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NTAN1

Gene
NTAN1
Protein
Protein N-terminal asparagine amidohydrolase
Organism
Arabidopsis thaliana
Length
347 amino acids
Function
N-terminal asparagine deamidase that mediates 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 NTAN1 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 (By similarity). Does not seems to be involved in immune response, unlike the N-terminal glutamine amidohydrolase NTAQ1 (PubMed:30117535).
Mass
39.174 kDa
Sequence
MIYVGGVQFLDESSSFSLSSSSQGSSLLVDVMSHPVITLASDSFKNLEEKNVSFDESDSESSTKDRYVYIFQREFAVVNPALVDFVGTDEATTCVGLVIRNRKSGMTSVAHMDSPEIVDLGISQMLLLVLQDDVDAELDVHMVGGYEDVDIKNADGVGDYAKPEGYSFPLCCKLVETLQKRRENFHIQTLFILGHNTKLDSQANTCPIFNGCLVNTSTGAILPASFNRTSRCPDEIVRRIRVSSSFEDSSWKGKLLDTYDTKTDRFIIAPCRWTMRLIEYVWELNQLTDEEILTNCSTSPSAEGPDFVNSLRRNWGYLLKYPEWSKTFPRRQPRVFERTVDGHWKKC

Gene
NTAN1
Protein
Protein N-terminal asparagine amidohydrolase
Organism
Sus scrofa
Length
311 amino acids
Function
N-terminal asparagine deamidase that mediates 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 NTAN1/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.
Mass
34.89 kDa
Sequence
MPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSVCILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVSLIMSSIKSFSDHTQRGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPIIYGIAVNVKTAEIYRASFPDRGPEEELRAARVLTGGPMISIYDAKTEQLRIGPYSWMPFPHVDFWLQQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKYPSPTNTLFPGNKALLYKKNEDGLWKEISSGGET

Gene
NTAN1
Protein
Protein N-terminal asparagine amidohydrolase
Organism
Homo sapiens
Length
310 amino acids
Function
N-terminal asparagine deamidase that mediates 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 NTAN1/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, nor on acetylated N-terminal peptidyl Asn.
Mass
34.677 kDa
Sequence
MPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQDRGPEEQLRAARTLAGGPMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEKISSPGS

Gene
Ntan1
Protein
Protein N-terminal asparagine amidohydrolase
Organism
Mus musculus
Length
310 amino acids
Function
N-terminal asparagine deamidase that mediates 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 NTAN1/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.
Mass
34.595 kDa
Sequence
MPLLVDGQRVRLPRSAVELVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGSDTKAEVPLIMSSIKSFSEHAECGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDKQDDDIHLVTLCVTELNDREENENHFPIIYGIAVNIKTAEIYRASFQDRGPEEQLRAARALAGGPMISIYDAKTEQLRIGPCSWTPFPQVDFWLQQDDKQILESLSTSPLAEPPHFVEHIRSTLMFLKKFPSPENILFPGNKALLYKKNKDGLWEKISSPGS