B3N6Y7 (ASPG1_DROER) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GG24090
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

ORF Names:

GG24090

Organism

Drosophila erecta (Fruit fly) [Complete proteome]

Taxonomic identifier

7220 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins By similarity. UniProtKB P20933
Catalytic activity	N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. UniProtKB P20933
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity. UniProtKB P20933
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
Domain	Signal
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein deglycosylation Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	lysosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – 245	222	Glycosylasparaginase alpha chain UniProtKB P20933		PRO_0000384125
	Chain	246 – 396	151	Glycosylasparaginase beta chain UniProtKB P20933		PRO_0000384126
Regions
	Region	274 – 277	4	Substrate binding By similarity
	Region	297 – 300	4	Substrate binding By similarity
Sites
	Active site	246	1	Nucleophile By similarity UniProtKB P20933
Amino acid modifications
	Disulfide bond	100 ↔ 105		By similarity UniProtKB P20933
	Disulfide bond	199 ↔ 215		By similarity UniProtKB P20933
	Disulfide bond	357 ↔ 384		By similarity UniProtKB P20933

Sequences

	Sequence		Length	Mass (Da)
	B3N6Y7 [UniParc]. Last modified September 2, 2008. Version 1. Checksum: BA2B302D0BD7D81C	FASTA	396	42,549
	10 20 30 40 50 60 MKRHLGTCLW VLCLASTAFS SLAVTTSPKP TLASAFSGKS KTTAGTTAVK ANKTTVELLP 70 80 90 100 110 120 MVINTWKFTA ANVLAWRILK QSKGGLRQTR NAVVEGCSKC EKLQCDRTVG YGGSPDELGE 130 140 150 160 170 180 TTLDAMVMDG ATMDVGAVAG LRRIKDAIKV ARHVLEHTQH TMLVGDAASA FANAMGFESE 190 200 210 220 230 240 SLITPESKDM WLQWTAENCQ PNFWKNVHPD PKVSCGPYKP RPTPLTRWKE DRARNEYEIG 250 260 270 280 290 300 RKNHDTIGMI AIDVESNIHA GTSTNGARHK IPGRVGDSPI PGAGAYADNE VGAAVATGDG 310 320 330 340 350 360 DVMMRFLPSL LAVEAMRAGK PPAEAAQEGL RRILKYHKDF MGALIAVDRL GNYAAACYGL 370 380 390 DEFPFMVSSP AGTDGPTRLE TVKCIAGQDK VNVVSL

References

[1]	"Evolution of genes and genomes on the Drosophila phylogeny." Drosophila 12 genomes consortium Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tucson 14021-0224.01.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH954177 Genomic DNA. Translation: EDV58236.1.
RefSeq	XP_001969177.1. XM_001969141.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0144144; FBpp0142636; FBgn0116229.
GeneID	6541640.
KEGG	der:Dere_GG24090.
Organism-specific databases
FlyBase	FBgn0116229. Dere\GG24090.
Phylogenomic databases
KO	K01444.
OrthoDB	EOG44MW7V.
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...

Entry information

Entry name

ASPG1_DROER

Accession

Primary (citable) accession number: B3N6Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	September 2, 2008
Last modified:	February 6, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project