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Protein

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase

Gene

Aga

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

Catalytic activityi

N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei206NucleophileBy similarity1

GO - Molecular functioni

  • N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Source: MGI
  • peptidase activity Source: UniProtKB-KW

GO - Biological processi

  • protein deglycosylation Source: MGI
  • protein maturation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiT02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (EC:3.5.1.26)
Alternative name(s):
Aspartylglucosaminidase
Short name:
AGA
Glycosylasparaginase
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
Gene namesi
Name:Aga
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:104873. Aga.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000233524 – 205Glycosylasparaginase alpha chainAdd BLAST182
ChainiPRO_0000002336206 – 346Glycosylasparaginase beta chainAdd BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi64 ↔ 69By similarity
Disulfide bondi163 ↔ 179By similarity
Disulfide bondi286 ↔ 306By similarity
Glycosylationi310N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi317 ↔ 345By similarity

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ64191.
MaxQBiQ64191.
PaxDbiQ64191.
PeptideAtlasiQ64191.
PRIDEiQ64191.

PTM databases

PhosphoSitePlusiQ64191.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031521.
CleanExiMM_AGA.
ExpressionAtlasiQ64191. baseline and differential.
GenevisibleiQ64191. MM.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033920.

Structurei

3D structure databases

ProteinModelPortaliQ64191.
SMRiQ64191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni234 – 237Substrate bindingBy similarity4
Regioni257 – 260Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1593. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174614.
HOVERGENiHBG004289.
InParanoidiQ64191.
KOiK01444.
OMAiKFFGAVI.
OrthoDBiEOG091G0L36.
PhylomeDBiQ64191.
TreeFamiTF300756.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 2 hits.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64191-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERKSNLSLL LLLLVLGMPL VRGSSPLPLV VNTWPFKNAT EAAWWTLLSG
60 70 80 90 100
GSALDAVENG CAVCEKEQCD GTVGFGGSPD EGGETTLDAM IMDGTAMDVG
110 120 130 140 150
AVGGLRRIKN AIGVARRVLE HTTHTLLVGD SATKFAESMG FTNEDLSTKT
160 170 180 190 200
SRDLHSDWLS RNCQPNYWRN VIPDPSKYCG PYKPSGFLKQ SISPHKEEVD
210 220 230 240 250
IHSHDTIGMV VIHKTGHTAA GTSTNGIKFK IPGRVGDSPI PGAGAYADDT
260 270 280 290 300
AGAAAATGDG DTLLRFLPSY QAVEYMRGGD DPAIACQKVI LRIQKYYPNF
310 320 330 340
FGAVICASVN GSYGAACNKL PTFTQFSFMV SNSLHNEPTE KKVDCI
Length:346
Mass (Da):37,022
Last modified:November 1, 1997 - v1
Checksum:i75464327B740D10D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81393 mRNA. Translation: AAB36101.1.
CCDSiCCDS22304.1.
RefSeqiNP_001005847.1. NM_001005847.2.
UniGeneiMm.334535.

Genome annotation databases

EnsembliENSMUST00000033920; ENSMUSP00000033920; ENSMUSG00000031521.
GeneIDi11593.
KEGGimmu:11593.
UCSCiuc009lrz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81393 mRNA. Translation: AAB36101.1.
CCDSiCCDS22304.1.
RefSeqiNP_001005847.1. NM_001005847.2.
UniGeneiMm.334535.

3D structure databases

ProteinModelPortaliQ64191.
SMRiQ64191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033920.

Protein family/group databases

MEROPSiT02.001.

PTM databases

PhosphoSitePlusiQ64191.

Proteomic databases

EPDiQ64191.
MaxQBiQ64191.
PaxDbiQ64191.
PeptideAtlasiQ64191.
PRIDEiQ64191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033920; ENSMUSP00000033920; ENSMUSG00000031521.
GeneIDi11593.
KEGGimmu:11593.
UCSCiuc009lrz.2. mouse.

Organism-specific databases

CTDi175.
MGIiMGI:104873. Aga.

Phylogenomic databases

eggNOGiKOG1593. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174614.
HOVERGENiHBG004289.
InParanoidiQ64191.
KOiK01444.
OMAiKFFGAVI.
OrthoDBiEOG091G0L36.
PhylomeDBiQ64191.
TreeFamiTF300756.

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiQ64191.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031521.
CleanExiMM_AGA.
ExpressionAtlasiQ64191. baseline and differential.
GenevisibleiQ64191. MM.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 2 hits.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiASPG_MOUSE
AccessioniPrimary (citable) accession number: Q64191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.