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Q64191 (ASPG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
Gene names
Name:Aga
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

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

Subcellular location

Lysosome.

Post-translational modification

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.

Sequence similarities

Belongs to the Ntn-hydrolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 205182Glycosylasparaginase alpha chain
PRO_0000002335
Chain206 – 346141Glycosylasparaginase beta chain
PRO_0000002336

Regions

Region234 – 2374Substrate binding By similarity
Region257 – 2604Substrate binding By similarity

Sites

Active site2061Nucleophile By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 69 By similarity
Disulfide bond163 ↔ 179 By similarity
Disulfide bond286 ↔ 306 By similarity
Disulfide bond317 ↔ 345 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64191 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 75464327B740D10D

FASTA34637,022
        10         20         30         40         50         60 
MERKSNLSLL LLLLVLGMPL VRGSSPLPLV VNTWPFKNAT EAAWWTLLSG GSALDAVENG 

        70         80         90        100        110        120 
CAVCEKEQCD GTVGFGGSPD EGGETTLDAM IMDGTAMDVG AVGGLRRIKN AIGVARRVLE 

       130        140        150        160        170        180 
HTTHTLLVGD SATKFAESMG FTNEDLSTKT SRDLHSDWLS RNCQPNYWRN VIPDPSKYCG 

       190        200        210        220        230        240 
PYKPSGFLKQ SISPHKEEVD IHSHDTIGMV VIHKTGHTAA GTSTNGIKFK IPGRVGDSPI 

       250        260        270        280        290        300 
PGAGAYADDT AGAAAATGDG DTLLRFLPSY QAVEYMRGGD DPAIACQKVI LRIQKYYPNF 

       310        320        330        340 
FGAVICASVN GSYGAACNKL PTFTQFSFMV SNSLHNEPTE KKVDCI 

« Hide

References

[1]"Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene."
Tenhunen K., Laan M., Manninen T., Palotie A., Peltonen L., Jalanko A.
Genomics 30:244-250(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S81393 mRNA. Translation: AAB36101.1.
IPIIPI00131231.
RefSeqNP_001005847.1. NM_001005847.2.
UniGeneMm.334535.

3D structure databases

ProteinModelPortalQ64191.
SMRQ64191. Positions 25-184, 206-346.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033920.

Protein family/group databases

MEROPST02.001.

PTM databases

PhosphoSiteQ64191.

Proteomic databases

PaxDbQ64191.
PRIDEQ64191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033920; ENSMUSP00000033920; ENSMUSG00000031521.
GeneID11593.
KEGGmmu:11593.

Organism-specific databases

CTD175.
MGIMGI:104873. Aga.

Phylogenomic databases

eggNOGCOG1446.
GeneTreeENSGT00530000063034.
HOGENOMHOG000174614.
HOVERGENHBG004289.
InParanoidQ64191.
KOK01444.
OMAEQCDGSV.
OrthoDBEOG4K6G4H.

Gene expression databases

ArrayExpressQ64191.
BgeeQ64191.
CleanExMM_AGA.
GenevestigatorQ64191.
GermOnlineENSMUSG00000031521. Mus musculus.

Family and domain databases

InterProIPR000246. Peptidase_T2.
[Graphical view]
PANTHERPTHR10188. PTHR10188. 1 hit.
PfamPF01112. Asparaginase_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279104.
SOURCESearch...

Entry information

Entry nameASPG_MOUSE
AccessionPrimary (citable) accession number: Q64191
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families