O02467 (ASPG_SPOFR) 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: Glycosylasparaginase alpha chain Glycosylasparaginase beta chain
Organism	Spodoptera frugiperda (Fall armyworm)
Taxonomic identifier	7108 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Noctuoidea › Noctuidae › Amphipyrinae › Spodoptera

Protein attributes

Sequence length	320 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 or heterodimer of an alpha and a beta chain.
Subcellular location	Lysosome.
Post-translational modification	Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity Probable.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Cellular component	Lysosome
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 183	183	Glycosylasparaginase alpha chain		PRO_0000002345
	Chain	184 – 320	137	Glycosylasparaginase beta chain		PRO_0000002346
Sites
	Active site	184	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	15	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 46		By similarity
	Disulfide bond	141 ↔ 157		By similarity
	Disulfide bond	295 ↔ 320		By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	O02467 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: D0C57ACA6F2A6183	FASTA	320	34,841
	10 20 30 40 50 60 EKNMPIVITT WSFTNASQKA WEVLKDEGKA LDAVEQGGIV CENEQCDRTV GYGGSPDEDG 70 80 90 100 110 120 ETTLDAFIMD GSTMNVGAVA ALRRIKSAIS VARHVMEYTT HSFLAGELAT KFAVEMGFKE 130 140 150 160 170 180 ESLSTDESRE LWSKWRFEKQ CQPNFRKNVK PDPRKHCGPY HKKRNFVDYI HPEVFVVDQY 190 200 210 220 230 240 NHDTIGMVAV DSKGDVAAGT STNGAKFKIP GRVGDSPIPG AGAYADNTVG GAAATGNGDT 250 260 270 280 290 300 MMRFLPSFLA VEEMRRGASP ANAAKTAIKR ISAHHPDFMG AVIALSKNGQ YGAACNGIET 310 320 FPFVVQDKTR KTFEVVTIKC

References

[1]	"Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda." Liu Y., Dunn G.S., Aronson N.N. Jr. Glycobiology 6:527-536(1996) [PubMed: 8877373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S83425 mRNA. Translation: AAB50885.2.
3D structure databases
ProteinModelPortal	O02467.
SMR	O02467. Positions 4-160, 184-301.
ModBase	Search...
Protein family/group databases
MEROPS	T02.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPG_SPOFR

Accession

Primary (citable) accession number: O02467

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	May 31, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)