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Reviewed, UniProtKB/Swiss-Prot Q64311 (NTAN1_MOUSE)

Last modified June 16, 2009. Version 50. 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:
    Protein N-terminal asparagine amidohydrolase
    EC=3.5.1.-
Alternative name(s):
    Protein NH2-terminal asparagine deamidase
      Short name=PNAD
      Short name=N-terminal Asn amidase
      Short name=NTN-amidase
    Protein NH2-terminal asparagine amidohydrolase
      Short name=PNAA
Gene names
Name: Ntan1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processadult locomotory behavior

Inferred from mutant phenotype. Source: MGI

memory

Inferred from mutant phenotype. Source: MGI

   Cellular componentcytoplasm

Inferred from direct assay. Source: MGI

nucleus

Inferred from direct assay. Source: MGI

   Molecular functionprotein N-terminal asparagine amidohydrolase activity Ref.1

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 310309Protein N-terminal asparagine amidohydrolase
PRO_0000057972

Sequences

Sequence LengthMass (Da)Tools
Q64311-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 09B1611DF3366959

FASTA31034,595
        10         20         30         40         50         60 
MPLLVDGQRV RLPRSAVELV RAHPPLEERA RLLRGQSVQQ VGPQGLLYVQ QRELAVTSPK 

        70         80         90        100        110        120 
DGSISILGSD DATTCHIVVL RHTGNGATCL THCDGSDTKA EVPLIMSSIK SFSEHAECGR 

       130        140        150        160        170        180 
LEVHLVGGFS DDRQLSQKLT HQLLSEFDKQ DDDIHLVTLC VTELNDREEN ENHFPIIYGI 

       190        200        210        220        230        240 
AVNIKTAEIY RASFQDRGPE EQLRAARALA GGPMISIYDA KTEQLRIGPC SWTPFPQVDF 

       250        260        270        280        290        300 
WLQQDDKQIL ESLSTSPLAE PPHFVEHIRS TLMFLKKFPS PENILFPGNK ALLYKKNKDG 

       310 
LWEKISSPGS 

« Hide

References

« Hide 'large scale' references
[1]"A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway."
Grigoryev S., Stewart A.E., Kwon Y.T., Arfin S.M., Bradshaw R.A., Jenkins N.A., Copeland N.G., Varshavsky A.
J. Biol. Chem. 271:28521-28532(1996) [PubMed: 8910481] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: C129.
[2]"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].
Strain: Czech II.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

U57692 mRNA. Translation: AAB66490.1.
U57691 Genomic DNA. Translation: AAC52885.1.
BC030172 mRNA. Translation: AAH30172.1.
IPIIPI00224124.
RefSeqNP_035076.1.
UniGeneMm.380410

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000022681. Mus musculus. [Contig view]
GeneID18203.
KEGGmmu:18203.

Organism-specific databases

MGIMGI:108471. Ntan1.

Phylogenomic databases

HOGENOMQ64311.
HOVERGENQ64311.
OMAQ64311. GNKALLY.

Gene expression databases

ArrayExpressQ64311.
BgeeQ64311.
CleanExMM_NTAN1.
GermOnlineENSMUSG00000022681. Mus musculus.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio293578.
SOURCESearch...

Entry information

Entry nameNTAN1_MOUSE
AccessionPrimary (citable) accession number: Q64311
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 50 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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