NMT2_DANRE
ID NMT2_DANRE Reviewed; 492 AA.
AC A7YT82; F1QBV9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 2 {ECO:0000250|UniProtKB:O60551};
DE EC=2.3.1.97 {ECO:0000250|UniProtKB:O60551};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 2 {ECO:0000250|UniProtKB:O60551};
DE Short=NMT 2 {ECO:0000250|UniProtKB:O60551};
DE AltName: Full=Peptide N-myristoyltransferase 2 {ECO:0000250|UniProtKB:O60551};
DE AltName: Full=Type II N-myristoyltransferase {ECO:0000250|UniProtKB:O60551};
GN Name=nmt2 {ECO:0000312|EMBL:AAI15324.1,
GN ECO:0000312|ZFIN:ZDB-GENE-030131-717};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI15324.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-492.
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2006) 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. {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:0000255}.
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; BX322614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115323; AAI15324.1; -; mRNA.
DR RefSeq; NP_001186683.1; NM_001199754.1.
DR AlphaFoldDB; A7YT82; -.
DR SMR; A7YT82; -.
DR STRING; 7955.ENSDARP00000024632; -.
DR PaxDb; A7YT82; -.
DR PeptideAtlas; A7YT82; -.
DR GeneID; 556483; -.
DR KEGG; dre:556483; -.
DR CTD; 9397; -.
DR ZFIN; ZDB-GENE-030131-717; nmt2.
DR eggNOG; KOG2779; Eukaryota.
DR InParanoid; A7YT82; -.
DR OMA; ILNVKSC; -.
DR OrthoDB; 1025421at2759; -.
DR Reactome; R-DRE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:A7YT82; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; Reference proteome; Transferase.
FT CHAIN 1..492
FT /note="Glycylpeptide N-tetradecanoyltransferase 2"
FT /id="PRO_0000413005"
FT REGION 1..77
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 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 116
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 244
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 246
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 254
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 255
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
FT BINDING 256
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:O60551"
SQ SEQUENCE 492 AA; 56347 MW; AABB27E3912E2907 CRC64;
MAEDSESAAS QQSLELDDQD TCGIDGDNEE ENEHMQGSPG GDLGAKKKKK KQKRKKEKPS
SGGTKSDSAS DSQEIKNPAI PMQKLQDIQR AMELLSTCQG PAKNIDEATK HKYQFWDTQP
VPKLNEVVTT HGPIEPDKEN IRQEPYSLPQ GFMWDTLDLS NAEVLKELYT LLNENYVEDD
DNMFRFDYSP NFLKWALRPP GWLPHWHCGV RVSSNKKLVG FISAIPADIH IYDTLKRMVE
INFLCVHKKL RSKRVAPVLI REITRRVNLE GIFQAVYTAG VVLPKPVSTC RYWHRSLNPR
KLVEVKFSHL SRNMTLQRTM KLYRLPDSTR TPGLRTMGDR DVKQVTALLQ KHLSQFHLRP
VMGEEEVKHW FLPQENIIDT FVVEGSGGML TDFISFYTLP STVMHHPLHK SLKAAYSFYN
VHTETPLIDL MNDALILAKL KGFDVFNALD LMDNKNFLEK LKFGIGDGNL QYYLYNWKCP
PMDPEKVGLV LQ
