNMT;
GN Name=Nmt; ORFNames=CG7436;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9044045; DOI=10.1242/jcs.110.2.149;
RA Ntwasa M., Egerton M., Gay N.J.;
RT "Sequence and expression of Drosophila myristoyl-CoA: protein N-myristoyl
RT transferase: evidence for proteolytic processing and membrane
RT localisation.";
RL J. Cell Sci. 110:149-156(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11139338; DOI=10.1006/excr.2000.5086;
RA Ntwasa M., Aapies S., Schiffmann D.A., Gay N.J.;
RT "Drosophila embryos lacking N-myristoyltransferase have multiple
RT developmental defects.";
RL Exp. Cell Res. 262:134-144(2001).
CC -!- FUNCTION: Adds a myristoyl group (tetradecanoyl group) to the N-
CC terminal glycine residue of certain cellular proteins (Probable). Such
CC protein modification are critical for the developmental processes that
CC involve cell shape changes and movement (PubMed:11139338).
CC {ECO:0000269|PubMed:11139338, ECO:0000305|PubMed:11139338,
CC ECO:0000305|PubMed:9044045}.
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:0000305|PubMed:11139338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15522;
CC Evidence={ECO:0000305|PubMed:11139338};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9044045}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9044045}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos show disrupted actin cytoskeleton
CC and abnormal cell morphology (PubMed:11139338). The range of phenotypes
CC includes head involution failure, dorsal closure, and germ-band
CC retraction, as well as widespread ectopic apoptosis (PubMed:11139338).
CC {ECO:0000269|PubMed:11139338}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08578.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF053725; AAC08578.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014296; AAF50476.1; -; Genomic_DNA.
DR EMBL; AF132556; AAD27855.1; -; mRNA.
DR EMBL; AY118963; AAM50823.1; -; mRNA.
DR RefSeq; NP_523969.1; NM_079245.3.
DR AlphaFoldDB; O61613; -.
DR SMR; O61613; -.
DR BioGRID; 64329; 4.
DR IntAct; O61613; 4.
DR STRING; 7227.FBpp0076451; -.
DR PaxDb; O61613; -.
DR PRIDE; O61613; -.
DR DNASU; 38909; -.
DR EnsemblMetazoa; FBtr0076728; FBpp0076451; FBgn0020392.
DR GeneID; 38909; -.
DR KEGG; dme:Dmel_CG7436; -.
DR CTD; 38909; -.
DR FlyBase; FBgn0020392; Nmt.
DR VEuPathDB; VectorBase:FBgn0020392; -.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; O61613; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; O61613; -.
DR Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 38909; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38909; -.
DR PRO; PR:O61613; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020392; Expressed in secondary oocyte and 29 other tissues.
DR Genevisible; O61613; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IDA:FlyBase.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IBA:GO_Central.
DR GO; GO:0006499; P:N-terminal protein myristoylation; IDA:FlyBase.
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; Membrane; Reference proteome; Transferase.
FT CHAIN 1..472
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064228"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 94
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 223
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 224
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 225
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 226
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 232
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 234
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 235
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 236
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT CONFLICT 130
FT /note="Missing (in Ref. 1; AAC08578)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="T -> S (in Ref. 1; AAC08578)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="N -> G (in Ref. 1; AAC08578)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..472
FT /note="EIALILM -> RLL (in Ref. 1; AAC08578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 53833 MW; 21A0961A9127A7FA CRC64;
MPNENAEDLS GQELKQKAKE VADASEAMLE KVVAGLNIQD TASTNAAGNE DAEQPDGAKN
EASVSANASK QALLQAVSDA MASTRQMAKK FAFWSTQPVT KLDEQVTTNE CIEPNKEISE
IRALPYTLPG GFKWVTLDLN DANDLKELYT LLNENYVEDD DAMFRFDYQP EFLKWSLQPP
GWKRDWHVGV RVEKSGKLVG FISAIPSKLK SYDKVLKVVD INFLCVHKKL RSKRVAPVLI
REITRRVNLT GIFQAAYTAG VVLPTPVATC RYWHRSLNPK KLVDVRFSHL ARNMTMQRTM
KLYKLPDQPK TKGYRRITAK DMDKAHKLLE DYLKRFQLSP VFSKEEFRHW FTPKEGIIDC
FVVADEKGNI TDLTSYYCLP SSVMHHPVHK TVRAAYSFYN VSTKTPWLDL MNDALISARN
VQMDVYNALD LMENKKYFAP LKFGAGDGNL QYYLYNWRCP SMQPEEIALI LM
