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P31717 (NMT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycylpeptide N-tetradecanoyltransferase 1

EC=2.3.1.97
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase 1
Short name=NMT 1
Short name=Type I N-myristoyltransferase
Peptide N-myristoyltransferase 1
Gene names
Name:NMT1
Synonyms:NMT
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins.

Catalytic activity

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.

Subunit structure

May be associated with other proteins.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the NMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processN-terminal protein myristoylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycylpeptide N-tetradecanoyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Glycylpeptide N-tetradecanoyltransferase 1
PRO_0000064220

Regions

Compositional bias55 – 6713Poly-Lys

Amino acid modifications

Modified residue311Phosphoserine By similarity
Modified residue471Phosphoserine By similarity

Experimental info

Sequence conflict114 – 1152KR → AK AA sequence Ref.2
Sequence conflict1221T → V AA sequence Ref.2
Sequence conflict168 – 1692VL → LF AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P31717 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 701A5C0B3554B037

FASTA49756,919
        10         20         30         40         50         60 
MGDESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN DTGAKKKKKK 

        70         80         90        100        110        120 
QKKKKEKGSE TDSAQDQPVK MNSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW 

       130        140        150        160        170        180 
DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY TLPQGFTWDA LDLGDRGVLK ELYTLLNENY 

       190        200        210        220        230        240 
VEDDDNMFRF DYSPEFLLWA LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK 

       250        260        270        280        290        300 
KMVEINFLCV HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS 

       310        320        330        340        350        360 
LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP MEKKDIPVVH QLLSRYLKQF 

       370        380        390        400        410        420 
HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY 

       430        440        450        460        470        480 
SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNNLQYYLY 

       490 
NWKCPSMGAE KVGLVLQ 

« Hide

References

[1]"Bovine retina type I N-myristoyltransferase."
Rundle D.R., Alvarez R.A., Anderson R.E.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]"Purification and partial sequencing of myristoyl-CoA:protein N-myristoyltransferase from bovine brain."
McIlhinney R.A.J., McGlone K., Willis A.C.
Biochem. J. 290:405-410(1993) [PubMed: 8452528] [Abstract]
Cited for: PROTEIN SEQUENCE OF 95-104; 114-123; 168-191 AND 449-459.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF223384 mRNA. Translation: AAF31460.1.
IPIIPI00723270.
PIRS30363.
UniGeneBt.88362.

3D structure databases

ProteinModelPortalP31717.
SMRP31717. Positions 155-497.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG13900.
HOVERGENHBG003404.
InParanoidP31717.
OrthoDBEOG4C5CJ6.
PhylomeDBP31717.

Enzyme and pathway databases

BRENDA2.3.1.97. 908.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.
PANTHERPTHR11377. Myristoyl_trans. 1 hit.
PfamPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 2 hits.
PROSITEPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNMT1_BOVIN
AccessionPrimary (citable) accession number: P31717
Secondary accession number(s): Q9N177
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 11, 2001
Last modified: November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families