Q64191 (ASPG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Glycosylasparaginase alpha chain
2. Glycosylasparaginase beta chain

Gene names

Name:

Aga

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein deglycosylation Inferred from electronic annotation. Source: Compara protein maturation Inferred from direct assay Ref.1. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from direct assay Ref.1. Source: MGI peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 205	182	Glycosylasparaginase alpha chain		PRO_0000002335
	Chain	206 – 346	141	Glycosylasparaginase beta chain		PRO_0000002336
Regions
	Region	234 – 237	4	Substrate binding By similarity
	Region	257 – 260	4	Substrate binding By similarity
Sites
	Active site	206	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
	Disulfide bond	64 ↔ 69		By similarity
	Disulfide bond	163 ↔ 179		By similarity
	Disulfide bond	286 ↔ 306		By similarity
	Disulfide bond	317 ↔ 345		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q64191 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 75464327B740D10D	FASTA	346	37,022
	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

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.
IPI	IPI00131231.
RefSeq	NP_001005847.1. NM_001005847.2.
UniGene	Mm.334535.
3D structure databases
ProteinModelPortal	Q64191.
SMR	Q64191. Positions 25-184, 206-346.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000033920.
Protein family/group databases
MEROPS	T02.001.
PTM databases
PhosphoSite	Q64191.
Proteomic databases
PaxDb	Q64191.
PRIDE	Q64191.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033920; ENSMUSP00000033920; ENSMUSG00000031521.
GeneID	11593.
KEGG	mmu:11593.
Organism-specific databases
CTD	175.
MGI	MGI:104873. Aga.
Phylogenomic databases
eggNOG	COG1446.
GeneTree	ENSGT00530000063034.
HOGENOM	HOG000174614.
HOVERGEN	HBG004289.
InParanoid	Q64191.
KO	K01444.
OMA	EQCDGSV.
OrthoDB	EOG4K6G4H.
Gene expression databases
ArrayExpress	Q64191.
Bgee	Q64191.
CleanEx	MM_AGA.
Genevestigator	Q64191.
GermOnline	ENSMUSG00000031521. Mus musculus.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. PTHR10188. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	279104.
SOURCE	Search...

Entry information

Entry name

ASPG_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program