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Reviewed, UniProtKB/Swiss-Prot P50297 (ARY1_RAT)

Last modified January 19, 2010. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arylamine N-acetyltransferase 1
    EC=2.3.1.5
Alternative name(s):
    Arylamide acetylase 1
    N-acetyltransferase type 1
      Short name=NAT-1
      Short name=AT-1
Gene names
Name: Nat1
Synonyms: Aac1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Acetylates both arylamines and arylalkylamines.

Catalytic activity

Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the arylamine N-acetyltransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processliver development

Inferred from expression pattern. Source: RGD

metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarylamine N-acetyltransferase activity

Inferred from direct assay. Source: RGD

translation repressor activity

Traceable author statement. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 290290Arylamine N-acetyltransferase 1
PRO_0000107911

Regions

Region106 – 1072Substrate binding By similarity

Sites

Active site681Acyl-thioester intermediate By similarity
Active site1071 By similarity
Active site1221 By similarity
Binding site1031Coenzyme A By similarity
Binding site2081Coenzyme A By similarity

Sequences

Sequence LengthMass (Da)Tools
P50297-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2897CC1F84B7D72A

FASTA29033,437
        10         20         30         40         50         60 
MDIEAYFERI GYKNSVNKLD LATLTEVLQH QMRAVPFENL SMHCGEAMCL GLEATFDHIV 

        70         80         90        100        110        120 
RKKRGGWCLQ VNHLLYWALT KMGFETTMLG GYVYITPVNK YSSEMVHLLV QVTISDRNYI 

       130        140        150        160        170        180 
VDSAYGSSYQ MWEPLELTSG KDQPQVPAIF RLTEENGTWY LDQIRREQDV PNQEFVNSDL 

       190        200        210        220        230        240 
LEKSKYRKIY SFTLEPRTIE DFEYVNTYLQ TSPASVFVST SFCSLQTSEG VCCLIGSTLT 

       250        260        270        280        290 
SRRFSYKDNV DLVEFKSLTE EEIEDVLKTT FGISLEKKFV PKHGELVFTI 

« Hide

References

« Hide 'large scale' references
[1]"Complementary DNAs for two arylamine N-acetyltransferases with identical 5' non-coding regions from rat pineal gland."
Ebisawa T., Sasaki Y., Deguchi T.
Eur. J. Biochem. 228:129-137(1995) [PubMed: 7882993] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Pineal gland.
[2]"Recombinant rat and hamster acetyltransferases-1 and -2: relative rates of N-acetylation of arylamines and N,O-acyltransfer with arylhydroxamic acids."
Jones R.F., Gott B., Land S.J., Park J., King C.M.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01344 mRNA. Translation: AAA70157.1.
U01343 mRNA. Translation: AAA70156.1.
U17260 mRNA. Translation: AAA56771.1.
U01345 mRNA. Translation: AAA70158.1.
BC078765 mRNA. Translation: AAH78765.1.
IPIIPI00196630.
PIRI67465.
RefSeqNP_001032392.1.
NP_001032393.1.
NP_446305.1.
UniGeneRn.37420

3D structure databases

SMRP50297. Positions 2-290.
ModBaseSearch...

Protein-protein interaction databases

STRINGP50297.

PTM databases

PhosphoSiteP50297.

Genome annotation databases

EnsemblENSRNOT00000018854; ENSRNOP00000018854; ENSRNOG00000014055; Rattus norvegicus. [Genome view]
GeneID116631.
KEGGrno:116631.
UCSCNM_053853. rat.

Organism-specific databases

CTD116631.
RGD70490. Nat1.

Phylogenomic databases

eggNOGroNOG04860.
HOVERGENP50297.
OMAAIFDHIV.
PhylomeDBP50297.

Enzyme and pathway databases

BRENDA2.3.1.5. 248.
2.3.1.56. 248.

Gene expression databases

ArrayExpressP50297.
GenevestigatorP50297.
GermOnlineENSRNOG00000014055. Rattus norvegicus.

Family and domain databases

InterProIPR001447. N-AcTrfase.
[Graphical view]
PANTHERPTHR11786. Acetyltransf2. 1 hit.
PfamPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSPR01543. ANATRNSFRASE.
ProtoNetSearch...

Other Resources

NextBio619321.

Entry information

Entry nameARY1_RAT
AccessionPrimary (citable) accession number: P50297
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 19, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents