NameN(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
Synonyms
  • 3.5.1.26
  • Aspartylglucosaminidase
  • Glycosylasparaginase
  • N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Gene NameAGA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0013740|N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
MARKSNLPVLLVPFLLCQALVRCSSPLPLVVNTWPFKNATEAAWRALASGGSALDAVESG
CAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLE
HTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCG
PYKPPGILKQDIPIHKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPI
PGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEF
FGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI
Number of residues346
Molecular Weight37207.955
Theoretical pINot Available
GO Classification
Functions
  • N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
  • peptidase activity
Processes
  • protein deglycosylation
  • protein maturation
Components
  • extracellular space
  • lysosome
  • extracellular exosome
  • endoplasmic reticulum
General FunctionPeptidase activity
Specific FunctionCleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP20933
UniProtKB Entry NameASPG_HUMAN
Cellular LocationLysosome
Gene sequence
>lcl|BSEQ0013741|N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (AGA)
ATGGCGCGGAAGTCGAACTTGCCTGTGCTTCTCGTGCCGTTTCTGCTCTGCCAGGCCCTA
GTGCGCTGCTCCAGCCCTCTGCCCCTGGTCGTCAACACTTGGCCCTTTAAGAATGCAACC
GAAGCAGCGTGGAGGGCATTAGCATCTGGAGGCTCTGCCCTGGATGCAGTGGAGAGCGGC
TGTGCCATGTGTGAGAGAGAGCAGTGTGACGGCTCTGTAGGCTTTGGAGGAAGTCCTGAT
GAACTTGGAGAAACCACACTAGATGCCATGATCATGGATGGCACTACTATGGATGTAGGA
GCAGTAGGAGATCTCAGACGAATTAAAAATGCTATTGGTGTGGCACGGAAAGTACTGGAA
CATACAACACACACACTTTTAGTAGGAGAGTCAGCCACCACATTTGCTCAAAGTATGGGG
TTTATCAATGAAGACTTATCTACCACTGCTTCTCAAGCTCTTCATTCAGATTGGCTTGCT
CGGAATTGCCAGCCAAATTATTGGAGGAATGTTATACCAGATCCCTCAAAATACTGCGGA
CCCTACAAACCACCTGGTATCTTAAAGCAGGATATTCCTATCCATAAAGAAACAGAAGAT
GATCGTGGTCATGACACTATTGGCATGGTTGTAATCCATAAGACAGGACATATTGCTGCT
GGTACATCTACAAATGGTATAAAATTCAAAATACATGGCCGTGTAGGAGACTCACCAATA
CCTGGAGCTGGAGCCTATGCTGACGATACTGCAGGGGCAGCCGCAGCCACTGGGAATGGT
GATATATTGATGCGCTTCCTGCCAAGCTACCAAGCTGTAGAATACATGAGAAGAGGAGAA
GATCCAACCATAGCTTGCCAAAAAGTGATTTCAAGAATCCAGAAGCATTTTCCAGAATTC
TTTGGGGCTGTTATATGTGCCAATGTGACTGGAAGTTACGGTGCTGCTTGCAATAAACTT
TCAACATTTACTCAGTTTAGTTTCATGGTTTATAATTCCGAAAAAAATCAGCCAACTGAG
GAAAAAGTGGACTGCATCTAA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:318
Chromosome Location4
LocusNot Available
References
  1. Fisher KJ, Tollersrud OK, Aronson NN Jr: Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase. FEBS Lett. 1990 Sep 3;269(2):440-4. 2401370
  2. Fisher KJ, Tollersrud OK, Aronson NN Jr: Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase. FEBS Lett. 1990 Dec 10;276(1-2):232. 2265705
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  5. Fisher KJ, Aronson NN Jr: Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits. J Biol Chem. 1991 Jun 25;266(18):12105-13. 1904874
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